RNA pseudouridylation: new insights into an old modification
Pseudouridine is the most abundant post-transcriptionally modified nucleotide in various stable RNAs of all organisms. Pseudouridine is derived from uridine via base-specific isomerization, resulting in an extra hydrogen-bond donor that distinguishes it from other nucleotides. In eukaryotes, uridine...
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| Published in | Trends in biochemical sciences (Amsterdam. Regular ed.) Vol. 38; no. 4; pp. 210 - 218 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
England
Elsevier Ltd
01.04.2013
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| Abstract | Pseudouridine is the most abundant post-transcriptionally modified nucleotide in various stable RNAs of all organisms. Pseudouridine is derived from uridine via base-specific isomerization, resulting in an extra hydrogen-bond donor that distinguishes it from other nucleotides. In eukaryotes, uridine-to-pseudouridine isomerization is catalyzed primarily by box H/ACA RNPs, ribonucleoproteins that act as pseudouridylases. When introduced into RNA, pseudouridine contributes significantly to RNA-mediated cellular processes. It was recently discovered that pseudouridylation can be induced by stress, suggesting a regulatory role for pseudouridine. It has also been reported that pseudouridine can be artificially introduced into mRNA by box H/ACA RNPs and that such introduction can mediate nonsense-to-sense codon conversion, thus demonstrating a new means of generating coding or protein diversity. |
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| AbstractList | Pseudouridine is the most abundant post-transcriptionally modified nucleotide in various stable RNAs of all organisms. Pseudouridine is derived from uridine via base-specific isomerization, resulting in an extra hydrogen-bond donor that distinguishes it from other nucleotides. In eukaryotes, uridine-to-pseudouridine isomerization is catalyzed primarily by box H/ACA RNPs, ribonucleoproteins that act as pseudouridylases. When introduced into RNA, pseudouridine contributes significantly to RNA-mediated cellular processes. It was recently discovered that pseudouridylation can be induced by stress, suggesting a regulatory role for pseudouridine. It has also been reported that pseudouridine can be artificially introduced into mRNA by box H/ACA RNPs and that such introduction can mediate nonsense-to-sense codon conversion, thus demonstrating a new means of generating coding or protein diversity. Pseudouridine is the most abundant posttranscriptionally modified nucleotide in various stable RNAs of all organisms. Pseudouridine is derived from uridine via base-specific isomerization, resulting in an extra hydrogen bond donor that distinguishes it from other nucleotides. In eukaryotes, uridine-to-pseudouridine isomerization is catalyzed primarily by box H/ACA RNPs, ribonucleoproteins that act as pseudouridylases. When introduced into RNA, pseudouridine contributes significantly to RNA-mediated cellular processes. It was recently discovered that pseudouridylation can be induced by stress, suggesting a regulatory role for pseudouridine. It has also been reported that pseudouridine can be artificially introduced into mRNA by box H/ACA RNPs and that such introduction can mediate nonsense-to-sense codon conversion, thus demonstrating a new means of generating coding/protein diversity. Pseudouridine is the most abundant post-transcriptionally modified nucleotide in various stable RNAs of all organisms. Pseudouridine is derived from uridine via base-specific isomerization, resulting in an extra hydrogen-bond donor that distinguishes it from other nucleotides. In eukaryotes, uridine-to-pseudouridine isomerization is catalyzed primarily by box H/ACA RNPs, ribonucleoproteins that act as pseudouridylases. When introduced into RNA, pseudouridine contributes significantly to RNA-mediated cellular processes. It was recently discovered that pseudouridylation can be induced by stress, suggesting a regulatory role for pseudouridine. It has also been reported that pseudouridine can be artificially introduced into mRNA by box H/ACA RNPs and that such introduction can mediate nonsense-to-sense codon conversion, thus demonstrating a new means of generating coding or protein diversity.Pseudouridine is the most abundant post-transcriptionally modified nucleotide in various stable RNAs of all organisms. Pseudouridine is derived from uridine via base-specific isomerization, resulting in an extra hydrogen-bond donor that distinguishes it from other nucleotides. In eukaryotes, uridine-to-pseudouridine isomerization is catalyzed primarily by box H/ACA RNPs, ribonucleoproteins that act as pseudouridylases. When introduced into RNA, pseudouridine contributes significantly to RNA-mediated cellular processes. It was recently discovered that pseudouridylation can be induced by stress, suggesting a regulatory role for pseudouridine. It has also been reported that pseudouridine can be artificially introduced into mRNA by box H/ACA RNPs and that such introduction can mediate nonsense-to-sense codon conversion, thus demonstrating a new means of generating coding or protein diversity. |
| Author | Yu, Yi-Tao Ge, Junhui |
| Author_xml | – sequence: 1 givenname: Junhui surname: Ge fullname: Ge, Junhui – sequence: 2 givenname: Yi-Tao surname: Yu fullname: Yu, Yi-Tao email: yitao_yu@urmc.rochester.edu |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/23391857$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1038/nsmb1336 10.1261/rna.5520403 10.1093/genetics/133.4.851 10.1016/S0092-8674(00)80263-9 10.1093/emboj/17.23.7078 10.1093/emboj/18.18.5120 10.1007/s13238-011-1087-1 10.1093/nar/gkp816 10.1016/j.molcel.2007.10.012 10.1101/gad.12.4.527 10.1016/S0092-8674(00)80238-X 10.4161/nucl.2.1.14437 10.1093/nar/29.13.2733 10.1074/jbc.M413288200 10.1016/S0079-6603(08)60629-7 10.1261/rna.2210406 10.1038/emboj.2010.323 10.1093/nar/gkn710 10.1016/S0021-9258(18)70770-9 10.1093/nar/gki630 10.1093/nar/9.17.4303 10.1261/rna.031385.111 10.1128/MCB.00531-10 10.1002/wrna.77 10.1016/S0092-8674(00)80156-7 10.1261/rna.1361509 10.1261/rna.031351.111 10.1261/rna.5440303 10.1038/emboj.2010.316 10.1016/0300-9084(96)88117-X 10.1093/emboj/cdg191 10.1016/j.clinbiochem.2006.11.021 10.1016/j.molcel.2011.09.017 10.1080/152165400410182 10.1038/nature10165 10.1073/pnas.0810953105 10.1016/S0968-0004(02)02109-6 10.1261/rna.7186504 10.1017/S1355838201002308 10.1021/bi7022392 10.1093/nar/gkq1028 10.1016/j.molcel.2005.11.017 10.1038/nsmb.1624 10.1038/mt.2008.200 10.1128/MCB.19.3.2142 10.1093/emboj/17.19.5783 10.1016/S1367-5931(02)00397-6 10.1126/science.1165357 10.1093/emboj/cdg394 10.1261/rna.5159504 10.1093/nar/23.24.5020 10.1038/nature05151 10.1101/gad.1309605 10.1016/j.molcel.2009.02.020 10.1093/nar/gkj482 10.1128/MCB.19.11.7461 10.1093/nar/gkq347 10.1038/sj.emboj.7600718 10.1073/pnas.0701534104 10.1261/rna.5240503 10.1093/emboj/16.15.4770 10.1038/167483a0 10.1006/excr.1996.0372 10.1038/nsmb1036 10.1073/pnas.202477199 10.1091/mbc.10.11.3877 10.1038/nsb873 10.1101/gad.197467.112 10.1101/gad.1049103 10.1038/ng0598-32 10.1093/emboj/18.2.457 10.1016/j.molcel.2009.05.005 10.1093/hmg/ddp416 10.1021/bi00190a008 10.1074/jbc.M803049200 10.1093/emboj/20.3.541 10.1093/nar/26.1.148 10.1093/nar/gki366 10.1261/rna.1724409 10.1016/j.molcel.2007.03.014 10.1093/emboj/20.11.2943 10.1016/S1097-2765(03)00040-6 10.1093/nar/27.7.1683 10.1038/mt.2012.7 10.1017/S1355838202022537 10.1093/nar/gkh768 |
