eRF1 mediates codon usage effects on mRNA translation efficiency through premature termination at rare codons
Codon usage bias is a universal feature of eukaryotic and prokaryotic genomes and plays an important role in regulating gene expression levels. A major role of codon usage is thought to regulate protein expression levels by affecting mRNA translation efficiency, but the underlying mechanism is uncle...
Saved in:
| Published in | Nucleic acids research Vol. 47; no. 17; pp. 9243 - 9258 |
|---|---|
| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Oxford University Press
26.09.2019
|
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | Codon usage bias is a universal feature of eukaryotic and prokaryotic genomes and plays an important role in regulating gene expression levels. A major role of codon usage is thought to regulate protein expression levels by affecting mRNA translation efficiency, but the underlying mechanism is unclear. By analyzing ribosome profiling results, here we showed that codon usage regulates translation elongation rate and that rare codons are decoded more slowly than common codons in all codon families in Neurospora. Rare codons resulted in ribosome stalling in manners both dependent and independent of protein sequence context and caused premature translation termination. This mechanism was shown to be conserved in Drosophila cells. In both Neurospora and Drosophila cells, codon usage plays an important role in regulating mRNA translation efficiency. We found that the rare codon-dependent premature termination is mediated by the translation termination factor eRF1, which recognizes ribosomes stalled on rare sense codons. Silencing of eRF1 expression resulted in codon usage-dependent changes in protein expression. Together, these results establish a mechanism for how codon usage regulates mRNA translation efficiency. |
|---|---|
| AbstractList | Codon usage bias is a universal feature of eukaryotic and prokaryotic genomes and plays an important role in regulating gene expression levels. A major role of codon usage is thought to regulate protein expression levels by affecting mRNA translation efficiency, but the underlying mechanism is unclear. By analyzing ribosome profiling results, here we showed that codon usage regulates translation elongation rate and that rare codons are decoded more slowly than common codons in all codon families in
Neurospora
. Rare codons resulted in ribosome stalling in manners both dependent and independent of protein sequence context and caused premature translation termination. This mechanism was shown to be conserved in
Drosophila
cells. In both
Neurospora
and
Drosophila
cells, codon usage plays an important role in regulating mRNA translation efficiency. We found that the rare codon-dependent premature termination is mediated by the translation termination factor eRF1, which recognizes ribosomes stalled on rare sense codons. Silencing of eRF1 expression resulted in codon usage-dependent changes in protein expression. Together, these results establish a mechanism for how codon usage regulates mRNA translation efficiency. Codon usage bias is a universal feature of eukaryotic and prokaryotic genomes and plays an important role in regulating gene expression levels. A major role of codon usage is thought to regulate protein expression levels by affecting mRNA translation efficiency, but the underlying mechanism is unclear. By analyzing ribosome profiling results, here we showed that codon usage regulates translation elongation rate and that rare codons are decoded more slowly than common codons in all codon families in Neurospora. Rare codons resulted in ribosome stalling in manners both dependent and independent of protein sequence context and caused premature translation termination. This mechanism was shown to be conserved in Drosophila cells. In both Neurospora and Drosophila cells, codon usage plays an important role in regulating mRNA translation efficiency. We found that the rare codon-dependent premature termination is mediated by the translation termination factor eRF1, which recognizes ribosomes stalled on rare sense codons. Silencing of eRF1 expression resulted in codon usage-dependent changes in protein expression. Together, these results establish a mechanism for how codon usage regulates mRNA translation efficiency. Codon usage bias is a universal feature of eukaryotic and prokaryotic genomes and plays an important role in regulating gene expression levels. A major role of codon usage is thought to regulate protein expression levels by affecting mRNA translation efficiency, but the underlying mechanism is unclear. By analyzing ribosome profiling results, here we showed that codon usage regulates translation elongation rate and that rare codons are decoded more slowly than common codons in all codon families in Neurospora. Rare codons resulted in ribosome stalling in manners both dependent and independent of protein sequence context and caused premature translation termination. This mechanism was shown to be conserved in Drosophila cells. In both Neurospora and Drosophila cells, codon usage plays an important role in regulating mRNA translation efficiency. We found that the rare codon-dependent premature termination is mediated by the translation termination factor eRF1, which recognizes ribosomes stalled on rare sense codons. Silencing of eRF1 expression resulted in codon usage-dependent changes in protein expression. Together, these results establish a mechanism for how codon usage regulates mRNA translation efficiency.Codon usage bias is a universal feature of eukaryotic and prokaryotic genomes and plays an important role in