A Novel 3-Methylhistidine Modification of Yeast Ribosomal Protein Rpl3 Is Dependent upon the YIL110W Methyltransferase

We have shown that Rpl3, a protein of the large ribosomal subunit from baker's yeast (Saccharomyces cerevisiae), is stoichiometrically monomethylated at position 243, producing a 3-methylhistidine residue. This conclusion is supported by top-down and bottom-up mass spectrometry of Rpl3, as well...

Full description

Saved in:
Bibliographic Details
Published inThe Journal of biological chemistry Vol. 285; no. 48; pp. 37598 - 37606
Main Authors Webb, Kristofor J., Zurita-Lopez, Cecilia I., Al-Hadid, Qais, Laganowsky, Arthur, Young, Brian D., Lipson, Rebecca S., Souda, Puneet, Faull, Kym F., Whitelegge, Julian P., Clarke, Steven G.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 26.11.2010
American Society for Biochemistry and Molecular Biology
Subjects
Actin
Amino Acid Sequence
Covalent Regulation
Mass Spectrometry (MS)
Methylhistidines - metabolism
Methyltransferase
Methyltransferases - chemistry
Methyltransferases - genetics
Methyltransferases - metabolism
Molecular Sequence Data
Post-translational Modification
Protein Methylation
Protein Synthesis and Degradation
Ribosomal Proteins - genetics
Ribosomal Proteins - metabolism
Ribosomes
S-adenosylmethionine (SAM)
Saccharomyces cerevisiae
Saccharomyces cerevisiae - chemistry
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Sequence Alignment
Translation
Yeast
Protein Methylation
S-adenosylmethionine (SAM)
Translation
Yeast
Actin
Post-translational Modification
Ribosomes
Methyltransferase
Mass Spectrometry (MS)
Covalent Regulation
Online AccessGet full text

Cover

Abstract We have shown that Rpl3, a protein of the large ribosomal subunit from baker's yeast (Saccharomyces cerevisiae), is stoichiometrically monomethylated at position 243, producing a 3-methylhistidine residue. This conclusion is supported by top-down and bottom-up mass spectrometry of Rpl3, as well as by biochemical analysis of Rpl3 radiolabeled in vivo with S-adenosyl-l-[methyl-3H]methionine. The results show that a +14-Da modification occurs within the GTKKLPRKTHRGLRKVAC sequence of Rpl3. Using high-resolution cation-exchange chromatography and thin layer chromatography, we demonstrate that neither lysine nor arginine residues are methylated and that a 3-methylhistidine residue is present. Analysis of 37 deletion strains of known and putative methyltransferases revealed that only the deletion of the YIL110W gene, encoding a seven β-strand methyltransferase, results in the loss of the +14-Da modification of Rpl3. We suggest that YIL110W encodes a protein histidine methyltransferase responsible for the modification of Rpl3 and potentially other yeast proteins, and now designate it Hpm1 (Histidine protein methyltransferase 1). Deletion of the YIL110W/HPM1 gene results in numerous phenotypes including some that may result from abnormal interactions between Rpl3 and the 25 S ribosomal RNA. This is the first report of a methylated histidine residue in yeast cells, and the first example of a gene required for protein histidine methylation in nature.
AbstractList We have shown that Rpl3, a protein of the large ribosomal subunit from baker's yeast ( Saccharomyces cerevisiae ), is stoichiometrically monomethylated at position 243, producing a 3-methylhistidine residue. This conclusion is supported by top-down and bottom-up mass spectrometry of Rpl3, as well as by biochemical analysis of Rpl3 radiolabeled in vivo with S -adenosyl- l -[ methyl - 3 H]methionine. The results show that a +14-Da modification occurs within the GTKKLPRKTHRGLRKVAC sequence of Rpl3. Using high-resolution cation-exchange chromatography and thin layer chromatography, we demonstrate that neither lysine nor arginine residues are methylated and that a 3-methylhistidine residue is present. Analysis of 37 deletion strains of known and putative methyltransferases revealed that only the deletion of the YIL110W gene, encoding a seven β-strand methyltransferase, results in the loss of the +14-Da modification of Rpl3. We suggest that YIL110W encodes a protein histidine methyltransferase responsible for the modification of Rpl3 and potentially other yeast proteins, and now designate it Hpm1 ( H istidine p rotein m ethyltransferase 1). Deletion of the YIL110W/ HPM1 gene results in numerous phenotypes including some that may result from abnormal interactions between Rpl3 and the 25 S ribosomal RNA. This is the first report of a methylated histidine residue in yeast cells, and the first example of a gene required for protein histidine methylation in nature.