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| References | Grosjean (bib0040) 1995; 77 King (bib0340) 2003; 11 Kariko (bib0465) 2008; 16 Sprinzl (bib0045) 1998; 26 Newby, Greenbaum (bib0160) 2002; 99 Maden (bib0065) 1990; 39 Ni (bib0100) 1997; 89 Ma (bib0135) 2003; 22 Schattner (bib0200) 2004; 32 Tomita (bib0450) 1999; 27 Ganot (bib0105) 1997; 89 Charette, Gray (bib0165) 2000; 49 Lange (bib0280) 1999; 10 Ofengand, Fournier (bib0060) 1998 Yu (bib0215) 1996; 229 Yu (bib0090) 2011; 2 Xiao (bib0110) 2009; 15 Jin (bib0290) 2007; 26 Liang (bib0325) 2009; 16 Henras (bib0255) 2001; 29 Valadkhan, Manley (bib0400) 2003; 9 Zebarjadian (bib0265) 1999; 19 Bortolin (bib0285) 1999; 18 Liang (bib0330) 2007; 14 Narayanan (bib0275) 1999; 18 Newby, Greenbaum (bib0155) 2001; 7 Korostelev (bib0435) 2008; 105 Piekna-Przybylska (bib0360) 2008; 283 Heiss (bib0180) 1998; 19 Bernick (bib0190) 2012; 18 Grosjean (bib0015) 2009 Lee (bib0170) 2007; 40 Wu, Feigon (bib0295) 2007; 104 Badis (bib0365) 2003; 9 Yang (bib0390) 2005; 280 Wu (bib0405) 2011; 30 Jack (bib0370) 2011; 44 Yu (bib0085) 2005 Lin, Kielkopf (bib0395) 2008; 47 Meier (bib0410) 2011; 30 Cohn, Volkin (bib0020) 1951; 167 Manival (bib0310) 2006; 34 Lafontaine (bib0270) 1998; 12 Ma (bib0125) 2005; 24 Duan (bib0320) 2009; 34 Zhao, Yu (bib0375) 2004; 10 Bjork (bib0035) 1995 Karijolich, Yu (bib0420) 2011; 474 Decatur, Fournier (bib0335) 2002; 27 Grozdanov (bib0175) 2009; 18 Zhao (bib0220) 2002; 8 Reddy, Busch (bib0075) 1988 Schattner (bib0195) 2005; 33 Liang (bib0355) 2007; 28 Massenet (bib0130) 1999; 19 Henras (bib0260) 1998; 17 Chen (bib0425) 2010; 30 Donmez (bib0385) 2004; 10 Tycowski (bib0240) 2009; 34 Cantara (bib0005) 2011; 39 Lane (bib0030) 1998 Hopper, Phizicky (bib0050) 2003; 17 Branlant (bib0055) 1981; 9 Jady, Kiss (bib0225) 2001; 20 Czerwoniec (bib0010) 2009; 37 Massenet (bib0080) 1998 Balakin (bib0185) 1996; 86 Huttenhofer (bib0210) 2001; 20 Yu (bib0380) 1998; 17 Charpentier (bib0120) 2005; 33 Wu (bib0095) 2011; 2 Richard (bib0230) 2003; 22 Liang (bib0350) 2009; 15 Kariko (bib0455) 2012; 20 Schattner (bib0070) 2006; 12 Huttenhofer (bib0205) 2002; 6 Rashid (bib0305) 2006; 21 Davis (bib0150) 1995; 23 Parisien (bib0445) 2012; 18 Westman, Lamond (bib0415) 2011; 2 Anderson (bib0460) 2010; 38 Davis, Allen (bib0025) 1957; 227 Behm-Ansmant (bib0245) 2003; 9 Lesser, Guthrie (bib0440) 1993; 133 Bousquet-Antonelli (bib0250) 1997; 16 Arnez, Steitz (bib0140) 1994; 33 Venteicher (bib0235) 2009; 323 Hamma (bib0300) 2005; 12 Newby, Greenbaum (bib0145) 2002; 9 Baudin-Baillieu (bib0345) 2009; 37 Baker (bib0115) 2005; 19 Li, Ye (bib0315) 2006; 443 Jady (bib0430) 2012; 26 Manival (10.1016/j.tibs.2013.01.002_bib0310) 2006; 34 Baker (10.1016/j.tibs.2013.01.002_bib0115) 2005; 19 Lin (10.1016/j.tibs.2013.01.002_bib0395) 2008; 47 Davis (10.1016/j.tibs.2013.01.002_bib0025) 1957; 227 Yu (10.1016/j.tibs.2013.01.002_bib0215) 1996; 229 Donmez (10.1016/j.tibs.2013.01.002_bib0385) 2004; 10 Hopper (10.1016/j.tibs.2013.01.002_bib0050) 2003; 17 Schattner (10.1016/j.tibs.2013.01.002_bib0200) 2004; 32 Piekna-Przybylska (10.1016/j.tibs.2013.01.002_bib0360) 2008; 283 Jack (10.1016/j.tibs.2013.01.002_bib0370) 2011; 44 Narayanan (10.1016/j.tibs.2013.01.002_bib0275) 1999; 18 Wu (10.1016/j.tibs.2013.01.002_bib0295) 2007; 104 Grozdanov (10.1016/j.tibs.2013.01.002_bib0175) 2009; 18 Liang (10.1016/j.tibs.2013.01.002_bib0355) 2007; 28 Liang (10.1016/j.tibs.2013.01.002_bib0350) 2009; 15 Massenet (10.1016/j.tibs.2013.01.002_bib0130) 1999; 19 Lee (10.1016/j.tibs.2013.01.002_bib0170) 2007; 40 Jin (10.1016/j.tibs.2013.01.002_bib0290) 2007; 26 Parisien (10.1016/j.tibs.2013.01.002_bib0445) 2012; 18 Wu (10.1016/j.tibs.2013.01.002_bib0095) 2011; 2 Hamma (10.1016/j.tibs.2013.01.002_bib0300) 2005; 12 Ofengand (10.1016/j.tibs.2013.01.002_bib0060) 1998 Huttenhofer (10.1016/j.tibs.2013.01.002_bib0210) 2001; 20 Chen (10.1016/j.tibs.2013.01.002_bib0425) 2010; 30 Arnez (10.1016/j.tibs.2013.01.002_bib0140) 1994; 33 Tycowski (10.1016/j.tibs.2013.01.002_bib0240) 2009; 34 Lesser (10.1016/j.tibs.2013.01.002_bib0440) 1993; 133 Baudin-Baillieu (10.1016/j.tibs.2013.01.002_bib0345) 2009; 37 Li (10.1016/j.tibs.2013.01.002_bib0315) 2006; 443 Yang (10.1016/j.tibs.2013.01.002_bib0390) 2005; 280 Yu (10.1016/j.tibs.2013.01.002_bib0090) 2011; 2 Lafontaine (10.1016/j.tibs.2013.01.002_bib0270) 1998; 12 Korostelev (10.1016/j.tibs.2013.01.002_bib0435) 2008; 105 Branlant (10.1016/j.tibs.2013.01.002_bib0055) 1981; 9 Bortolin (10.1016/j.tibs.2013.01.002_bib0285) 1999; 18 Balakin (10.1016/j.tibs.2013.01.002_bib0185) 1996; 86 Davis (10.1016/j.tibs.2013.01.002_bib0150) 1995; 23 Zhao (10.1016/j.tibs.2013.01.002_bib0220) 2002; 8 Wu (10.1016/j.tibs.2013.01.002_bib0405) 2011; 30 Grosjean (10.1016/j.tibs.2013.01.002_bib0015) 2009 Richard (10.1016/j.tibs.2013.01.002_bib0230) 2003; 22 Liang (10.1016/j.tibs.2013.01.002_bib0325) 2009; 16 Bousquet-Antonelli (10.1016/j.tibs.2013.01.002_bib0250) 1997; 16 Westman (10.1016/j.tibs.2013.01.002_bib0415) 2011; 2 Bjork (10.1016/j.tibs.2013.01.002_bib0035) 1995 Kariko (10.1016/j.tibs.2013.01.002_bib0465) 2008; 16 Jady (10.1016/j.tibs.2013.01.002_bib0430) 2012; 26 Yu (10.1016/j.tibs.2013.01.002_bib0085) 2005 Venteicher (10.1016/j.tibs.2013.01.002_bib0235) 2009; 323 Kariko (10.1016/j.tibs.2013.01.002_bib0455) 2012; 20 Cohn (10.1016/j.tibs.2013.01.002_bib0020) 1951; 167 Heiss (10.1016/j.tibs.2013.01.002_bib0180) 1998; 19 Newby (10.1016/j.tibs.2013.01.002_bib0155) 2001; 7 Rashid (10.1016/j.tibs.2013.01.002_bib0305) 2006; 21 Maden (10.1016/j.tibs.2013.01.002_bib0065) 1990; 39 Yu (10.1016/j.tibs.2013.01.002_bib0380) 1998; 17 Henras (10.1016/j.tibs.2013.01.002_bib0260) 1998; 17 Sprinzl (10.1016/j.tibs.2013.01.002_bib0045) 1998; 26 Massenet (10.1016/j.tibs.2013.01.002_bib0080) 1998 Ganot (10.1016/j.tibs.2013.01.002_bib0105) 1997; 89 Huttenhofer (10.1016/j.tibs.2013.01.002_bib0205) 2002; 6 Meier (10.1016/j.tibs.2013.01.002_bib0410) 2011; 30 Czerwoniec (10.1016/j.tibs.2013.01.002_bib0010) 2009; 37 Lange (10.1016/j.tibs.2013.01.002_bib0280) 1999; 10 Decatur (10.1016/j.tibs.2013.01.002_bib0335) 2002; 27 Tomita (10.1016/j.tibs.2013.01.002_bib0450) 1999; 27 Grosjean (10.1016/j.tibs.2013.01.002_bib0040) 1995; 77 Cantara (10.1016/j.tibs.2013.01.002_bib0005) 2011; 39 Ma (10.1016/j.tibs.2013.01.002_bib0135) 2003; 22 Newby (10.1016/j.tibs.2013.01.002_bib0145) 2002; 9 Bernick (10.1016/j.tibs.2013.01.002_bib0190) 2012; 18 Schattner (10.1016/j.tibs.2013.01.002_bib0195) 2005; 33 Behm-Ansmant (10.1016/j.tibs.2013.01.002_bib0245) 2003; 9 Badis (10.1016/j.tibs.2013.01.002_bib0365) 2003; 9 Newby (10.1016/j.tibs.2013.01.002_bib0160) 2002; 99 Xiao (10.1016/j.tibs.2013.01.002_bib0110) 2009; 15 Henras (10.1016/j.tibs.2013.01.002_bib0255) 2001; 29 Lane (10.1016/j.tibs.2013.01.002_bib0030) 1998 Charette (10.1016/j.tibs.2013.01.002_bib0165) 2000; 49 Zebarjadian (10.1016/j.tibs.2013.01.002_bib0265) 1999; 19 Zhao (10.1016/j.tibs.2013.01.002_bib0375) 2004; 10 Ma (10.1016/j.tibs.2013.01.002_bib0125) 2005; 24 Schattner (10.1016/j.tibs.2013.01.002_bib0070) 2006; 12 Anderson (10.1016/j.tibs.2013.01.002_bib0460) 2010; 38 Charpentier (10.1016/j.tibs.2013.01.002_bib0120) 2005; 33 Liang (10.1016/j.tibs.2013.01.002_bib0330) 2007; 14 Reddy (10.1016/j.tibs.2013.01.002_bib0075) 1988 King (10.1016/j.tibs.2013.01.002_bib0340) 2003; 11 Karijolich (10.1016/j.tibs.2013.01.002_bib0420) 2011; 474 Duan (10.1016/j.tibs.2013.01.002_bib0320) 2009; 34 Valadkhan (10.1016/j.tibs.2013.01.002_bib0400) 2003; 9 Jady (10.1016/j.tibs.2013.01.002_bib0225) 2001; 20 Ni (10.1016/j.tibs.2013.01.002_bib0100) 1997; 89 |