regulating gene expression levels. A major role of codon usage is thought to regulate protein expression levels by affecting mRNA translation efficiency, but the underlying mechanism is unclear. By analyzing ribosome profiling results, here we showed that codon usage regulates translation elongation rate and that rare codons are decoded more slowly than common codons in all codon families in Neurospora. Rare codons resulted in ribosome stalling in manners both dependent and independent of protein sequence context and caused premature translation termination. This mechanism was shown to be conserved in Drosophila cells. In both Neurospora and Drosophila cells, codon usage plays an important role in regulating mRNA translation efficiency. We found that the rare codon-dependent premature termination is mediated by the translation termination factor eRF1, which recognizes ribosomes stalled on rare sense codons. Silencing of eRF1 expression resulted in codon usage-dependent changes in protein expression. Together, these results establish a mechanism for how codon usage regulates mRNA translation efficiency. |
| Author | Dang, Yunkun Yang, Qian Yu, Chien-Hung Xie, Pancheng Liu, Yi Sachs, Matthew S Zhao, Fangzhou Wu, Cheng |
| AuthorAffiliation | 5 Jiangsu Key Laboratory of Neuropsychiatric Diseases and Cambridge-Suda Genomic Resource Center, Soochow University , 199 Ren'ai Road, Suzhou, Jiangsu 215123, China 2 Department of Biochemistry and Molecular Biology, National Cheng Kung University , Tainan 701, Taiwan 1 Department of Physiology, The University of Texas Southwestern Medical Center , 5323 Harry Hines Boulevard, Dallas, TX 75390, USA 3 State Key Laboratory for Conservation and Utilization of Bio-Resources and Center for Life Science, School of Life Sciences, Yunnan University , Kunming, Yunnan 650500, China 4 Department of Biology, Texas A&M University , College Station, TX 77843-3258, USA |
| AuthorAffiliation_xml | – name: 3 State Key Laboratory for Conservation and Utilization of Bio-Resources and Center for Life Science, School of Life Sciences, Yunnan University , Kunming, Yunnan 650500, China – name: 2 Department of Biochemistry and Molecular Biology, National Cheng Kung University , Tainan 701, Taiwan – name: 4 Department of Biology, Texas A&M University , College Station, TX 77843-3258, USA – name: 1 Department of Physiology, The University of Texas Southwestern Medical Center , 5323 Harry Hines Boulevard, Dallas, TX 75390, USA – name: 5 Jiangsu Key Laboratory of Neuropsychiatric Diseases and Cambridge-Suda Genomic Resource Center, Soochow University , 199 Ren'ai Road, Suzhou, Jiangsu 215123, China |
| Author_xml | – sequence: 1 givenname: Qian orcidid: 0000-0003-4005-3580 surname: Yang fullname: Yang, Qian organization: Department of Physiology, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA – sequence: 2 givenname: Chien-Hung surname: Yu fullname: Yu, Chien-Hung organization: Department of Physiology, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA, Department of Biochemistry and Molecular Biology, National Cheng Kung University, Tainan 701, Taiwan – sequence: 3 givenname: Fangzhou surname: Zhao fullname: Zhao, Fangzhou organization: Department of Physiology, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA – sequence: 4 givenname: Yunkun surname: Dang fullname: Dang, Yunkun organization: Department of Physiology, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA, State Key Laboratory for Conservation and Utilization of Bio-Resources and Center for Life Science, School of Life Sciences, Yunnan University, Kunming, Yunnan 650500, China – sequence: 5 givenname: Cheng surname: Wu fullname: Wu, Cheng organization: Department of Biology, Texas A&M University, College Station, TX 77843-3258, USA – sequence: 6 givenname: Pancheng surname: Xie fullname: Xie, Pancheng organization: Department of Physiology, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA, Jiangsu Key Laboratory of Neuropsychiatric Diseases and Cambridge-Suda Genomic Resource Center, Soochow University, 199 Ren'ai Road, Suzhou, Jiangsu 215123, China – sequence: 7 givenname: Matthew S surname: Sachs fullname: Sachs, Matthew S organization: Department of Biology, Texas A&M University, College Station, TX 77843-3258, USA – sequence: 8 givenname: Yi surname: Liu fullname: Liu, Yi organization: Department of Physiology, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/31410471$$D View this record in MEDLINE/PubMed |
| BookMark | eNptkd9LHDEQx4NYeqf2xT9A8ijC9vJrk70XQcRrC1JB9DnksrN3aXeTM8kK17--qadSxacMM598Z74zB2jfBw8IHVPylZI5n3kTZ6vffxQle2hKuWSVmEu2j6aEk7qiRDQTdJDSL0KooLX4jCa8BEQoOkUD3C4oHqB1JkPCNrTB4zGZFWDoOrA54ZIYbn9e4ByNT73JriRKzVkH3m5xXscwrtZ4E2EweYyAM8TB-R1oMo6m5J6E0xH61Jk-wZfn9xDdL67uLr9X1zffflxeXFdWCJGrJeuEbZTiEpaibuWcSSOVoMu6MYoB76ChxXld3ICUVHFeMEUbzgxpW2b4ITrf6W7GZfFmwZfhe72JbjBxq4Nx-m3Fu7VehUctVV1TJovA6bNADA8jpKwHlyz0vfEQxqQZU5xRSeasoCf_93pt8rLjApztABtDShG6V4QS_e-AuhxQ7w5YYPIOti4_rbLM6fqPvvwFC7Sg8A |