We have shown that Rpl3, a protein of the large ribosomal subunit from baker's yeast (Saccharomyces cerevisiae), is stoichiometrically monomethylated at position 243, producing a 3-methylhistidine residue. This conclusion is supported by top-down and bottom-up mass spectrometry of Rpl3, as well as by biochemical analysis of Rpl3 radiolabeled in vivo with S-adenosyl-l-[methyl-3H]methionine. The results show that a +14-Da modification occurs within the GTKKLPRKTHRGLRKVAC sequence of Rpl3. Using high-resolution cation-exchange chromatography and thin layer chromatography, we demonstrate that neither lysine nor arginine residues are methylated and that a 3-methylhistidine residue is present. Analysis of 37 deletion strains of known and putative methyltransferases revealed that only the deletion of the YIL110W gene, encoding a seven β-strand methyltransferase, results in the loss of the +14-Da modification of Rpl3. We suggest that YIL110W encodes a protein histidine methyltransferase responsible for the modification of Rpl3 and potentially other yeast proteins, and now designate it Hpm1 (Histidine protein methyltransferase 1). Deletion of the YIL110W/HPM1 gene results in numerous phenotypes including some that may result from abnormal interactions between Rpl3 and the 25 S ribosomal RNA. This is the first report of a methylated histidine residue in yeast cells, and the first example of a gene required for protein histidine methylation in nature.
We have shown that Rpl3, a protein of the large ribosomal subunit from baker's yeast (Saccharomyces cerevisiae), is stoichiometrically monomethylated at position 243, producing a 3-methylhistidine residue. This conclusion is supported by top-down and bottom-up mass spectrometry of Rpl3, as well as by biochemical analysis of Rpl3 radiolabeled in vivo with S-adenosyl-L-[methyl-³H]methionine. The results show that a +14-Da modification occurs within the GTKKLPRKTHRGLRKVAC sequence of Rpl3. Using high-resolution cation-exchange chromatography and thin layer chromatography, we demonstrate that neither lysine nor arginine residues are methylated and that a 3-methylhistidine residue is present. Analysis of 37 deletion strains of known and putative methyltransferases revealed that only the deletion of the YIL110W gene, encoding a seven β-strand methyltransferase, results in the loss of the +14-Da modification of Rpl3. We suggest that YIL110W encodes a protein histidine methyltransferase responsible for the modification of Rpl3 and potentially other yeast proteins, and now designate it Hpm1 (Histidine protein methyltransferase 1). Deletion of the YIL110W/HPM1 gene results in numerous phenotypes including some that may result from abnormal interactions between Rpl3 and the 25 S ribosomal RNA. This is the first report of a methylated histidine residue in yeast cells, and the first example of a gene required for protein histidine methylation in nature.
We have shown that Rpl3, a protein of the large ribosomal subunit from baker's yeast (Saccharomyces cerevisiae), is stoichiometrically monomethylated at position 243, producing a 3-methylhistidine residue. This conclusion is supported by top-down and bottom-up mass spectrometry of Rpl3, as well as by biochemical analysis of Rpl3 radiolabeled in vivo with S-adenosyl-l -[methyl- super(3)H]methionine. The results show that a +14-Da modification occurs within the GTKKLPRKTHRGLRKVAC sequence of Rpl3. Using high-resolution cation-exchange chromatography and thin layer chromatography, we demonstrate that neither lysine nor arginine residues are methylated and that a 3-methylhistidine residue is present. Analysis of 37 deletion strains of known and putative methyltransferases revealed that only the deletion of the YIL110W gene, encoding a seven b-strand methyltransferase, results in the loss of the +14-Da modification of Rpl3. We suggest that YIL110W encodes a protein histidine methyltransferase responsible for the modification of Rpl3 and potentially other yeast proteins, and now designate it Hpm1 (H istidine p rotein m ethyltransferase 1). Deletion of the YIL110W/HPM1 gene results in numerous phenotypes including some that may result from abnormal interactions between Rpl3 and the 25 S ribosomal RNA. This is the first report of a methylated histidine residue in yeast cells, and the first example of a gene required for protein histidine methylation in nature.
We have shown that Rpl3, a protein of the large ribosomal subunit from baker's yeast (Saccharomyces cerevisiae), is stoichiometrically monomethylated at position 243, producing a 3-methylhistidine residue. This conclusion is supported by top-down and bottom-up mass spectrometry of Rpl3, as well as by biochemical analysis of Rpl3 radiolabeled in vivo with S-adenosyl-l-[methyl-(3)H]methionine. The results show that a +14-Da modification occurs within the GTKKLPRKTHRGLRKVAC sequence of Rpl3. Using high-resolution cation-exchange chromatography and thin layer chromatography, we demonstrate that neither lysine nor arginine residues are methylated and that a 3-methylhistidine residue is present. Analysis of 37 deletion strains of known and putative methyltransferases revealed that only the deletion of the YIL110W gene, encoding a seven β-strand methyltransferase, results in the loss of the +14-Da modification of Rpl3. We suggest that YIL110W encodes a protein histidine methyltransferase responsible for the modification of Rpl3 and potentially other yeast proteins, and now designate it Hpm1 (Histidine protein methyltransferase 1). Deletion of the YIL110W/HPM1 gene results in numerous phenotypes including some that may result from abnormal interactions between Rpl3 and the 25 S ribosomal RNA. This is the first report of a methylated histidine residue in yeast cells, and the first example of a gene required for protein histidine methylation in nature.