| References_xml | – volume: 40 start-page: 936 year: 2007 end-page: 938 ident: bib0170 article-title: Increased urinary level of oxidized nucleosides in patients with mild-to-moderate Alzheimer's disease publication-title: Clin. Biochem. – volume: 229 start-page: 276 year: 1996 end-page: 281 ident: bib0215 article-title: More Sm snRNAs from vertebrate cells publication-title: Exp. Cell Res. – volume: 18 start-page: 5120 year: 1999 end-page: 5130 ident: bib0275 article-title: Nucleolar localization signals of box H/ACA small nucleolar RNAs publication-title: EMBO J. – volume: 28 start-page: 965 year: 2007 end-page: 977 ident: bib0355 article-title: rRNA modifications in an intersubunit bridge of the ribosome strongly affect both ribosome biogenesis and activity publication-title: Mol. Cell – volume: 19 start-page: 2142 year: 1999 end-page: 2154 ident: bib0130 article-title: Pseudouridine mapping in the publication-title: Mol. Cell. Biol. – volume: 18 start-page: 457 year: 1999 end-page: 469 ident: bib0285 article-title: Elements essential for accumulation and function of small nucleolar RNAs directing site-specific pseudouridylation of ribosomal RNAs publication-title: EMBO J. – volume: 30 start-page: 3 year: 2011 end-page: 4 ident: bib0410 article-title: Pseudouridylation goes regulatory publication-title: EMBO J. – volume: 2 start-page: 30 year: 2011 end-page: 37 ident: bib0415 article-title: A role for SUMOylation in snoRNP biogenesis revealed by quantitative proteomics publication-title: Nucleus – volume: 9 start-page: 958 year: 2002 end-page: 965 ident: bib0145 article-title: Sculpting of the spliceosomal branch site recognition motif by a conserved pseudouridine publication-title: Nat. Struct. Biol. – volume: 23 start-page: 5020 year: 1995 end-page: 5026 ident: bib0150 article-title: Stabilization of RNA stacking by pseudouridine publication-title: Nucleic Acids Res. – start-page: 165 year: 1995 end-page: 205 ident: bib0035 article-title: Biosynthesis and function of modified nucleotides publication-title: tRNA: Structure, Biosynthesis, and Function – volume: 12 start-page: 1101 year: 2005 end-page: 1107 ident: bib0300 article-title: The Cbf5–Nop10 complex is a molecular bracket that organizes box H/ACA RNPs publication-title: Nat. Struct. Mol. Biol. – volume: 37 start-page: D118 year: 2009 end-page: D121 ident: bib0010 article-title: MODOMICS: a database of RNA modification pathways. 2008 update publication-title: Nucleic Acids Res. – volume: 26 start-page: 205 year: 2007 end-page: 215 ident: bib0290 article-title: Solution structure of an rRNA substrate bound to the pseudouridylation pocket of a box H/ACA snoRNA publication-title: Mol. Cell – volume: 12 start-page: 15 year: 2006 end-page: 25 ident: bib0070 article-title: A computational screen for mammalian pseudouridylation guide H/ACA RNAs publication-title: RNA – volume: 14 start-page: 1189 year: 2007 end-page: 1195 ident: bib0330 article-title: Substrate RNA positioning in the archaeal H/ACA ribonucleoprotein complex publication-title: Nat. Struct. Mol. Biol. – volume: 39 start-page: D195 year: 2011 end-page: D201 ident: bib0005 article-title: The RNA Modification Database, RNAMDB: 2011 update publication-title: Nucleic Acids Res. – volume: 227 start-page: 907 year: 1957 end-page: 915 ident: bib0025 article-title: Ribonucleic acids from yeast which contain a fifth nucleotide publication-title: J. Biol. Chem. – volume: 280 start-page: 6655 year: 2005 end-page: 6662 ident: bib0390 article-title: Psi35 in the branch site recognition region of U2 small nuclear RNA is important for pre-mRNA splicing in publication-title: J. Biol. Chem. – volume: 133 start-page: 851 year: 1993 end-page: 863 ident: bib0440 article-title: Mutational analysis of pre-mRNA splicing in publication-title: Genetics – volume: 27 start-page: 344 year: 2002 end-page: 351 ident: bib0335 article-title: rRNA modifications and ribosome function publication-title: Trends Biochem. Sci. – volume: 15 start-page: 1716 year: 2009 end-page: 1728 ident: bib0350 article-title: Loss of rRNA modifications in the decoding center of the ribosome impairs translation and strongly delays pre-rRNA processing publication-title: RNA – volume: 22 start-page: 1889 year: 2003 end-page: 1897 ident: bib0135 article-title: Pseudouridylation (Psi) of U2 snRNA in publication-title: EMBO J. – volume: 32 start-page: 4281 year: 2004 end-page: 4296 ident: bib0200 article-title: Genome-wide searching for pseudouridylation guide snoRNAs: analysis of the publication-title: Nucleic Acids Res. – volume: 24 start-page: 2403 year: 2005 end-page: 2413 ident: bib0125 article-title: Pseudouridylation of yeast U2 snRNA is catalyzed by either an RNA-guided or RNA-independent mechanism publication-title: EMBO J. – volume: 77 start-page: 139 year: 1995 end-page: 141 ident: bib0040 article-title: Posttranscriptionally modified nucleosides in transfer RNA: their locations and frequencies publication-title: Biochimie – volume: 33 start-page: 3133 year: 2005 end-page: 3144 ident: bib0120 article-title: Reconstitution of archaeal H/ACA small ribonucleoprotein complexes active in pseudouridylation publication-title: Nucleic Acids Res. – start-page: 1 year: 1998 end-page: 20 ident: bib0030 article-title: Historical perspectives on RNA nucleoside sodifications publication-title: Modification and Editing of RNA – volume: 30 start-page: 4108 year: 2010 end-page: 4119 ident: bib0425 article-title: A flexible RNA backbone within the polypyrimidine tract is required for U2AF65 binding and pre-mRNA splicing publication-title: Mol. Cell. Biol. – volume: 12 start-page: 527 year: 1998 end-page: 537 ident: bib0270 article-title: The box H + ACA snoRNAs carry Cbf5p, the putative rRNA pseudouridine synthase publication-title: Genes Dev. – volume: 104 start-page: 6655 year: 2007 end-page: 6660 ident: bib0295 article-title: H/ACA small nucleolar RNA pseudouridylation pockets bind substrate RNA to form three-way junctions that position the target U for modification publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 9 start-page: 771 year: 2003 end-page: 779 ident: bib0365 article-title: A snoRNA that guides the two most conserved pseudouridine modifications within rRNA confers a growth advantage in yeast publication-title: RNA – start-page: 201 year: 1998 end-page: 228 ident: bib0080 article-title: Posttranscriptional modifications in the U small nuclear RNAs publication-title: Modification and Editing of RNA – volume: 17 start-page: 162 year: 2003 end-page: 180 ident: bib0050 article-title: tRNA transfers to the limelight publication-title: Genes