| CitedBy_id | crossref_primary_10_7554_eLife_76893 crossref_primary_10_1016_j_aquaculture_2020_735631 crossref_primary_10_1016_j_molcel_2024_05_025 crossref_primary_10_1093_nar_gkaa1253 crossref_primary_10_1007_s00253_022_12032_8 crossref_primary_10_3390_vaccines9090965 crossref_primary_10_31857_S0026898424040091 crossref_primary_10_1186_s12863_022_01089_z crossref_primary_10_1049_enb2_12004 crossref_primary_10_1073_pnas_2022590118 crossref_primary_10_3390_biom10060911 crossref_primary_10_1016_j_celrep_2021_109217 crossref_primary_10_3390_pathogens12020325 crossref_primary_10_1146_annurev_biochem_052621_091808 crossref_primary_10_1128_mBio_02605_20 crossref_primary_10_3389_fnmol_2024_1406708 crossref_primary_10_1093_gbe_evab097 crossref_primary_10_1093_nar_gkab1241 crossref_primary_10_1146_annurev_biochem_071320_112701 crossref_primary_10_1186_s12964_020_00642_6 crossref_primary_10_3390_v16040502 crossref_primary_10_1134_S0026893324700298 crossref_primary_10_2147_CPAA_S418314 crossref_primary_10_3390_v14091959 crossref_primary_10_3389_fmicb_2023_1136386 crossref_primary_10_3389_fpls_2023_1168124 crossref_primary_10_3390_ijms252111622 crossref_primary_10_1186_s43141_023_00605_7 crossref_primary_10_1002_1873_3468_13918 crossref_primary_10_1016_j_isci_2024_109413 crossref_primary_10_1016_j_tig_2022_05_009 crossref_primary_10_1002_bies_202400058 crossref_primary_10_1016_j_jbiotec_2021_11_001 crossref_primary_10_1080_23802359_2020_1780969 crossref_primary_10_1093_nar_gkab729 crossref_primary_10_1093_jb_mvaa022 crossref_primary_10_1016_j_molcel_2020_09_014 crossref_primary_10_1371_journal_pgen_1008836 crossref_primary_10_1016_j_gene_2024_148661 crossref_primary_10_1016_j_cell_2023_05_035 crossref_primary_10_1371_journal_pone_0284708 crossref_primary_10_1016_j_micpath_2024_107054 crossref_primary_10_1128_mcb_00265_22 crossref_primary_10_1093_nar_gkae365 |
| Cites_doi | 10.1038/ncomms13521 10.1016/j.cell.2016.05.070 10.1074/jbc.M708224200 10.1371/journal.pbio.0040180 10.1021/ja411302m 10.1038/nature04530 10.1016/j.cell.2014.08.011 10.1074/jbc.274.53.37565 10.1261/rna.294907 10.1038/s41467-017-00188-1 10.1016/j.molcel.2015.05.035 10.1016/j.cell.2016.04.040 10.1101/cshperspect.a032656 10.1093/nar/gkw566 10.1038/nature11942 10.1093/nar/14.13.5125 10.1038/nature14896 10.1073/pnas.0909910107 10.1128/MCB.00421-08 10.1074/jbc.272.1.255 10.1016/j.jmb.2012.06.010 10.1016/j.cell.2008.05.042 10.1016/j.jmb.2012.02.008 10.1261/rna.2411710 10.1016/j.cell.2015.02.029 10.1016/j.cell.2009.01.042 10.15252/embj.201694699 10.1093/nar/gkt113 10.1017/S135583829999043X 10.1038/nature11833 10.1073/pnas.1606724113 10.1126/science.1259724 10.1101/cshperspect.a013706 10.1016/S0076-6879(07)29010-X 10.1038/srep00075 10.1111/j.1432-1033.1985.tb09241.x 10.1074/jbc.M109.039040 10.1101/gad.1266805 10.7554/eLife.32496 10.1016/j.molcel.2015.07.018 10.1016/j.celrep.2016.01.043 10.1128/MCB.00799-14 10.1007/PL00006256 10.1126/science.1168978 10.1534/genetics.109.111294 10.1016/S0092-8674(00)80667-4 10.1016/j.ymeth.2017.12.003 10.1038/372701a0 10.1016/j.molcel.2006.03.033 10.1074/jbc.M112.447177 10.1534/genetics.104.026351 10.1101/gad.281030.116 10.1016/j.molcel.2016.01.008 10.1016/j.molcel.2012.03.013 10.1038/msb.2011.14 10.1073/pnas.1113956108 10.1371/journal.pbio.2000779 10.1126/science.1192430 10.1016/j.jmb.2008.08.089 10.7554/eLife.33569 10.1038/nature07582 10.1038/ncomms3988 10.1073/pnas.0601456103 10.1126/science.1170160 10.1093/nar/gkr1176 10.1038/nature16509 10.1016/S0014-5793(99)01566-5 10.1111/mmi.13079 10.1074/jbc.AW118.003232 10.1016/j.molcel.2007.07.019 10.1038/nrg2899 10.1016/S0022-2836(03)00813-1 10.1186/1471-2164-16-S10-S5 10.1038/s41580-018-0011-4 10.1074/jbc.M113.487090 10.1016/j.cub.2012.11.031 10.15252/msb.20145524 10.1074/jbc.RA118.004908 10.1016/j.molcel.2008.03.020 10.1038/emboj.2011.93 10.1038/325728a0 10.1093/nar/23.4.683 10.1371/journal.pgen.1005732 10.1016/S0021-9258(19)61434-1 10.1146/annurev.micro.62.081307.162835 10.1093/nar/gkx501 10.1016/j.cell.2016.04.034 10.1017/S1355838200000777 |
| ContentType | Journal Article |
| Copyright | The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research. The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research. 2019 |
| Copyright_xml | – notice: The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research. – notice: The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research. 2019 |
| DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 5PM |
| DOI | 10.1093/nar/gkz710 |
| DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic PubMed Central (Full Participant titles) |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic |
| DatabaseTitleList | MEDLINE MEDLINE - Academic CrossRef |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Anatomy & Physiology Chemistry |
| EISSN | 1362-4962 |
| EndPage | 9258 |
| ExternalDocumentID | PMC6755126 31410471 10_1093_nar_gkz710 |
| Genre | Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural |
| GrantInformation_xml | – fundername: NIGMS NIH HHS grantid: R35 GM118118 – fundername: ; ; grantid: R35GM118118 – fundername: ; ; grantid: RP160268 – fundername: ; ; grantid: I-1560 |
| GroupedDBID | --- -DZ -~X .I3 0R~ 123 18M 1TH 29N 2WC 4.4 482 53G 5VS 5WA 70E 85S A8Z AAFWJ AAHBH AAMVS AAOGV AAPXW AAUQX AAVAP AAYXX ABEJV ABGNP ABPTD ABQLI ABXVV ACGFO ACGFS ACIWK ACNCT ACPRK ACUTJ ADBBV ADHZD AEGXH AENEX AENZO AFFNX AFPKN AFRAH AFYAG AHMBA AIAGR ALMA_UNASSIGNED_HOLDINGS ALUQC AMNDL AOIJS BAWUL BAYMD BCNDV CAG CIDKT CITATION CS3 CZ4 DIK DU5 D~K E3Z EBD EBS EMOBN F5P GROUPED_DOAJ GX1 H13 HH5 HYE HZ~ IH2 KAQDR KQ8 KSI OAWHX OBC OBS OEB OES OJQWA OVT P2P PEELM PQQKQ R44 RD5 RNS ROL ROZ RPM RXO SV3 TN5 TOX TR2 WG7 WOQ X7H XSB YSK ZKX ~91 ~D7 ~KM AAPPN ADIXU AFULF BTTYL CGR CUY CVF ECM EIF M49 M~E NPM ROX 7X8 5PM |
| ID | FETCH-LOGICAL-c444t-b2f4c87736eb45d6926a6741b58a72e3fe811095415e661733b4571832a0dd2a3 |
| ISSN | 0305-1048 1362-4962 |
| IngestDate | Thu Aug 21 13:41:18 EDT 2025 Fri Jul 11 08:15:31 EDT 2025 Wed Feb 19 02:30:21 EST 2025 Tue Jul 01 02:07:22 EDT 2025 Thu Apr 24 23:01:58 EDT 2025 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 17 |
| Language | English |
| License | http://creativecommons.org/licenses/by/4.0 The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
| LinkModel | OpenURL |
| MergedId | FETCHMERGED-LOGICAL-c444t-b2f4c87736eb45d6926a6741b58a72e3fe811095415e661733b4571832a0dd2a3 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| ORCID | 0000-0003-4005-3580 |