We have shown that Rpl3, a protein of the large ribosomal subunit from baker's yeast (Saccharomyces cerevisiae), is stoichiometrically monomethylated at position 243, producing a 3-methylhistidine residue. This conclusion is supported by top-down and bottom-up mass spectrometry of Rpl3, as well as by biochemical analysis of Rpl3 radiolabeled in vivo with S-adenosyl-L-[methyl-3H]methionine. The results show that a +14-Da modification occurs within the GTKKLPRKTHRGLRKVAC sequence of Rpl3. Using high-resolution cation-exchange chromatography and thin layer chromatography, we demonstrate that neither lysine nor arginine residues are methylated and that a 3-methylhistidine residue is present. Analysis of 37 deletion strains of known and putative methyltransferases revealed that only the deletion of the YIL110W gene, encoding a seven beta -strand methyltransferase, results in the loss of the +14-Da modification of Rpl3. We suggest that YIL110W encodes a protein histidine methyltransferase responsible for the modification of Rpl3 and potentially other yeast proteins, and now designate it Hpm1 (Histidine protein methyltransferase 1). Deletion of the YIL110W/HPM1 gene results in numerous phenotypes including some that may result from abnormal interactions between Rpl3 and the 25 S ribosomal RNA. This is the first report of a methylated histidine residue in yeast cells, and the first example of a gene required for protein histidine methylation in nature.
Author Webb, Kristofor J.
Zurita-Lopez, Cecilia I.
Lipson, Rebecca S.
Faull, Kym F.
Clarke, Steven G.
Young, Brian D.
Whitelegge, Julian P.
Al-Hadid, Qais
Laganowsky, Arthur
Souda, Puneet
Author_xml – sequence: 1
  givenname: Kristofor J.
  surname: Webb
  fullname: Webb, Kristofor J.
  organization: From the Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California Los Angeles, Los Angeles, California 90095-1569
– sequence: 2
  givenname: Cecilia I.
  surname: Zurita-Lopez
  fullname: Zurita-Lopez, Cecilia I.
  organization: From the Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California Los Angeles, Los Angeles, California 90095-1569
– sequence: 3
  givenname: Qais
  surname: Al-Hadid
  fullname: Al-Hadid, Qais
  organization: From the Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California Los Angeles, Los Angeles, California 90095-1569
– sequence: 4
  givenname: Arthur
  surname: Laganowsky
  fullname: Laganowsky, Arthur
  organization: From the Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California Los Angeles, Los Angeles, California 90095-1569
– sequence: 5
  givenname: Brian D.
  surname: Young
  fullname: Young, Brian D.
  organization: From the Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California Los Angeles, Los Angeles, California 90095-1569
– sequence: 6
  givenname: Rebecca S.
  surname: Lipson
  fullname: Lipson, Rebecca S.
  organization: From the Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California Los Angeles, Los Angeles, California 90095-1569
– sequence: 7
  givenname: Puneet
  surname: Souda
  fullname: Souda, Puneet
  organization: Pasarow Mass Spectrometry Laboratory, NPI-Semel Institute for Neuroscience and Human Behavior, University of California Los Angeles, Los Angeles, California 90024
– sequence: 8
  givenname: Kym F.
  surname: Faull
  fullname: Faull, Kym F.
  organization: From the Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California Los Angeles, Los Angeles, California 90095-1569
– sequence: 9
  givenname: Julian P.
  surname: Whitelegge
  fullname: Whitelegge, Julian P.
  organization: From the Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California Los Angeles, Los Angeles, California 90095-1569
– sequence: 10
  givenname: Steven G.
  surname: Clarke
  fullname: Clarke, Steven G.