Dev. – volume: 30 start-page: 79 year: 2011 end-page: 89 ident: bib0405 article-title: U2 snRNA is inducibly pseudouridylated at novel sites by Pus7p and snR81 RNP publication-title: EMBO J. – volume: 9 start-page: 1371 year: 2003 end-page: 1382 ident: bib0245 article-title: The publication-title: RNA – volume: 26 start-page: 148 year: 1998 end-page: 153 ident: bib0045 article-title: Compilation of tRNA sequences and sequences of tRNA genes publication-title: Nucleic Acids Res. – volume: 283 start-page: 26026 year: 2008 end-page: 26036 ident: bib0360 article-title: Ribosome performance is enhanced by a rich cluster of pseudouridines in the A-site finger region of the large subunit publication-title: J. Biol. Chem. – volume: 15 start-page: 176 year: 2009 end-page: 186 ident: bib0110 article-title: Functionality and substrate specificity of human box H/ACA guide RNAs publication-title: RNA – start-page: 223 year: 2005 end-page: 262 ident: bib0085 article-title: Mechanisms and functions of RNA-guided RNA modification publication-title: Topics in Current Genetics – volume: 16 start-page: 4770 year: 1997 end-page: 4776 ident: bib0250 article-title: A small nucleolar RNP protein is required for pseudouridylation of eukaryotic ribosomal RNAs publication-title: EMBO J. – volume: 443 start-page: 302 year: 2006 end-page: 307 ident: bib0315 article-title: Crystal structure of an H/ACA box ribonucleoprotein particle publication-title: Nature – volume: 33 start-page: 7560-7567 year: 1994 ident: bib0140 article-title: Crystal structure of unmodified tRNA(Gln) complexed with glutaminyl-tRNA synthetase and ATP suggests a possible role for pseudo-uridines in stabilization of RNA structure publication-title: Biochemistry – volume: 10 start-page: 3877 year: 1999 end-page: 3890 ident: bib0280 article-title: Box H and box ACA are nucleolar localization elements of U17 small nucleolar RNA publication-title: Mol. Biol. Cell – volume: 9 start-page: 892 year: 2003 end-page: 904 ident: bib0400 article-title: Characterization of the catalytic activity of U2 and U6 snRNAs publication-title: RNA – volume: 99 start-page: 12697 year: 2002 end-page: 12702 ident: bib0160 article-title: Investigation of Overhauser effects between pseudouridine and water protons in RNA helices publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 19 start-page: 1238 year: 2005 end-page: 1248 ident: bib0115 article-title: RNA-guided RNA modification: functional organization of the archaeal H/ACA RNP publication-title: Genes Dev. – volume: 17 start-page: 5783 year: 1998 end-page: 5795 ident: bib0380 article-title: Modifications of U2 snRNA are required for snRNP assembly and pre-mRNA splicing publication-title: EMBO J. – volume: 167 start-page: 483 year: 1951 end-page: 484 ident: bib0020 article-title: Nucleoside-5′-phosphates from ribonucleic acid publication-title: Nature – start-page: 1 year: 1988 end-page: 37 ident: bib0075 article-title: Small nuclear RNAs: RNA sequences, structure, and modifications publication-title: Structure and Function of Major and Minor Small Nuclear Ribonucleoprotein Particles – volume: 20 start-page: 541 year: 2001 end-page: 551 ident: bib0225 article-title: A small nucleolar guide RNA functions both in 2′- publication-title: EMBO J. – volume: 34 start-page: 47 year: 2009 end-page: 57 ident: bib0240 article-title: A conserved WD40 protein binds the Cajal body localization signal of scaRNP particles publication-title: Mol. Cell – volume: 9 start-page: 4303 year: 1981 end-page: 4324 ident: bib0055 article-title: Primary and secondary structures of Escherichia coli MRE 600 23S ribosomal RNA. Comparison with models of secondary structure for maize chloroplast 23S rRNA and for large portions of mouse and human 16S mitochondrial rRNAs publication-title: Nucleic Acids Res. – volume: 18 start-page: 402 year: 2012 end-page: 411 ident: bib0190 article-title: Discovery of publication-title: RNA – volume: 27 start-page: 1683 year: 1999 end-page: 1689 ident: bib0450 article-title: The presence of pseudouridine in the anticodon alters the genetic code: a possible mechanism for assignment of the AAA lysine codon as asparagine in echinoderm mitochondria publication-title: Nucleic Acids Res. – volume: 18 start-page: 4546 year: 2009 end-page: 4551 ident: bib0175 article-title: Pathogenic publication-title: Hum. Mol. Genet. – volume: 10 start-page: 681 year: 2004 end-page: 690 ident: bib0375 article-title: Pseudouridines in and near the branch site recognition region of U2 snRNA are required for snRNP biogenesis and pre-mRNA splicing in publication-title: RNA – year: 2009 ident: bib0015 article-title: DNA and RNA Modification Enzymes: Structure, Mechanism, Function and Evolution – volume: 2 start-page: 571 year: 2011 end-page: 581 ident: bib0095 article-title: Functions and mechanisms of spliceosomal small nuclear RNA pseudouridylation publication-title: Wiley Interdiscip. Rev. RNA – volume: 89 start-page: 565 year: 1997 end-page: 573 ident: bib0100 article-title: Small nucleolar RNAs direct site-specific synthesis of pseudouridine in ribosomal RNA publication-title: Cell – volume: 22 start-page: 4283 year: 2003 end-page: 4293 ident: bib0230 article-title: A common sequence motif determines the Cajal body-specific localization of box H/ACA scaRNAs publication-title: EMBO J. – volume: 323 start-page: 644 year: 2009 end-page: 648 ident: bib0235 article-title: A human telomerase holoenzyme protein required for Cajal body localization and telomere synthesis publication-title: Science – volume: 10 start-page: 1924 year: 2004 end-page: 1944 ident: bib0385 article-title: Modified nucleotides at the 5′ end of human U2 snRNA are required for spliceosomeal E complex formation publication-title: RNA – volume: 16 start-page: 1833 year: 2008 end-page: 1840 ident: bib0465 article-title: Incorporation of pseudouridine into mRNA yields superior nonimmunogenic vector with increased translational capacity and biological stability publication-title: Mol. Ther. – volume: 20 start-page: 948 year: 2012 end-page: 953 ident: bib0455 article-title: Increased erythropoiesis in mice injected with submicrogram quantities of pseudouridine-containing mRNA encoding erythropoietin publication-title: Mol. Ther. – volume: 11 start-page: 425 year: 2003 end-page: 435 ident: bib0340 article-title: Ribosome structure and activity are altered in cells lacking snoRNPs that form pseudouridines in the peptidyl transferase center publication-title: Mol. Cell – volume: 21 start-page: 249 year: 2006 end-page: 260 ident: bib0305 article-title: Crystal structure of a Cbf5–Nop10–Gar1 complex and implications in RNA-guided pseudouridylation and dyskeratosis congenita publication-title: Mol. Cell – volume: 26 start-page: 1897 year: 2012 end-page: 1910 ident: bib0430 article-title: Human intron-encoded Alu RNAs are processed and packaged into Wdr79-associated nucleoplasmic box H/ACA RNPs publication-title: Genes Dev. – volume: 86 start-page: 823 year: 1996 end-page: 834 ident: bib0185 article-title: The RNA world of the nucleolus: two major families of small RNAs defined by different box elements with related functions publication-title: Cell – volume: 33 start-page: W686 year: 2005 end-page: W689 ident: bib0195 