| OpenAccessLink | http://dx.doi.org/10.1093/nar/gkz710 |
| PMID | 31410471 |
| PQID | 2273216092 |
| PQPubID | 23479 |
| PageCount | 16 |
| ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_6755126 proquest_miscellaneous_2273216092 pubmed_primary_31410471 crossref_primary_10_1093_nar_gkz710 crossref_citationtrail_10_1093_nar_gkz710 |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2019-09-26 |
| PublicationDateYYYYMMDD | 2019-09-26 |
| PublicationDate_xml | – month: 09 year: 2019 text: 2019-09-26 day: 26 |
| PublicationDecade | 2010 |
| PublicationPlace | England |
| PublicationPlace_xml | – name: England |
| PublicationTitle | Nucleic acids research |
| PublicationTitleAlternate | Nucleic Acids Res |
| PublicationYear | 2019 |
| Publisher | Oxford University Press |
| Publisher_xml | – name: Oxford University Press |
| References | Gingold (2019092221514488700_B86) 2014; 158 Kirchner (2019092221514488700_B38) 2017; 15 Cheng (2019092221514488700_B68) 2005; 19 Presnyak (2019092221514488700_B22) 2015; 160 Zhou (2019092221514488700_B33) 2015; 97 Brown (2019092221514488700_B61) 2015; 524 Kramer (2019092221514488700_B27) 2007; 13 Fan-Minogue (2019092221514488700_B57) 2008; 30 Gingold (2019092221514488700_B9) 2011; 7 Fu (2019092221514488700_B14) 2018; 293 Hellen (2019092221514488700_B60) 2018; 10 Eyler (2019092221514488700_B72) 2013; 288 Hense (2019092221514488700_B7) 2010; 184 Lampson (2019092221514488700_B8) 2013; 23 Plotkin (2019092221514488700_B4) 2011; 12 Colot (2019092221514488700_B67) 2006; 103 Sharma (2019092221514488700_B81) 2012; 40 Moriyama (2019092221514488700_B41) 1997; 45 Xu (2019092221514488700_B5) 2013; 495 Pisareva (2019092221514488700_B87) 2011; 30 Muto (2019092221514488700_B80) 2006; 22 Pop (2019092221514488700_B19) 2014; 10 Bulmer (2019092221514488700_B40) 1987; 325 Lu (2019092221514488700_B79) 2008; 384 Kudla (2019092221514488700_B25) 2006; 4 Tanner (2019092221514488700_B43) 2009; 284 Weinberg (2019092221514488700_B16) 2016; 14 Sonenberg (2019092221514488700_B21) 2009; 136 Svidritskiy (2019092221514488700_B66) 2018; 293 Spencer (2019092221514488700_B32) 2012; 422 Zhao (2019092221514488700_B29) 2017; 45 Ingolia (2019092221514488700_B73) 2009; 324 Jeacock (2019092221514488700_B13) 2018; 7 Song (2019092221514488700_B58) 2000; 100 Frolova (2019092221514488700_B62) 1999; 5 Kryuchkova (2019092221514488700_B63) 2013; 41 Sander (2019092221514488700_B35) 2014; 136 Fu (2019092221514488700_B36) 2016; 30 Sabi (2019092221514488700_B44) 2015; 16 Buhr (2019092221514488700_B37) 2016; 61 Doma (2019092221514488700_B49) 2006; 440 Hussmann (2019092221514488700_B17) 2015; 11 Yan (2019092221514488700_B31) 2016; 165 Yu (2019092221514488700_B15) 2015; 59 Shen (2019092221514488700_B48) 2015; 347 Wang (2019092221514488700_B75) 1999; 274 Boel (2019092221514488700_B24) 2016; 529 Tsuboi (2019092221514488700_B54) 2012; 46 Chiabudini (2019092221514488700_B83) 2014; 34 Hilal (2019092221514488700_B88) 2016; 7 Shoemaker (2019092221514488700_B89) 2011; 108 Zhou (2019092221514488700_B12) 2016; 113 Wu (2019092221514488700_B70) 2018; 137 Comeron (2019092221514488700_B3) 2004; 167 Chavatte (2019092221514488700_B64) 2003; 331 Hood (2019092221514488700_B76) 2009; 63 Sharp (2019092221514488700_B2) 1986; 14 Zhou (2019092221514488700_B23) 2018; 7 Dever (2019092221514488700_B59) 2012; 4 Wang (2019092221514488700_B74) 1997; 272 Wang (2019092221514488700_B30) 2016; 165 Bertram (2019092221514488700_B56) 2000; 6 Wei (2019092221514488700_B77) 2013; 288 Quax (2019092221514488700_B10) 2015; 59 Shoemaker (2019092221514488700_B50) 2010; 330 Bazzini (2019092221514488700_B26) 2016; 35 Matsuo (2019092221514488700_B55) 2017; 8 Curran (2019092221514488700_B46) 1995; 23 O’Brien (2019092221514488700_B39) 2014; 5 Lee (2019092221514488700_B53) 2007; 27 Cheng (2019092221514488700_B85) 2005; 19 Gamble (2019092221514488700_B11) 2016; 166 Schuller (2019092221514488700_B51) 2018; 19 Ikemura (2019092221514488700_B1) 1985; 2 Doronina (2019092221514488700_B82) 2008; 28 Letzring (2019092221514488700_B47) 2010; 16 Fang (2019092221514488700_B42) 2000; 275 Wu (2019092221514488700_B78) 2007; 429 Gonzalez (2019092221514488700_B69) 2011; 1 Graille (2019092221514488700_B52) 2008; 283 Kudla (2019092221514488700_B18) 2009; 324 Vivanco-Dominguez (2019092221514488700_B65) 2012; 417 Komar (2019092221514488700_B34) 1999; 462 Zhou (2019092221514488700_B6) 2013; 495 Shcherbik (2019092221514488700_B84) 2016; 44 Drummond (2019092221514488700_B28) 2008; 134 Lindhout (2019092221514488700_B45) 1985; 152 Tuller (2019092221514488700_B20) 2010; 107 Frolova (2019092221514488700_B71) 1994; 372 Zaher (2019092221514488700_B90) 2009; 457 |
| References_xml | – volume: 7 start-page: 13521 year: 2016 ident: 2019092221514488700_B88 article-title: Structural insights into ribosomal rescue by Dom34 and Hbs1 at near-atomic resolution publication-title: Nat. Commun. doi: 10.1038/ncomms13521 – volume: 166 start-page: 679 year: 2016 ident: 2019092221514488700_B11 article-title: Adjacent codons act in concert to modulate translation efficiency in yeast publication-title: Cell doi: 10.1016/j.cell.2016.05.070 – volume: 283 start-page: 7145 year: 2008 ident: 2019092221514488700_B52 article-title: Structure of yeast Dom34: a protein related to translation termination factor Erf1 and involved in No-Go decay publication-title: J. Biol. Chem. doi: 10.1074/jbc.M708224200 – volume: 4 start-page: e180 year: 2006 ident: 2019092221514488700_B25 article-title: High guanine and cytosine content increases mRNA levels in mammalian cells publication-title: PLoS Biol. doi: 10.1371/journal.pbio.0040180 – volume: 136 start-page: 858 year: 2014 