  email: clarke@mbi.ucla.edu
  organization: From the Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California Los Angeles, Los Angeles, California 90095-1569
BackLink https://www.ncbi.nlm.nih.gov/pubmed/20864530$$D View this record in MEDLINE/PubMed
BookMark eNqFks9vFCEUx4mpsdvq2Zty8zQtP4aZ4WLSVFs32VVTbbQnwjCPLs0srMBu0v9eNlMbPZhyIYTP-74vvO8ROvDBA0KvKTmhpK1P73pzsqT7U0varn2GZpR0vOKC_jxAM0IYrSQT3SE6SumOlFVL-gIdMtI1teBkhnZn-HPYwYh5tYS8uh9XLmU3OA94GQZnndHZBY-DxTegU8ZXrg8prPWIv8aQwXl8tRk5nif8ATbgB_AZbzelIq8A38wXxdwPPEnnqH2yEHWCl-i51WOCVw_7Mbq--Pj9_FO1-HI5Pz9bVEbIJldaD8T21NS84b221uqm5lIY3g96EG3PhJG1NayRtpeyE5YPgndElBKra8L4MXo_6W62_RoGU9xFPapNdGsd71XQTv17491K3YadYrLreCOKwLsHgRh-bSFltXbJwDhqD2GbVPlHKVouydMkl41kvKFPk5RRXstmr3k6kSaGlCLYR-eUqH0AVAmA2gdATQEoFW_-fvAj_2fiBXg7AVYHpW-jS-r6GyOUEyoprRtZCDkRUAazcxBVMg68gcFFMFkNwf23_W9KhMvc
CitedBy_id crossref_primary_10_1038_s41422_018_0003_0
crossref_primary_10_1074_jbc_AW118_003235
crossref_primary_10_1016_j_jprot_2014_07_032
crossref_primary_10_1021_pr400556c
crossref_primary_10_1016_j_mcpro_2022_100249
crossref_primary_10_1186_1754_6834_5_45
crossref_primary_10_1002_pmic_201100397
crossref_primary_10_1016_j_bcp_2013_01_012
crossref_primary_10_7554_eLife_37921
crossref_primary_10_1073_pnas_2215431120
crossref_primary_10_1002_2211_5463_12153
crossref_primary_10_1016_j_tibs_2013_02_004
crossref_primary_10_7554_eLife_72780
crossref_primary_10_1093_molbev_msab267
crossref_primary_10_1016_j_jbc_2023_105131
crossref_primary_10_3390_life11101040
crossref_primary_10_1093_jb_mvad042
crossref_primary_10_1371_journal_pone_0023168
crossref_primary_10_1007_s13238_021_00857_4
crossref_primary_10_1128_AEM_01978_13
crossref_primary_10_1074_jbc_RA119_009045
crossref_primary_10_2174_1389203721666200318161330
crossref_primary_10_1074_jbc_M117_808451
crossref_primary_10_1093_nar_gkx002
crossref_primary_10_1371_journal_pone_0287558
crossref_primary_10_1016_j_jbc_2021_101130
crossref_primary_10_1021_bi300186g
crossref_primary_10_1038_ncomms2041
crossref_primary_10_1016_j_bbcan_2020_188465
crossref_primary_10_1371_journal_pone_0131426
crossref_primary_10_1074_jbc_M114_601658
crossref_primary_10_1016_j_bbrc_2014_11_022
crossref_primary_10_1038_s41467_023_37838_6
crossref_primary_10_1074_mcp_M116_066308
crossref_primary_10_1371_journal_pgen_1003210
crossref_primary_10_3389_fpls_2023_1201129
crossref_primary_10_1042_BCJ20160117
crossref_primary_10_1074_jbc_RA118_005473
crossref_primary_10_1111_febs_12039
crossref_primary_10_1016_j_cellin_2023_100090
crossref_primary_10_1093_nar_gkab088
crossref_primary_10_4161_nucl_25261
crossref_primary_10_1371_journal_pone_0141472
crossref_primary_10_1016_j_cbpa_2012_09_014
crossref_primary_10_1074_jbc_M114_580464
crossref_primary_10_1074_jbc_M115_640037
crossref_primary_10_1126_science_abf3546
crossref_primary_10_1093_nargab_lqab045
crossref_primary_10_1002_pmic_201700300
crossref_primary_10_7554_eLife_43676
crossref_primary_10_1074_jbc_M113_465765
crossref_primary_10_1261_rna_054569_115
crossref_primary_10_1186_s12953_015_0080_7
crossref_primary_10_1016_j_jbc_2021_101230
crossref_primary_10_1128_MCB_01634_13
crossref_primary_10_1074_jbc_M110_200410
crossref_primary_10_1093_pcp_pcv098
crossref_primary_10_1021_acs_jproteome_7b00601
crossref_primary_10_1038_s41586_018_0821_8
crossref_primary_10_1101_gad_350755_123
Cites_doi 10.1126/science.278.5342.1457
10.1515/bchm3.1987.368.2.1607
10.1016/S0021-9673(00)93923-2
10.1016/j.sbi.2003.10.003
10.1016/j.bbrc.2009.12.112
10.1093/nar/gkn642
10.1016/j.febslet.2004.09.080
10.1074/jbc.274.2.814
10.1074/jbc.274.52.37443
10.1038/nrc2876
10.1038/196829a0
10.1006/jmbi.2002.5436
10.1002/yea.1638
10.1016/S0969-2126(03)00071-6