article-title: The tRNAscan-SE, snoscan and snoGPS web servers for the detection of tRNAs and snoRNAs publication-title: Nucleic Acids Res. – volume: 17 start-page: 7078 year: 1998 end-page: 7090 ident: bib0260 article-title: Nhp2p and Nop10p are essential for the function of H/ACA snoRNPs publication-title: EMBO J. – volume: 19 start-page: 7461 year: 1999 end-page: 7472 ident: bib0265 article-title: Point mutations in yeast CBF5 can abolish publication-title: Mol. Cell. Biol. – volume: 7 start-page: 833 year: 2001 end-page: 845 ident: bib0155 article-title: A conserved pseudouridine modification in eukaryotic U2 snRNA induces a change in branch-site architecture publication-title: RNA – volume: 34 start-page: 826 year: 2006 end-page: 839 ident: bib0310 article-title: Crystal structure determination and site-directed mutagenesis of the publication-title: Nucleic Acids Res. – volume: 105 start-page: 19684 year: 2008 end-page: 19689 ident: bib0435 article-title: Crystal structure of a translation termination complex formed with release factor RF2 publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 474 start-page: 395 year: 2011 end-page: 398 ident: bib0420 article-title: Converting nonsense codons into sense codons by targeted pseudouridylation publication-title: Nature – start-page: 229 year: 1998 end-page: 253 ident: bib0060 article-title: The pseudouridine residues of rRNA: number, location, biosynthesis, and function publication-title: Modification and Editing of RNA – volume: 34 start-page: 427 year: 2009 end-page: 439 ident: bib0320 article-title: Structural mechanism of substrate RNA recruitment in H/ACA RNA-guided pseudouridine synthase publication-title: Mol. Cell – volume: 29 start-page: 2733 year: 2001 end-page: 2746 ident: bib0255 article-title: Accumulation of H/ACA snoRNPs depends on the integrity of the conserved central domain of the RNA-binding protein Nhp2p publication-title: Nucleic Acids Res. – volume: 16 start-page: 740 year: 2009 end-page: 746 ident: bib0325 article-title: Structure of a functional ribonucleoprotein pseudouridine synthase bound to a substrate RNA publication-title: Nat. Struct. Mol. Biol. – volume: 37 start-page: 7665 year: 2009 end-page: 7677 ident: bib0345 article-title: Nucleotide modifications in three functionally important regions of the publication-title: Nucleic Acids Res. – volume: 49 start-page: 341 year: 2000 end-page: 351 ident: bib0165 article-title: Pseudouridine in RNA: what, where, how, and why publication-title: IUBMB Life – volume: 2 start-page: 712 year: 2011 end-page: 725 ident: bib0090 article-title: Pseudouridines in spliceosomal snRNAs publication-title: Protein Cell – volume: 8 start-page: 1515 year: 2002 end-page: 1525 ident: bib0220 article-title: An H/ACA guide RNA directs U2 pseudouridylation at two different sites in the branchpoint recognition region in publication-title: RNA – volume: 19 start-page: 32 year: 1998 end-page: 38 ident: bib0180 article-title: X-linked dyskeratosis congenita is caused by mutations in a highly conserved gene with putative nucleolar functions publication-title: Nat. Genet. – volume: 44 start-page: 660 year: 2011 end-page: 666 ident: bib0370 article-title: rRNA pseudouridylation defects affect ribosomal ligand binding and translational fidelity from yeast to human cells publication-title: Mol. Cell – volume: 47 start-page: 5503 year: 2008 end-page: 5514 ident: bib0395 article-title: X-Ray structures of U2 snRNA–branchpoint duplexes containing conserved pseudouridines publication-title: Biochemistry – volume: 18 start-page: 355 year: 2012 end-page: 367 ident: bib0445 article-title: Rationalization and prediction of selective decoding of pseudouridine-modified nonsense and sense codons publication-title: RNA – volume: 6 start-page: 835 year: 2002 end-page: 843 ident: bib0205 article-title: RNomics: identification and function of small, non-messenger RNAs publication-title: Curr. Opin. Chem. Biol. – volume: 20 start-page: 2943 year: 2001 end-page: 2953 ident: bib0210 article-title: RNomics: an experimental approach that identifies 201 candidates for novel, small, non-messenger RNAs in mouse publication-title: EMBO J. – volume: 38 start-page: 5884 year: 2010 end-page: 5892 ident: bib0460 article-title: Incorporation of pseudouridine into mRNA enhances translation by diminishing PKR activation publication-title: Nucleic Acids Res. – volume: 39 start-page: 241 year: 1990 end-page: 303 ident: bib0065 article-title: The numerous modified nucleotides in eukaryotic ribosomal RNA publication-title: Prog. Nucleic Acid Res. Mol. Biol. – volume: 89 start-page: 799 year: 1997 end-page: 809 ident: bib0105 article-title: Site-specific pseudouridine formation in preribosomal RNA is guided by small nucleolar RNAs publication-title: Cell – volume: 14 start-page: 1189 year: 2007 ident: 10.1016/j.tibs.2013.01.002_bib0330 article-title: Substrate RNA positioning in the archaeal H/ACA ribonucleoprotein complex publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb1336 – volume: 9 start-page: 1371 year: 2003 ident: 10.1016/j.tibs.2013.01.002_bib0245 article-title: The Saccharomyces cerevisiae U2 snRNA:pseudouridine-synthase Pus7p is a novel multisite-multisubstrate RNA:Psi-synthase also acting on tRNAs publication-title: RNA doi: 10.1261/rna.5520403 – volume: 133 start-page: 851 year: 1993 ident: 10.1016/j.tibs.2013.01.002_bib0440 article-title: Mutational analysis of pre-mRNA splicing in Saccharomyces cerevisiae using a sensitive new reporter gene, CUP1 publication-title: Genetics doi: 10.1093/genetics/133.4.851 – volume: 89 start-page: 799 year: 1997 ident: 10.1016/j.tibs.2013.01.002_bib0105 article-title: Site-specific pseudouridine formation in preribosomal RNA is guided by small nucleolar RNAs publication-title: Cell doi: 10.1016/S0092-8674(00)80263-9 – volume: 17 start-page: 7078 year: 1998 ident: 10.1016/j.tibs.2013.01.002_bib0260 article-title: Nhp2p and Nop10p are essential for the function of H/ACA snoRNPs publication-title: EMBO J. doi: 10.1093/emboj/17.23.7078 – volume: 18 start-page: 5120 year: 1999 ident: 10.1016/j.tibs.2013.01.002_bib0275 article-title: Nucleolar localization signals of box H/ACA small nucleolar RNAs publication-title: EMBO J. doi: 10.1093/emboj/18.18.5120 – volume: 2 start-page: 712 year: 2011 ident: 10.1016/j.tibs.2013.01.002_bib0090 article-title: Pseudouridines in spliceosomal snRNAs publication-title: Protein Cell doi: 10.1007/s13238-011-1087-1 – volume: 37 start-page: 7665 year: 2009 ident: 10.1016/j.tibs.2013.01.002_bib0345 article-title: Nucleotide modifications in three functionally important regions of the Saccharomyces cerevisiae ribosome affect translation accuracy publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkp816 – volume: 28 start-page: 965 year: 2007 ident: 10.1016/j.tibs.2013.01.002_bib0355 article-title: rRNA modifications in an intersubunit bridge of the ribosome strongly affect both ribosome biogenesis and activity publication-title: Mol. Cell doi: 10.1016/j.molcel.2007.10.012 – volume: 12 start-page: 527 year: 1998 ident: 10.1016/j.tibs.2013.01.002_bib0270 article-title: The box H + ACA snoRNAs carry Cbf5p, the putative rRNA pseudouridine synthase publication-title: Genes Dev. doi: 