ident: 2019092221514488700_B35 article-title: Expanding Anfinsen's principle: contributions of synonymous codon selection to rational protein design publication-title: J. Am. Chem. Soc. doi: 10.1021/ja411302m – volume: 440 start-page: 561 year: 2006 ident: 2019092221514488700_B49 article-title: Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation publication-title: Nature doi: 10.1038/nature04530 – volume: 158 start-page: 1281 year: 2014 ident: 2019092221514488700_B86 article-title: A dual program for translation regulation in cellular proliferation and differentiation publication-title: Cell doi: 10.1016/j.cell.2014.08.011 – volume: 274 start-page: 37565 year: 1999 ident: 2019092221514488700_B75 article-title: A highly conserved mechanism of regulated ribosome stalling mediated by fungal arginine attenuator peptides that appears independent of the charging status of arginyl-tRNAs publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.53.37565 – volume: 13 start-page: 87 year: 2007 ident: 2019092221514488700_B27 article-title: The frequency of translational misreading errors in E. coli is largely determined by tRNA competition publication-title: RNA doi: 10.1261/rna.294907 – volume: 8 start-page: 159 year: 2017 ident: 2019092221514488700_B55 article-title: Ubiquitination of stalled ribosome triggers ribosome-associated quality control publication-title: Nat. Commun. doi: 10.1038/s41467-017-00188-1 – volume: 59 start-page: 149 year: 2015 ident: 2019092221514488700_B10 article-title: Codon bias as a means to Fine-Tune gene expression publication-title: Mol. Cell doi: 10.1016/j.molcel.2015.05.035 – volume: 165 start-page: 990 year: 2016 ident: 2019092221514488700_B30 article-title: Real-time imaging of translation on single mRNA transcripts in live cells publication-title: Cell doi: 10.1016/j.cell.2016.04.040 – volume: 10 start-page: a032656 year: 2018 ident: 2019092221514488700_B60 article-title: Translation termination and ribosome recycling in eukaryotes publication-title: Cold Spring Harb. Perspect. Biol. doi: 10.1101/cshperspect.a032656 – volume: 44 start-page: 6840 year: 2016 ident: 2019092221514488700_B84 article-title: Distinct types of translation termination generate substrates for ribosome-associated quality control publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkw566 – volume: 495 start-page: 116 year: 2013 ident: 2019092221514488700_B5 article-title: Non-optimal codon usage is a mechanism to achieve circadian clock conditionality publication-title: Nature doi: 10.1038/nature11942 – volume: 14 start-page: 5125 year: 1986 ident: 2019092221514488700_B2 article-title: Codon usage in yeast: cluster analysis clearly differentiates highly and lowly expressed genes publication-title: Nucleic Acids Res. doi: 10.1093/nar/14.13.5125 – volume: 524 start-page: 493 year: 2015 ident: 2019092221514488700_B61 article-title: Structural basis for stop codon recognition in eukaryotes publication-title: Nature doi: 10.1038/nature14896 – volume: 107 start-page: 3645 year: 2010 ident: 2019092221514488700_B20 article-title: Translation efficiency is determined by both codon bias and folding energy publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0909910107 – volume: 28 start-page: 4227 year: 2008 ident: 2019092221514488700_B82 article-title: Site-specific release of nascent chains from ribosomes at a sense codon publication-title: Mol. Cell Biol. doi: 10.1128/MCB.00421-08 – volume: 272 start-page: 255 year: 1997 ident: 2019092221514488700_B74 article-title: Arginine-specific regulation mediated by the Neurospora crassa arg-2 upstream open reading frame in a homologous, cell-free in vitro translation system publication-title: J. Biol. Chem. doi: 10.1074/jbc.272.1.255 – volume: 422 start-page: 328 year: 2012 ident: 2019092221514488700_B32 article-title: Silent substitutions predictably alter translation elongation rates and protein folding efficiencies publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2012.06.010 – volume: 134 start-page: 341 year: 2008 ident: 2019092221514488700_B28 article-title: Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution publication-title: Cell doi: 10.1016/j.cell.2008.05.042 – volume: 417 start-page: 425 year: 2012 ident: 2019092221514488700_B65 article-title: Protein synthesis factors (RF1, RF2, RF3, RRF, and tmRNA) and peptidyl-tRNA hydrolase rescue stalled ribosomes at sense codons publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2012.02.008 – volume: 16 start-page: 2516 year: 2010 ident: 2019092221514488700_B47 article-title: Control of translation efficiency in yeast by codon-anticodon interactions publication-title: RNA doi: 10.1261/rna.2411710 – volume: 160 start-page: 1111 year: 2015 ident: 2019092221514488700_B22 article-title: Codon optimality is a major determinant of mRNA stability publication-title: Cell doi: 10.1016/j.cell.2015.02.029 – volume: 136 start-page: 731 year: 2009 ident: 2019092221514488700_B21 article-title: Regulation of translation initiation in eukaryotes: mechanisms and biological targets publication-title: Cell doi: 10.1016/j.cell.2009.01.042 – volume: 35 start-page: 2087 year: 2016 ident: 2019092221514488700_B26 article-title: Codon identity regulates mRNA stability and translation efficiency during the maternal-to-zygotic transition publication-title: EMBO J. doi: 10.15252/embj.201694699 – volume: 41 start-page: 4573 year: 2013 ident: 2019092221514488700_B63 article-title: Two-step model of stop codon recognition by eukaryotic release factor eRF1 publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkt113 – volume: 2 start-page: 13 year: 1985 ident: 2019092221514488700_B1 article-title: Codon usage and tRNA