10.1074/jbc.M611896200
10.1016/0304-4165(87)90139-5
10.1074/jbc.M507672200
10.1016/j.jmb.2004.03.076
10.1126/science.1091317
10.1016/0076-6879(84)06033-X
10.1006/jmbi.2000.4136
10.1128/MCB.25.24.10863-10874.2005
10.1074/jbc.M806006200
10.1021/ja00440a033
10.1093/oxfordjournals.jbchem.a123545
10.1042/bj3160285
10.1006/jmbi.2001.5095
10.1111/j.1365-2958.2007.05831.x
10.1074/jbc.271.21.12585
10.1016/j.molcel.2008.12.013
10.1021/ac60255a005
10.1111/j.1432-1033.1994.tb19912.x
10.1074/mcp.M300037-MCP200
10.1007/BF00330833
10.1016/j.mrfmmm.2006.05.041
10.1021/bi100428x
10.1006/abbi.1999.1370
10.1016/j.abb.2010.05.023
10.1093/oxfordjournals.jbchem.a124439
10.1016/S0021-9258(17)40373-5
10.1016/S0021-9258(17)39878-2
10.1534/genetics.167.1.35
10.1016/j.molcel.2007.02.015
10.1074/jbc.M606578200
10.2217/epi.09.3
10.1021/bi00778a005
10.1111/j.1432-1033.1992.tb17423.x
10.1016/j.sbi.2006.10.002
10.1111/j.1432-1033.1981.tb06425.x
10.1093/emboj/19.14.3509
10.1126/science.1117230
10.1073/pnas.0805642105
10.1073/pnas.082119899
10.1021/bi00778a006
10.1146/annurev.biochem.78.070907.103946
10.1038/nmeth.1234
10.1016/j.jmb.2005.03.056
10.1074/jbc.274.52.37035
10.1074/mcp.M900025-MCP200
10.1126/science.1070850
ContentType Journal Article
Copyright 2010 © 2010 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.
2010 by The American Society for Biochemistry and Molecular Biology, Inc.
Copyright_xml – notice: 2010 © 2010 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.
– notice: 2010 by The American Society for Biochemistry and Molecular Biology, Inc.
DBID 6I.
AAFTH
FBQ
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7X8
7TM
M7N
5PM
DOI 10.1074/jbc.M110.170787
DatabaseName ScienceDirect Open Access Titles
Elsevier:ScienceDirect:Open Access
AGRIS
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
MEDLINE - Academic
Nucleic Acids Abstracts
Algology Mycology and Protozoology Abstracts (Microbiology C)
PubMed Central (Full Participant titles)
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
MEDLINE - Academic
Algology Mycology and Protozoology Abstracts (Microbiology C)
Nucleic Acids Abstracts
DatabaseTitleList


Algology Mycology and Protozoology Abstracts (Microbiology C)
MEDLINE
Algology Mycology and Protozoology Abstracts (Microbiology C)
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
– sequence: 3
  dbid: FBQ
  name: AGRIS
  url: http://www.fao.org/agris/Centre.asp?Menu_1ID=DB&Menu_2ID=DB1&Language=EN&Content=http://www.fao.org/agris/search?Language=EN
  sourceTypes: Publisher
DeliveryMethod fulltext_linktorsrc
Discipline Anatomy & Physiology
Chemistry
DocumentTitleAlternate 3-Methylhistidine, a Novel Yeast Post-translational Modification
EISSN 1083-351X
EndPage 37606
ExternalDocumentID 10_1074_jbc_M110_170787
20864530
US201301911469
S0021925820467353
Genre Journal Article
Research Support, N.I.H., Extramural
GrantInformation_xml – fundername: NIGMS NIH HHS
  grantid: R01 GM026020
– fundername: NIGMS NIH HHS
  grantid: GM026020
– fundername: NIGMS NIH HHS
  grantid: R37 GM026020
– fundername: National Institutes of Health
  grantid: GM026020
GroupedDBID ---
-DZ
-ET
-~X
0SF
18M
29J
2WC
34G
39C
4.4
53G
5BI
5GY
5RE
5VS
6I.
79B
85S
AAEDW
AAFTH
AAFWJ
AARDX
AAXUO
ABDNZ
ABOCM
ABPPZ
ABRJW
ACGFO
ACNCT
ADBBV
ADIYS
ADNWM
AENEX
AEXQZ
AFFNX
AFOSN
AFPKN
ALMA_UNASSIGNED_HOLDINGS
AMRAJ
AOIJS
BAWUL
BTFSW
C1A
CJ0
CS3
DIK
DU5
E3Z
EBS
EJD
F5P
FDB
FRP
GROUPED_DOAJ
GX1
HH5
HYE
IH2
KQ8
L7B
N9A
OK1
P-O
P0W
P2P
R.V
RHF
RHI
RNS
ROL
RPM
SJN
TBC
TN5
TR2
UHB
UKR
UPT
VQA
W8F
WH7
WOQ
XFK
XSW
YQT
YSK
YWH
YZZ
ZA5
ZE2
~02
~KM
.55
.GJ
186
3O-
41~
6TJ
AAYJJ
AAYOK
ABFSI
ABPTK
ABTAH
ACSFO
ACYGS
AEQTP
AFDAS
AFMIJ
AI.