10.1101/gad.12.4.527 – volume: 89 start-page: 565 year: 1997 ident: 10.1016/j.tibs.2013.01.002_bib0100 article-title: Small nucleolar RNAs direct site-specific synthesis of pseudouridine in ribosomal RNA publication-title: Cell doi: 10.1016/S0092-8674(00)80238-X – volume: 2 start-page: 30 year: 2011 ident: 10.1016/j.tibs.2013.01.002_bib0415 article-title: A role for SUMOylation in snoRNP biogenesis revealed by quantitative proteomics publication-title: Nucleus doi: 10.4161/nucl.2.1.14437 – volume: 29 start-page: 2733 year: 2001 ident: 10.1016/j.tibs.2013.01.002_bib0255 article-title: Accumulation of H/ACA snoRNPs depends on the integrity of the conserved central domain of the RNA-binding protein Nhp2p publication-title: Nucleic Acids Res. doi: 10.1093/nar/29.13.2733 – start-page: 1 year: 1988 ident: 10.1016/j.tibs.2013.01.002_bib0075 article-title: Small nuclear RNAs: RNA sequences, structure, and modifications – volume: 280 start-page: 6655 year: 2005 ident: 10.1016/j.tibs.2013.01.002_bib0390 article-title: Psi35 in the branch site recognition region of U2 small nuclear RNA is important for pre-mRNA splicing in Saccharomyces cerevisiae publication-title: J. Biol. Chem. doi: 10.1074/jbc.M413288200 – volume: 39 start-page: 241 year: 1990 ident: 10.1016/j.tibs.2013.01.002_bib0065 article-title: The numerous modified nucleotides in eukaryotic ribosomal RNA publication-title: Prog. Nucleic Acid Res. Mol. Biol. doi: 10.1016/S0079-6603(08)60629-7 – volume: 12 start-page: 15 year: 2006 ident: 10.1016/j.tibs.2013.01.002_bib0070 article-title: A computational screen for mammalian pseudouridylation guide H/ACA RNAs publication-title: RNA doi: 10.1261/rna.2210406 – start-page: 229 year: 1998 ident: 10.1016/j.tibs.2013.01.002_bib0060 article-title: The pseudouridine residues of rRNA: number, location, biosynthesis, and function – volume: 30 start-page: 3 year: 2011 ident: 10.1016/j.tibs.2013.01.002_bib0410 article-title: Pseudouridylation goes regulatory publication-title: EMBO J. doi: 10.1038/emboj.2010.323 – volume: 37 start-page: D118 year: 2009 ident: 10.1016/j.tibs.2013.01.002_bib0010 article-title: MODOMICS: a database of RNA modification pathways. 2008 update publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkn710 – volume: 227 start-page: 907 year: 1957 ident: 10.1016/j.tibs.2013.01.002_bib0025 article-title: Ribonucleic acids from yeast which contain a fifth nucleotide publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)70770-9 – volume: 33 start-page: 3133 year: 2005 ident: 10.1016/j.tibs.2013.01.002_bib0120 article-title: Reconstitution of archaeal H/ACA small ribonucleoprotein complexes active in pseudouridylation publication-title: Nucleic Acids Res. doi: 10.1093/nar/gki630 – volume: 9 start-page: 4303 year: 1981 ident: 10.1016/j.tibs.2013.01.002_bib0055 article-title: Primary and secondary structures of Escherichia coli MRE 600 23S ribosomal RNA. Comparison with models of secondary structure for maize chloroplast 23S rRNA and for large portions of mouse and human 16S mitochondrial rRNAs publication-title: Nucleic Acids Res. doi: 10.1093/nar/9.17.4303 – volume: 18 start-page: 402 year: 2012 ident: 10.1016/j.tibs.2013.01.002_bib0190 article-title: Discovery of Pyrobaculum small RNA families with atypical pseudouridine guide RNA features publication-title: RNA doi: 10.1261/rna.031385.111 – volume: 30 start-page: 4108 year: 2010 ident: 10.1016/j.tibs.2013.01.002_bib0425 article-title: A flexible RNA backbone within the polypyrimidine tract is required for U2AF65 binding and pre-mRNA splicing in vivo publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.00531-10 – volume: 2 start-page: 571 year: 2011 ident: 10.1016/j.tibs.2013.01.002_bib0095 article-title: Functions and mechanisms of spliceosomal small nuclear RNA pseudouridylation publication-title: Wiley Interdiscip. Rev. RNA doi: 10.1002/wrna.77 – volume: 86 start-page: 823 year: 1996 ident: 10.1016/j.tibs.2013.01.002_bib0185 article-title: The RNA world of the nucleolus: two major families of small RNAs defined by different box elements with related functions publication-title: Cell doi: 10.1016/S0092-8674(00)80156-7 – year: 2009 ident: 10.1016/j.tibs.2013.01.002_bib0015 – volume: 15 start-page: 176 year: 2009 ident: 10.1016/j.tibs.2013.01.002_bib0110 article-title: Functionality and substrate specificity of human box H/ACA guide RNAs publication-title: RNA doi: 10.1261/rna.1361509 – volume: 18 start-page: 355 year: 2012 ident: 10.1016/j.tibs.2013.01.002_bib0445 article-title: Rationalization and prediction of selective decoding of pseudouridine-modified nonsense and sense codons publication-title: RNA doi: 10.1261/rna.031351.111 – volume: 9 start-page: 892 year: 2003 ident: 10.1016/j.tibs.2013.01.002_bib0400 article-title: Characterization of the catalytic activity of U2 and U6 snRNAs publication-title: RNA doi: 10.1261/rna.5440303 – volume: 30 start-page: 79 year: 2011 ident: 10.1016/j.tibs.2013.01.002_bib0405 article-title: U2 snRNA is inducibly pseudouridylated at novel sites by Pus7p and snR81 RNP publication-title: EMBO J. doi: 10.1038/emboj.2010.316 – volume: 77 start-page: 139 year: 1995 ident: 10.1016/j.tibs.2013.01.002_bib0040 article-title: Posttranscriptionally modified nucleosides in transfer RNA: their locations and frequencies publication-title: Biochimie doi: 10.1016/0300-9084(96)88117-X – volume: 22 start-page: 1889 year: 2003 ident: 10.1016/j.tibs.2013.01.002_bib0135 article-title: Pseudouridylation (Psi) of U2 snRNA in S. cerevisiae is catalyzed by an RNA-independent mechanism publication-title: EMBO J. doi: 10.1093/emboj/cdg191 – volume: 40 start-page: 936 year: 2007 ident: 10.1016/j.tibs.2013.01.002_bib0170 article-title: Increased urinary level of oxidized nucleosides in patients with mild-to-moderate Alzheimer's disease publication-title: Clin. Biochem. doi: 10.1016/j.clinbiochem.2006.11.021 – volume: 44 start-page: 660 year: 2011 ident: 10.1016/j.tibs.2013.01.002_bib0370 article-title: rRNA pseudouridylation defects affect ribosomal ligand binding and translational fidelity from yeast to human cells publication-title: Mol. Cell doi: 10.1016/j.molcel.2011.09.017 – volume: 49 start-page: 341 year: 2000 ident: 10.1016/j.tibs.2013.01.002_bib0165 article-title: Pseudouridine in RNA: what, where, how, and why publication-title: IUBMB Life doi: 10.1080/152165400410182 – volume: 474 start-page: 395 year: 2011 ident: 10.1016/j.tibs.2013.01.002_bib0420 article-title: Converting nonsense codons into sense codons by targeted pseudouridylation publication-title: Nature doi: 10.1038/nature10165 – volume: 105 start-page: 19684 year: 2008 ident: 10.1016/j.tibs.2013.01.002_bib0435 article-title: Crystal structure of a translation termination complex formed with release factor RF2 publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0810953105 – start-page: 223 year: 2005 ident: 10.1016/j.tibs.2013.01.002_bib0085 article-title: Mechanisms and functions of RNA-guided RNA modification – volume: 27 start-page: 344 year: 2002 ident: 10.1016/j.tibs.2013.01.002_bib0335 article-title: rRNA modifications and ribosome function publication-title: Trends Biochem. Sci. doi: 10.1016/S0968-0004(02)02109-6 – volume: 10 start-page: 1924 year: 2004 ident: 