content in unicellular and multicellular organisms publication-title: Mol. Biol. Evol. – volume: 5 start-page: 1014 year: 1999 ident: 2019092221514488700_B62 article-title: Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis publication-title: RNA doi: 10.1017/S135583829999043X – volume: 495 start-page: 111 year: 2013 ident: 2019092221514488700_B6 article-title: Non-optimal codon usage affects expression, structure and function of clock protein FRQ publication-title: Nature doi: 10.1038/nature11833 – volume: 113 start-page: E6117 year: 2016 ident: 2019092221514488700_B12 article-title: Codon usage is an important determinant of gene expression levels largely through its effects on transcription publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.1606724113 – volume: 347 start-page: 75 year: 2015 ident: 2019092221514488700_B48 article-title: Rqc2p and 60S ribosomal subunits mediate mRNA-independent elongation of nascent chains publication-title: Science doi: 10.1126/science.1259724 – volume: 4 start-page: a013706 year: 2012 ident: 2019092221514488700_B59 article-title: The elongation, termination, and recycling phases of translation in eukaryotes publication-title: Cold Spring Harb. Perspect. Biol. doi: 10.1101/cshperspect.a013706 – volume: 429 start-page: 203 year: 2007 ident: 2019092221514488700_B78 article-title: The use of fungal in vitro systems for studying translational regulation publication-title: Methods Enzymol. doi: 10.1016/S0076-6879(07)29010-X – volume: 1 start-page: 75 year: 2011 ident: 2019092221514488700_B69 article-title: Generation of stable Drosophila cell lines using multicistronic vectors publication-title: Sci. Rep. doi: 10.1038/srep00075 – volume: 152 start-page: 625 year: 1985 ident: 2019092221514488700_B45 article-title: Ribosomes are stalled during in vitro translation of alfalfa mosaic virus RNA 1 publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1985.tb09241.x – volume: 284 start-page: 34809 year: 2009 ident: 2019092221514488700_B43 article-title: Genetic identification of nascent peptides that induce ribosome stalling publication-title: J. Biol. Chem. doi: 10.1074/jbc.M109.039040 – volume: 19 start-page: 234 year: 2005 ident: 2019092221514488700_B68 article-title: Regulation of the Neurospora circadian clock by an RNA helicase publication-title: Genes Dev. doi: 10.1101/gad.1266805 – volume: 7 start-page: e32496 year: 2018 ident: 2019092221514488700_B13 article-title: Codon usage bias controls mRNA and protein abundance in trypanosomatids publication-title: Elife doi: 10.7554/eLife.32496 – volume: 59 start-page: 744 year: 2015 ident: 2019092221514488700_B15 article-title: Codon usage influences the local rate of translation elongation to regulate co-translational protein folding publication-title: Mol. Cell doi: 10.1016/j.molcel.2015.07.018 – volume: 14 start-page: 1787 year: 2016 ident: 2019092221514488700_B16 article-title: Improved ribosome-footprint and mRNA measurements provide insights into dynamics and regulation of yeast translation publication-title: Cell Rep. doi: 10.1016/j.celrep.2016.01.043 – volume: 34 start-page: 4062 year: 2014 ident: 2019092221514488700_B83 article-title: Release factor eRF3 mediates premature translation termination on polylysine-stalled ribosomes in Saccharomyces cerevisiae publication-title: Mol. Cell Biol. doi: 10.1128/MCB.00799-14 – volume: 45 start-page: 514 year: 1997 ident: 2019092221514488700_B41 article-title: Codon usage bias and tRNA abundance in Drosophila publication-title: J. Mol. Evol. doi: 10.1007/PL00006256 – volume: 324 start-page: 218 year: 2009 ident: 2019092221514488700_B73 article-title: Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling publication-title: Science doi: 10.1126/science.1168978 – volume: 184 start-page: 547 year: 2010 ident: 2019092221514488700_B7 article-title: Experimentally increased codon bias in the Drosophila Adh gene leads to an increase in larval, but not adult, alcohol dehydrogenase activity publication-title: Genetics doi: 10.1534/genetics.109.111294 – volume: 100 start-page: 311 year: 2000 ident: 2019092221514488700_B58 article-title: The crystal structure of human eukaryotic release factor eRF1–mechanism of stop codon recognition and peptidyl-tRNA hydrolysis publication-title: Cell doi: 10.1016/S0092-8674(00)80667-4 – volume: 137 start-page: 11 year: 2018 ident: 2019092221514488700_B70 article-title: The cell free protein synthesis system from the model filamentous fungus Neurospora crassa publication-title: Methods doi: 10.1016/j.ymeth.2017.12.003 – volume: 372 start-page: 701 year: 1994 ident: 2019092221514488700_B71 article-title: A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor publication-title: Nature doi: 10.1038/372701a0 – volume: 22 start-page: 545 year: 2006 ident: 2019092221514488700_B80 article-title: Genetically encoded but nonpolypeptide prolyl-tRNA functions in the A site for SecM-mediated ribosomal stall publication-title: Mol. Cell doi: 10.1016/j.molcel.2006.03.033 – volume: 288 start-page: 9549 year: 2013 ident: 2019092221514488700_B77 article-title: The stringency of start codon selection in the filamentous fungus Neurospora crassa publication-title: J. Biol. Chem. doi: 10.1074/jbc.M112.447177 – volume: 167 start-page: 1293 year: 2004 ident: 2019092221514488700_B3 article-title: Selective and mutational patterns associated with gene expression in humans: influences on synonymous composition and intron presence publication-title: Genetics doi: 10.1534/genetics.104.026351 – volume: 30 start-page: 1761 year: 2016 ident: 2019092221514488700_B36 article-title: Codon usage affects the structure and function of the Drosophila circadian clock protein PERIOD