E.L
F20
FA8
FBQ
J5H
MVM
NHB
OHT
QZG
UQL
VH1
WHG
X7M
XJT
Y6R
YYP
ZGI
ZY4
0R~
AALRI
ADVLN
AITUG
AKRWK
CGR
CUY
CVF
ECM
EIF
H13
NPM
AAYXX
CITATION
7X8
7TM
M7N
5PM
ID FETCH-LOGICAL-c596t-aad0fb1c4363bafffa64395c3bdad57b25c94fc269fb9985f3d53805b1cfa4023
IEDL.DBID RPM
ISSN 0021-9258
IngestDate Tue Sep 17 21:24:52 EDT 2024
Sat Oct 26 00:17:32 EDT 2024
Fri Oct 25 00:33:25 EDT 2024
Thu Oct 24 22:59:52 EDT 2024
Fri Aug 23 01:00:15 EDT 2024
Sat Sep 28 08:24:45 EDT 2024
Wed Dec 27 19:19:25 EST 2023
Fri Feb 23 02:46:22 EST 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 48
Keywords Protein Methylation
S-adenosylmethionine (SAM)
Translation
Yeast
Actin
Post-translational Modification
Ribosomes
Methyltransferase
Mass Spectrometry (MS)
Covalent Regulation
Language English
License This is an open access article under the CC BY license.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c596t-aad0fb1c4363bafffa64395c3bdad57b25c94fc269fb9985f3d53805b1cfa4023
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ObjectType-Article-2
ObjectType-Feature-1
OpenAccessLink https://dx.doi.org/10.1074/jbc.M110.170787
PMID 20864530
PQID 812134960
PQPubID 23462
PageCount 9
ParticipantIDs pubmedcentral_primary_oai_pubmedcentral_nih_gov_2988365
proquest_miscellaneous_864957390
proquest_miscellaneous_839692361
proquest_miscellaneous_812134960
crossref_primary_10_1074_jbc_M110_170787
pubmed_primary_20864530
fao_agris_US201301911469
elsevier_sciencedirect_doi_10_1074_jbc_M110_170787
PublicationCentury 2000
PublicationDate 2010-11-26
PublicationDateYYYYMMDD 2010-11-26
PublicationDate_xml – month: 11
  year: 2010
  text: 2010-11-26
  day: 26
PublicationDecade 2010
PublicationPlace United States
PublicationPlace_xml – name: United States
– name: 9650 Rockville Pike, Bethesda, MD 20814, U.S.A
PublicationTitle The Journal of biological chemistry
PublicationTitleAlternate J Biol Chem
PublicationYear 2010
Publisher Elsevier Inc
American Society for Biochemistry and Molecular Biology
Publisher_xml – name: Elsevier Inc
– name: American Society for Biochemistry and Molecular Biology
References Couture, Trievel (bib8) 2006; 16
Griffith, Sawaya, Boutz, Thapar, Katz, Clarke, Yeates (bib47) 2001; 313
Grabarse, Mahlert, Shima, Thauer, Ermler (bib25) 2000; 303
Lee, Berger, Martinović, Pasa-Tolić, Anderson, Shen, Zhao, Smith (bib12) 2002; 99
Yao, Grade, Wriggers, Rubenstein (bib4) 1999; 274
Chi, Allis, Wang (bib9) 2010; 10
Zhang, Cheng (bib49) 2003; 11
Nyman, Schüler, Korenbaum, Schutt, Karlsson, Lindberg (bib30) 2002; 317
Tong, Lesage, Bader, Ding, Xu, Xin, Young, Berriz, Brost, Chang, Chen, Cheng, Chua, Friesen, Goldberg, Haynes, Humphries, He, Hussein, Ke, Krogan, Li, Levinson, Lu, Ménard, Munyana, Parsons, Ryan, Tonikian, Roberts, Sdicu, Shapiro, Sheikh, Suter, Wong, Zhang, Zhu, Burd, Munro, Sander, Rine, Greenblatt, Peter, Bretscher, Bell, Roth, Brown, Andrews, Bussey, Boone (bib63) 2004; 303
Porras-Yakushi, Whitelegge, Clarke (bib17) 2007; 282
Huszar, Elzinga (bib20) 1971; 10
Miranda, Lowenson, Clarke (bib40) 2004; 577
Zhang, Zhou, Cheng (bib48) 2000; 19
Nakayama, Tanaka, Yajima, Maita (bib22) 1994; 115
Jorgensen, Nishikawa, Breitkreutz, Tyers (bib59) 2002; 297
Schuwirth, Borovinskaya, Hau, Zhang, Vila-Sanjurjo, Holton, Cate (bib50) 2005; 310