10.1016/j.tibs.2013.01.002_bib0385 article-title: Modified nucleotides at the 5′ end of human U2 snRNA are required for spliceosomeal E complex formation publication-title: RNA doi: 10.1261/rna.7186504 – volume: 7 start-page: 833 year: 2001 ident: 10.1016/j.tibs.2013.01.002_bib0155 article-title: A conserved pseudouridine modification in eukaryotic U2 snRNA induces a change in branch-site architecture publication-title: RNA doi: 10.1017/S1355838201002308 – volume: 47 start-page: 5503 year: 2008 ident: 10.1016/j.tibs.2013.01.002_bib0395 article-title: X-Ray structures of U2 snRNA–branchpoint duplexes containing conserved pseudouridines publication-title: Biochemistry doi: 10.1021/bi7022392 – volume: 39 start-page: D195 year: 2011 ident: 10.1016/j.tibs.2013.01.002_bib0005 article-title: The RNA Modification Database, RNAMDB: 2011 update publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkq1028 – volume: 21 start-page: 249 year: 2006 ident: 10.1016/j.tibs.2013.01.002_bib0305 article-title: Crystal structure of a Cbf5–Nop10–Gar1 complex and implications in RNA-guided pseudouridylation and dyskeratosis congenita publication-title: Mol. Cell doi: 10.1016/j.molcel.2005.11.017 – volume: 16 start-page: 740 year: 2009 ident: 10.1016/j.tibs.2013.01.002_bib0325 article-title: Structure of a functional ribonucleoprotein pseudouridine synthase bound to a substrate RNA publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.1624 – volume: 16 start-page: 1833 year: 2008 ident: 10.1016/j.tibs.2013.01.002_bib0465 article-title: Incorporation of pseudouridine into mRNA yields superior nonimmunogenic vector with increased translational capacity and biological stability publication-title: Mol. Ther. doi: 10.1038/mt.2008.200 – volume: 19 start-page: 2142 year: 1999 ident: 10.1016/j.tibs.2013.01.002_bib0130 article-title: Pseudouridine mapping in the Saccharomyces cerevisiae spliceosomal U small nuclear RNAs (snRNAs) reveals that pseudouridine synthase pus1p exhibits a dual substrate specificity for U2 snRNA and tRNA publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.19.3.2142 – volume: 17 start-page: 5783 year: 1998 ident: 10.1016/j.tibs.2013.01.002_bib0380 article-title: Modifications of U2 snRNA are required for snRNP assembly and pre-mRNA splicing publication-title: EMBO J. doi: 10.1093/emboj/17.19.5783 – volume: 6 start-page: 835 year: 2002 ident: 10.1016/j.tibs.2013.01.002_bib0205 article-title: RNomics: identification and function of small, non-messenger RNAs publication-title: Curr. Opin. Chem. Biol. doi: 10.1016/S1367-5931(02)00397-6 – volume: 323 start-page: 644 year: 2009 ident: 10.1016/j.tibs.2013.01.002_bib0235 article-title: A human telomerase holoenzyme protein required for Cajal body localization and telomere synthesis publication-title: Science doi: 10.1126/science.1165357 – volume: 22 start-page: 4283 year: 2003 ident: 10.1016/j.tibs.2013.01.002_bib0230 article-title: A common sequence motif determines the Cajal body-specific localization of box H/ACA scaRNAs publication-title: EMBO J. doi: 10.1093/emboj/cdg394 – volume: 10 start-page: 681 year: 2004 ident: 10.1016/j.tibs.2013.01.002_bib0375 article-title: Pseudouridines in and near the branch site recognition region of U2 snRNA are required for snRNP biogenesis and pre-mRNA splicing in Xenopus oocytes publication-title: RNA doi: 10.1261/rna.5159504 – volume: 23 start-page: 5020 year: 1995 ident: 10.1016/j.tibs.2013.01.002_bib0150 article-title: Stabilization of RNA stacking by pseudouridine publication-title: Nucleic Acids Res. doi: 10.1093/nar/23.24.5020 – volume: 443 start-page: 302 year: 2006 ident: 10.1016/j.tibs.2013.01.002_bib0315 article-title: Crystal structure of an H/ACA box ribonucleoprotein particle publication-title: Nature doi: 10.1038/nature05151 – start-page: 201 year: 1998 ident: 10.1016/j.tibs.2013.01.002_bib0080 article-title: Posttranscriptional modifications in the U small nuclear RNAs – volume: 19 start-page: 1238 year: 2005 ident: 10.1016/j.tibs.2013.01.002_bib0115 article-title: RNA-guided RNA modification: functional organization of the archaeal H/ACA RNP publication-title: Genes Dev. doi: 10.1101/gad.1309605 – volume: 34 start-page: 47 year: 2009 ident: 10.1016/j.tibs.2013.01.002_bib0240 article-title: A conserved WD40 protein binds the Cajal body localization signal of scaRNP particles publication-title: Mol. Cell doi: 10.1016/j.molcel.2009.02.020 – volume: 34 start-page: 826 year: 2006 ident: 10.1016/j.tibs.2013.01.002_bib0310 article-title: Crystal structure determination and site-directed mutagenesis of the Pyrococcus abyssi aCBF5–aNOP10 complex reveal crucial roles of the C-terminal domains of both proteins in H/ACA sRNP activity publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkj482 – volume: 19 start-page: 7461 year: 1999 ident: 10.1016/j.tibs.2013.01.002_bib0265 article-title: Point mutations in yeast CBF5 can abolish in vivo pseudouridylation of rRNA publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.19.11.7461 – volume: 38 start-page: 5884 year: 2010 ident: 10.1016/j.tibs.2013.01.002_bib0460 article-title: Incorporation of pseudouridine into mRNA enhances translation by diminishing PKR activation publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkq347 – volume: 24 start-page: 2403 year: 2005 ident: 10.1016/j.tibs.2013.01.002_bib0125 article-title: Pseudouridylation of yeast U2 snRNA is catalyzed by either an RNA-guided or RNA-independent mechanism publication-title: EMBO J. doi: 10.1038/sj.emboj.7600718 – volume: 104 start-page: 6655 year: 2007 ident: 10.1016/j.tibs.2013.01.002_bib0295 article-title: H/ACA small nucleolar RNA pseudouridylation pockets bind substrate RNA to form three-way junctions that position the target U for modification publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0701534104 – volume: 9 start-page: 771 year: 2003 ident: 10.1016/j.tibs.2013.01.002_bib0365 article-title: A snoRNA that guides the two most conserved pseudouridine modifications within rRNA confers a growth advantage in yeast publication-title: RNA doi: 10.1261/rna.5240503 – volume: 16 start-page: 4770 year: 1997 ident: 10.1016/j.tibs.2013.01.002_bib0250 article-title: A small nucleolar RNP protein is required for pseudouridylation of eukaryotic ribosomal RNAs publication-title: EMBO J. doi: 10.1093/emboj/16.15.4770 – volume: 167 start-page: 483 year: 1951 ident: 10.1016/j.tibs.2013.01.002_bib0020 article-title: Nucleoside-5′-phosphates from ribonucleic acid publication-title: Nature doi: 10.1038/167483a0 – volume: 229 start-page: 276 year: 1996 ident: 10.1016/j.tibs.2013.01.002_bib0215 article-title: More Sm snRNAs from vertebrate cells publication-title: Exp. Cell Res. doi: 10.1006/excr.1996.0372 – volume: 12 start-page: 1101 year: 2005 ident: 10.1016/j.tibs.2013.01.002_bib0300 article-title: The Cbf5–Nop10 complex is a molecular bracket that organizes box H/ACA RNPs publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb1036 – volume: 99 start-page: 12697 year: 2002 ident: 10.1016/j.tibs.2013.01.002_bib0160 article-title: Investigation of Overhauser effects between pseudouridine and water protons in RNA helices publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.202477199 – volume: 10 start-page: 3877 