publication-title: Genes Dev. doi: 10.1101/gad.281030.116 – volume: 61 start-page: 341 year: 2016 ident: 2019092221514488700_B37 article-title: Synonymous codons direct cotranslational folding toward different protein conformations publication-title: Mol. Cell doi: 10.1016/j.molcel.2016.01.008 – volume: 46 start-page: 518 year: 2012 ident: 2019092221514488700_B54 article-title: Dom34:hbs1 plays a general role in quality-control systems by dissociation of a stalled ribosome at the 3′ end of aberrant mRNA publication-title: Mol. Cell doi: 10.1016/j.molcel.2012.03.013 – volume: 19 start-page: 234 year: 2005 ident: 2019092221514488700_B85 article-title: Regulation of the Neurospora circadian clock by an RNA helicase publication-title: Genes Dev. doi: 10.1101/gad.1266805 – volume: 7 start-page: 481 year: 2011 ident: 2019092221514488700_B9 article-title: Determinants of translation efficiency and accuracy publication-title: Mol. Syst. Biol. doi: 10.1038/msb.2011.14 – volume: 108 start-page: E1392 year: 2011 ident: 2019092221514488700_B89 article-title: Kinetic analysis reveals the ordered coupling of translation termination and ribosome recycling in yeast publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.1113956108 – volume: 15 start-page: e2000779 year: 2017 ident: 2019092221514488700_B38 article-title: Alteration of protein function by a silent polymorphism linked to tRNA abundance publication-title: PLoS Biol. doi: 10.1371/journal.pbio.2000779 – volume: 330 start-page: 369 year: 2010 ident: 2019092221514488700_B50 article-title: Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay publication-title: Science doi: 10.1126/science.1192430 – volume: 384 start-page: 73 year: 2008 ident: 2019092221514488700_B79 article-title: Electrostatics in the ribosomal tunnel modulate chain elongation rates publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2008.08.089 – volume: 7 start-page: e33569 year: 2018 ident: 2019092221514488700_B23 article-title: Codon usage biases co-evolve with transcription termination machinery to suppress premature cleavage and polyadenylation publication-title: Elife doi: 10.7554/eLife.33569 – volume: 457 start-page: 161 year: 2009 ident: 2019092221514488700_B90 article-title: Quality control by the ribosome following peptide bond formation publication-title: Nature doi: 10.1038/nature07582 – volume: 5 start-page: 2988 year: 2014 ident: 2019092221514488700_B39 article-title: Kinetic modelling indicates that fast-translating codons can coordinate cotranslational protein folding by avoiding misfolded intermediates publication-title: Nat. Commun. doi: 10.1038/ncomms3988 – volume: 103 start-page: 10352 year: 2006 ident: 2019092221514488700_B67 article-title: A high-throughput gene knockout procedure for Neurospora reveals functions for multiple transcription factors publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0601456103 – volume: 324 start-page: 255 year: 2009 ident: 2019092221514488700_B18 article-title: Coding-sequence determinants of gene expression in Escherichia coli publication-title: Science doi: 10.1126/science.1170160 – volume: 40 start-page: 3143 year: 2012 ident: 2019092221514488700_B81 article-title: 2A peptides provide distinct solutions to driving stop-carry on translational recoding publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkr1176 – volume: 529 start-page: 358 year: 2016 ident: 2019092221514488700_B24 article-title: Codon influence on protein expression in E. coli correlates with mRNA levels publication-title: Nature doi: 10.1038/nature16509 – volume: 462 start-page: 387 year: 1999 ident: 2019092221514488700_B34 article-title: Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation publication-title: FEBS Lett. doi: 10.1016/S0014-5793(99)01566-5 – volume: 97 start-page: 974 year: 2015 ident: 2019092221514488700_B33 article-title: Nonoptimal codon usage influences protein structure in intrinsically disordered regions publication-title: Mol. Microbiol. doi: 10.1111/mmi.13079 – volume: 293 start-page: 12472 year: 2018 ident: 2019092221514488700_B66 article-title: Mechanism of premature translation termination on a sense codon publication-title: J. Biol. Chem. doi: 10.1074/jbc.AW118.003232 – volume: 27 start-page: 938 year: 2007 ident: 2019092221514488700_B53 article-title: Structural and functional insights into Dom34, a key component of no-go mRNA decay publication-title: Mol. Cell doi: 10.1016/j.molcel.2007.07.019 – volume: 12 start-page: 32 year: 2011 ident: 2019092221514488700_B4 article-title: Synonymous but not the same: the causes and consequences of codon bias publication-title: Nat. Rev. Genet. doi: 10.1038/nrg2899 – volume: 331 start-page: 745 year: 2003 ident: 2019092221514488700_B64 article-title: Stop codons and UGG promote efficient binding of the polypeptide release factor eRF1 to the ribosomal A site publication-title: J. Mol. Biol. doi: 10.1016/S0022-2836(03)00813-1 – volume: 16 start-page: S5 year: 2015 ident: 2019092221514488700_B44 article-title: A comparative genomics study on the effect of individual amino acids on ribosome stalling publication-title: BMC Genomics doi: 10.1186/1471-2164-16-S10-S5 – volume: 19 start-page: 526 year: 2018 ident: 2019092221514488700_B51 article-title: Roadblocks and resolutions in eukaryotic translation publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/s41580-018-0011-4 – volume: 288 start-page: 29530 year: 2013 ident: 2019092221514488700_B72 article-title: Eukaryotic release factor 3 is required for multiple turnovers of peptide release catalysis by eukaryotic release factor 1 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M113.487090 – volume: 23 start-page: 70 year: 2013 