Kleene, Toews, Adler (bib42) 1977; 252
Lhoest, Colson (bib55) 1977; 154
Maita, Miyanishi, Matsuzono, Tanioka, Matsuda (bib21) 1991; 110
Raftery, Harrison, Alewood, Jones, Geczy (bib24) 1996; 316
Sussman, Sellers, Flicker, Lai, Cannon, Szent-Györgyi, Fulton (bib27) 1984; 259
Meyer, Mayr (bib23) 1987; 368
Gary, Lin, Yang, Herschman, Clarke (bib44) 1996; 271
Petrossian, Clarke (bib33) 2009; 1
(bib5) 2006; Vol. 24
Smith, Birchenough (bib34) 1960
Walsh (bib1) 2006
Niewmierzycka, Clarke (bib36) 1999; 274
Raghavan, Lindberg, Schutt (bib32) 1992; 210
Horakova, Deyl (bib41) 1978; 159
Bedford, Clarke (bib3) 2009; 33
Porras-Yakushi, Whitelegge, Clarke (bib16) 2006; 281
Meskauskas, Dinman (bib54) 2008; 36
Klein, Moore, Steitz (bib51) 2004; 340
Vijayasarathy, Rao (bib31) 1987; 923
Lipson, Webb, Clarke (bib18) 2010; 391
Ermler, Grabarse, Shima, Goubeaud, Thauer (bib26) 1997; 278
Bockhorn, Balar, He, Seitomer, Copeland, Kinzy (bib60) 2008; 10
Mosammaparast, Shi (bib10) 2010; 79
Bauer, Schulz (bib64) 1994; 219
Bengtsson, Jeppsson, Sonderegger, Parachin, Sauer, Hahn-Hägerdal, Gorwa-Grauslund (bib61) 2008; 25
Elzinga (bib19) 1971; 10
Lhoest, Colson (bib56) 1981; 121
Katz, Dlakić, Clarke (bib37) 2003; 2
Webb, Lipson, Al-Hadid, Whitelegge, Clarke (bib6) 2010; 49
Xiao, Wilson, Gamblin (bib7) 2003; 13
Petrossian, Clarke (bib38) 2009; 8
Lipson, Webb, Clarke (bib13) 2010; 500
Lesage, Sdicu, Ménard, Shapiro, Hussein, Bussey (bib62) 2004; 167
Gottschling, Freese (bib45) 1962; 196
Paiva, Juliano, Boschcov (bib57) 1976; 98
Clarke, McFadden, O'Connor, Lou (bib43) 1984; 106
Webb, Laganowsky, Whitelegge, Clarke (bib14) 2008; 283
Meskauskas, Dinman (bib53) 2007; 25
Hirs (bib39) 1970
Kalhor, Niewmierzycka, Faull, Yao, Grade, Clarke, Rubenstein (bib29) 1999; 370
Klein, Szczepanik (bib46) 1967; 39
Meskauskas, Petrov, Dinman (bib52) 2005; 25
Porras-Yakushi, Whitelegge, Miranda, Clarke (bib15) 2005; 280
Breslow, Cameron, Collins, Schuldiner, Stewart-Ornstein, Newman, Braun, Madhani, Krogan, Weissman (bib58) 2008; 5
Arnold, Polevoda, Reilly, Sherman (bib35) 1999; 274
Cheng, Zhang (bib2) 2007; 618
Schmitz, Grainger, Howell, Calder, Gaeb, Pinder, Holder, Veigel (bib28) 2005; 349
Polevoda, Sherman (bib11) 2007; 65
Nakayama (10.1074/jbc.M110.170787_bib22) 1994; 115
Vijayasarathy (10.1074/jbc.M110.170787_bib31) 1987; 923
Meyer (10.1074/jbc.M110.170787_bib23) 1987; 368
Raftery (10.1074/jbc.M110.170787_bib24) 1996; 316
Kalhor (10.1074/jbc.M110.170787_bib29) 1999; 370
Mosammaparast (10.1074/jbc.M110.170787_bib10) 2010; 79
Maita (10.1074/jbc.M110.170787_bib21) 1991; 110
Grabarse (10.1074/jbc.M110.170787_bib25) 2000; 303
Hirs (10.1074/jbc.M110.170787_bib39) 1970
Sussman (10.1074/jbc.M110.170787_bib27) 1984; 259
Smith (10.1074/jbc.M110.170787_bib34) 1960
Porras-Yakushi (10.1074/jbc.M110.170787_bib15) 2005; 280
Petrossian (10.1074/jbc.M110.170787_bib38) 2009; 8
Meskauskas (10.1074/jbc.M110.170787_bib52) 2005; 25
(10.1074/jbc.M110.170787_bib5) 2006; Vol. 24
Schuwirth (10.1074/jbc.M110.170787_bib50) 2005; 310
Xiao (10.1074/jbc.M110.170787_bib7) 2003; 13
Lee (10.1074/jbc.M110.170787_bib12) 2002; 99
Kleene (10.1074/jbc.M110.170787_bib42) 1977; 252
Lhoest (10.1074/jbc.M110.170787_bib55) 1977; 154