year: 1999 ident: 10.1016/j.tibs.2013.01.002_bib0280 article-title: Box H and box ACA are nucleolar localization elements of U17 small nucleolar RNA publication-title: Mol. Biol. Cell doi: 10.1091/mbc.10.11.3877 – volume: 9 start-page: 958 year: 2002 ident: 10.1016/j.tibs.2013.01.002_bib0145 article-title: Sculpting of the spliceosomal branch site recognition motif by a conserved pseudouridine publication-title: Nat. Struct. Biol. doi: 10.1038/nsb873 – volume: 26 start-page: 1897 year: 2012 ident: 10.1016/j.tibs.2013.01.002_bib0430 article-title: Human intron-encoded Alu RNAs are processed and packaged into Wdr79-associated nucleoplasmic box H/ACA RNPs publication-title: Genes Dev. doi: 10.1101/gad.197467.112 – volume: 17 start-page: 162 year: 2003 ident: 10.1016/j.tibs.2013.01.002_bib0050 article-title: tRNA transfers to the limelight publication-title: Genes Dev. doi: 10.1101/gad.1049103 – volume: 19 start-page: 32 year: 1998 ident: 10.1016/j.tibs.2013.01.002_bib0180 article-title: X-linked dyskeratosis congenita is caused by mutations in a highly conserved gene with putative nucleolar functions publication-title: Nat. Genet. doi: 10.1038/ng0598-32 – volume: 18 start-page: 457 year: 1999 ident: 10.1016/j.tibs.2013.01.002_bib0285 article-title: Elements essential for accumulation and function of small nucleolar RNAs directing site-specific pseudouridylation of ribosomal RNAs publication-title: EMBO J. doi: 10.1093/emboj/18.2.457 – start-page: 165 year: 1995 ident: 10.1016/j.tibs.2013.01.002_bib0035 article-title: Biosynthesis and function of modified nucleotides – volume: 34 start-page: 427 year: 2009 ident: 10.1016/j.tibs.2013.01.002_bib0320 article-title: Structural mechanism of substrate RNA recruitment in H/ACA RNA-guided pseudouridine synthase publication-title: Mol. Cell doi: 10.1016/j.molcel.2009.05.005 – start-page: 1 year: 1998 ident: 10.1016/j.tibs.2013.01.002_bib0030 article-title: Historical perspectives on RNA nucleoside sodifications – volume: 18 start-page: 4546 year: 2009 ident: 10.1016/j.tibs.2013.01.002_bib0175 article-title: Pathogenic NAP57 mutations decrease ribonucleoprotein assembly in dyskeratosis congenita publication-title: Hum. Mol. Genet. doi: 10.1093/hmg/ddp416 – volume: 33 start-page: 7560-7567 year: 1994 ident: 10.1016/j.tibs.2013.01.002_bib0140 article-title: Crystal structure of unmodified tRNA(Gln) complexed with glutaminyl-tRNA synthetase and ATP suggests a possible role for pseudo-uridines in stabilization of RNA structure publication-title: Biochemistry doi: 10.1021/bi00190a008 – volume: 283 start-page: 26026 year: 2008 ident: 10.1016/j.tibs.2013.01.002_bib0360 article-title: Ribosome performance is enhanced by a rich cluster of pseudouridines in the A-site finger region of the large subunit publication-title: J. Biol. Chem. doi: 10.1074/jbc.M803049200 – volume: 20 start-page: 541 year: 2001 ident: 10.1016/j.tibs.2013.01.002_bib0225 article-title: A small nucleolar guide RNA functions both in 2′-O-ribose methylation and pseudouridylation of the U5 spliceosomal RNA publication-title: EMBO J. doi: 10.1093/emboj/20.3.541 – volume: 26 start-page: 148 year: 1998 ident: 10.1016/j.tibs.2013.01.002_bib0045 article-title: Compilation of tRNA sequences and sequences of tRNA genes publication-title: Nucleic Acids Res. doi: 10.1093/nar/26.1.148 – volume: 33 start-page: W686 year: 2005 ident: 10.1016/j.tibs.2013.01.002_bib0195 article-title: The tRNAscan-SE, snoscan and snoGPS web servers for the detection of tRNAs and snoRNAs publication-title: Nucleic Acids Res. doi: 10.1093/nar/gki366 – volume: 15 start-page: 1716 year: 2009 ident: 10.1016/j.tibs.2013.01.002_bib0350 article-title: Loss of rRNA modifications in the decoding center of the ribosome impairs translation and strongly delays pre-rRNA processing publication-title: RNA doi: 10.1261/rna.1724409 – volume: 26 start-page: 205 year: 2007 ident: 10.1016/j.tibs.2013.01.002_bib0290 article-title: Solution structure of an rRNA substrate bound to the pseudouridylation pocket of a box H/ACA snoRNA publication-title: Mol. Cell doi: 10.1016/j.molcel.2007.03.014 – volume: 20 start-page: 2943 year: 2001 ident: 10.1016/j.tibs.2013.01.002_bib0210 article-title: RNomics: an experimental approach that identifies 201 candidates for novel, small, non-messenger RNAs in mouse publication-title: EMBO J. doi: 10.1093/emboj/20.11.2943 – volume: 11 start-page: 425 year: 2003 ident: 10.1016/j.tibs.2013.01.002_bib0340 article-title: Ribosome structure and activity are altered in cells lacking snoRNPs that form pseudouridines in the peptidyl transferase center publication-title: Mol. Cell doi: 10.1016/S1097-2765(03)00040-6 – volume: 27 start-page: 1683 year: 1999 ident: 10.1016/j.tibs.2013.01.002_bib0450 article-title: The presence of pseudouridine in the anticodon alters the genetic code: a possible mechanism for assignment of the AAA lysine codon as asparagine in echinoderm mitochondria publication-title: Nucleic Acids Res. doi: 10.1093/nar/27.7.1683 – volume: 20 start-page: 948 year: 2012 ident: 10.1016/j.tibs.2013.01.002_bib0455 article-title: Increased erythropoiesis in mice injected with submicrogram quantities of pseudouridine-containing mRNA encoding erythropoietin publication-title: Mol. Ther. doi: 10.1038/mt.2012.7 – volume: 8 start-page: 1515 year: 2002 ident: 10.1016/j.tibs.2013.01.002_bib0220 article-title: An H/ACA guide RNA directs U2 pseudouridylation at two different sites in the branchpoint recognition region in Xenopus oocytes publication-title: RNA doi: 10.1017/S1355838202022537 – volume: 32 start-page: 4281 year: 2004 ident: 10.1016/j.tibs.2013.01.002_bib0200 article-title: Genome-wide searching for pseudouridylation guide snoRNAs: analysis of the Saccharomyces cerevisiae genome publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkh768 |
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| Snippet | Pseudouridine is the most abundant post-transcriptionally modified nucleotide in various stable RNAs of all organisms. Pseudouridine is derived from uridine... Pseudouridine is the most abundant posttranscriptionally modified nucleotide in various stable RNAs of all organisms. Pseudouridine is derived from uridine via... |
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| SubjectTerms | Animals Base Pairing Codon - genetics eukaryotic cells Humans hydrogen bonding Isomerism isomerization messenger RNA Nucleic Acid Conformation nucleotides Pseudouridine - genetics Pseudouridine - metabolism ribonucleoproteins Ribonucleoproteins - genetics Ribonucleoproteins - metabolism RNA Processing, Post-Transcriptional RNA, Messenger - genetics RNA, Messenger - metabolism RNA, Ribosomal - genetics RNA, Ribosomal - metabolism RNA, Small Nuclear - genetics RNA, Small Nuclear - metabolism Spliceosomes - genetics Spliceosomes - metabolism uridine |
| Title | RNA pseudouridylation: new insights into an old modification |
| URI | https://dx.doi.org/10.1016/j.tibs.2013.01.002 https://www.ncbi.nlm.nih.gov/pubmed/23391857 https://www.proquest.com/docview/1319615756 https://www.proquest.com/docview/1348485167 https://www.proquest.com/docview/2000086735 https://pubmed.ncbi.nlm.nih.gov/PMC3608706 |
| Volume | 38 |
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