ident: 2019092221514488700_B8 article-title: Rare codons regulate KRas oncogenesis publication-title: Curr. Biol. doi: 10.1016/j.cub.2012.11.031 – volume: 10 start-page: 770 year: 2014 ident: 2019092221514488700_B19 article-title: Causal signals between codon bias, mRNA structure, and the efficiency of translation and elongation publication-title: Mol. Syst. Biol. doi: 10.15252/msb.20145524 – volume: 293 start-page: 17929 year: 2018 ident: 2019092221514488700_B14 article-title: Codon usage regulates human KRAS expression at both transcriptional and translational levels publication-title: J. Biol. Chem. doi: 10.1074/jbc.RA118.004908 – volume: 30 start-page: 599 year: 2008 ident: 2019092221514488700_B57 article-title: Distinct eRF3 requirements suggest alternate eRF1 conformations mediate peptide release during eukaryotic translation termination publication-title: Mol. Cell doi: 10.1016/j.molcel.2008.03.020 – volume: 30 start-page: 1804 year: 2011 ident: 2019092221514488700_B87 article-title: Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes publication-title: EMBO J. doi: 10.1038/emboj.2011.93 – volume: 325 start-page: 728 year: 1987 ident: 2019092221514488700_B40 article-title: Coevolution of codon usage and transfer RNA abundance publication-title: Nature doi: 10.1038/325728a0 – volume: 23 start-page: 683 year: 1995 ident: 2019092221514488700_B46 article-title: Decoding with the A:I wobble pair is inefficient publication-title: Nucleic Acids Res. doi: 10.1093/nar/23.4.683 – volume: 11 start-page: e1005732 year: 2015 ident: 2019092221514488700_B17 article-title: Understanding biases in ribosome profiling experiments reveals signatures of translation dynamics in yeast publication-title: PLos Genet. doi: 10.1371/journal.pgen.1005732 – volume: 275 start-page: 26710 year: 2000 ident: 2019092221514488700_B42 article-title: Evolutionarily conserved features of the arginine attenuator peptide provide the necessary requirements for its function in translational regulation publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)61434-1 – volume: 63 start-page: 385 year: 2009 ident: 2019092221514488700_B76 article-title: Evolutionary roles of upstream open reading frames in mediating gene regulation in fungi publication-title: Annu. Rev. Microbiol. doi: 10.1146/annurev.micro.62.081307.162835 – volume: 45 start-page: 8484 year: 2017 ident: 2019092221514488700_B29 article-title: Codon usage regulates protein structure and function by affecting translation elongation speed in Drosophila cells publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkx501 – volume: 165 start-page: 976 year: 2016 ident: 2019092221514488700_B31 article-title: Dynamics of translation of single mRNA molecules in vivo publication-title: Cell doi: 10.1016/j.cell.2016.04.034 – volume: 6 start-page: 1236 year: 2000 ident: 2019092221514488700_B56 article-title: Terminating eukaryote translation: domain 1 of release factor eRF1 functions in stop codon recognition publication-title: RNA doi: 10.1017/S1355838200000777 |
| SSID | ssj0014154 |
| Score | 2.4834063 |
| Snippet | Codon usage bias is a universal feature of eukaryotic and prokaryotic genomes and plays an important role in regulating gene expression levels. A major role of... |
| SourceID | pubmedcentral proquest pubmed crossref |
| SourceType | Open Access Repository Aggregation Database Index Database Enrichment Source |
| StartPage | 9243 |
| SubjectTerms | Amino Acid Sequence - genetics Animals Codon, Nonsense - genetics Codon, Terminator - genetics Drosophila - genetics Drosophila Proteins - genetics Molecular Biology Neurospora - genetics Peptide Termination Factors - genetics Protein Biosynthesis Ribosomes - genetics RNA, Messenger - genetics |
| Title | eRF1 mediates codon usage effects on mRNA translation efficiency through premature termination at rare codons |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/31410471 https://www.proquest.com/docview/2273216092 https://pubmed.ncbi.nlm.nih.gov/PMC6755126 |
| Volume | 47 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Na9swGBZZd9guZWv3kW4rGhuDEdw6lizHx1AawmCBlRbak5FtuQ1dlJLYh-ZP7C_vfSXbUZoeul1MsCUl0ftYej8fEfJVFoWIQ16AbSKUxwvBPBmHCrAsuVTS56kJtP-ciPEF_3EZXnY6f5yspapMj7LVo3Ul_yNVuAdyxSrZf5BsOyjcgM8gX7iChOH6JBmrs1Hf1n6g9zQDC1P3KswUW6dp6N7sbDLEkyD00qa94bOpeaPv21N67hZI3YqxhDo5xp4fXvYWJjEMB166auwEWZCR6TWb5hh3cFxiuILUPuhfDvSuKhvch-_1xlW9XVqHtXHWjqDP6mZerT3ndoyrSt9W2vVN9E3ylS2Ab2qyDM-p5dI8UnaJNXVa8eYabFk3G6xFzooK9iFzduc4sEzvWyu_ZcXSmJU-ur5dRXWy7AbB9oONr01HtIF4lkDvxPZ9Rp4HYHfgwhn5p21YCrQdy0dW_62G7zZmx9D32Pbd1HC2zJaH2beOOnP-iuzWdggdWlC9Jh2l98j-ECQ_n93Tb9RkBpuQyx55cdKcCrhPZog52mCOGmhQgzlaY47CDcQcdTBH15ijNeZoiznqYI7KkiLm7MDLN-RidHp-MvbqIzu8jHNeemlQ8GwQRUyolIe5iAMhBSitaTiQUaBYoQZIcRvCRCrQDCPGoFmE24r08zyQ7C3Z0XOt3hMqilT1ixzMY5FznvmxP1A8T5mvVOHnMu2S7800J1nNZ4_HqvxOtsXZJV_atneWxeXRVp8baSUwqxg5k1rNq2USgJIf9IUfB13yzkqvHYdhpjSoeF0Sbci1bYAE7ptP9PTGELmDsQ76tjh40q_7QF6uX7GPZKdcVOoTKMRlemhAemjcSX8BsH-_yA |
| linkProvider | Oxford University Press |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=eRF1+mediates+codon+usage+effects+on+mRNA+translation+efficiency+through+premature+termination+at+rare+codons&rft.jtitle=Nucleic+acids+research&rft.au=Yang%2C+Qian&rft.au=Yu%2C+Chien-Hung&rft.au=Zhao%2C+Fangzhou&rft.au=Dang%2C+Yunkun&rft.date=2019-09-26&rft.issn=0305-1048&rft.eissn=1362-4962&rft.volume=47&rft.issue=17&rft.spage=9243&rft.epage=9258&rft_id=info:doi/10.1093%2Fnar%2Fgkz710&rft.externalDBID=n%2Fa&rft.externalDocID=10_1093_nar_gkz710 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0305-1048&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0305-1048&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0305-1048&client=summon |