Walsh (10.1074/jbc.M110.170787_bib1) 2006
Miranda (10.1074/jbc.M110.170787_bib40) 2004; 577
Clarke (10.1074/jbc.M110.170787_bib43) 1984; 106
Jorgensen (10.1074/jbc.M110.170787_bib59) 2002; 297
Lipson (10.1074/jbc.M110.170787_bib13) 2010; 500
Lipson (10.1074/jbc.M110.170787_bib18) 2010; 391
Arnold (10.1074/jbc.M110.170787_bib35) 1999; 274
Lhoest (10.1074/jbc.M110.170787_bib56) 1981; 121
Paiva (10.1074/jbc.M110.170787_bib57) 1976; 98
Meskauskas (10.1074/jbc.M110.170787_bib54) 2008; 36
Gottschling (10.1074/jbc.M110.170787_bib45) 1962; 196
Elzinga (10.1074/jbc.M110.170787_bib19) 1971; 10
Yao (10.1074/jbc.M110.170787_bib4) 1999; 274
Lesage (10.1074/jbc.M110.170787_bib62) 2004; 167
Horakova (10.1074/jbc.M110.170787_bib41) 1978; 159
Polevoda (10.1074/jbc.M110.170787_bib11) 2007; 65
Webb (10.1074/jbc.M110.170787_bib14) 2008; 283
Schmitz (10.1074/jbc.M110.170787_bib28) 2005; 349
Breslow (10.1074/jbc.M110.170787_bib58) 2008; 5
Porras-Yakushi (10.1074/jbc.M110.170787_bib17) 2007; 282
Petrossian (10.1074/jbc.M110.170787_bib33) 2009; 1
Meskauskas (10.1074/jbc.M110.170787_bib53) 2007; 25
Zhang (10.1074/jbc.M110.170787_bib49) 2003; 11
Raghavan (10.1074/jbc.M110.170787_bib32) 1992; 210
Bockhorn (10.1074/jbc.M110.170787_bib60) 2008; 10
Chi (10.1074/jbc.M110.170787_bib9) 2010; 10
Klein (10.1074/jbc.M110.170787_bib51) 2004; 340
Cheng (10.1074/jbc.M110.170787_bib2) 2007; 618
Katz (10.1074/jbc.M110.170787_bib37) 2003; 2
Porras-Yakushi (10.1074/jbc.M110.170787_bib16) 2006; 281
Huszar (10.1074/jbc.M110.170787_bib20) 1971; 10
Zhang (10.1074/jbc.M110.170787_bib48) 2000; 19
Ermler (10.1074/jbc.M110.170787_bib26) 1997; 278
Niewmierzycka (10.1074/jbc.M110.170787_bib36) 1999; 274
Tong (10.1074/jbc.M110.170787_bib63) 2004; 303
Nyman (10.1074/jbc.M110.170787_bib30) 2002; 317
Gary (10.1074/jbc.M110.170787_bib44) 1996; 271
Webb (10.1074/jbc.M110.170787_bib6) 2010; 49
Griffith (10.1074/jbc.M110.170787_bib47) 2001; 313
Klein (10.1074/jbc.M110.170787_bib46) 1967; 39
Bengtsson (10.1074/jbc.M110.170787_bib61) 2008; 25
Bedford (10.1074/jbc.M110.170787_bib3) 2009; 33
Bauer (10.1074/jbc.M110.170787_bib64) 1994; 219
Couture (10.1074/jbc.M110.170787_bib8) 2006; 16
References_xml – volume: 618
  start-page: 102
  year: 2007
  end-page: 115
  ident: bib2
  publication-title: Mut. Res.
  contributor:
    fullname: Zhang
– volume: 110
  start-page: 68
  year: 1991
  end-page: 74
  ident: bib21
  publication-title: J. Biochem.
  contributor:
    fullname: Matsuda
– volume: 159
  start-page: 227
  year: 1978
  end-page: 314
  ident: bib41
  publication-title: J. Chromatogr.
  contributor:
    fullname: Deyl
– volume: 10
  start-page: 17682
  year: 2008
  end-page: 17687
  ident: bib60
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  contributor:
    fullname: Kinzy
– volume: 303
  start-page: 329
  year: 2000
  end-page: 344
  ident: bib25
  publication-title: J. Mol. Biol.
  contributor:
    fullname: Ermler
– volume: 274
  start-page: 814
  year: 1999
  end-page: 824
  ident: bib36
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Clarke
– volume: 259
  start-page: 7349
  year: 1984
  end-page: 7354
  ident: bib27
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Fulton
– volume: 391
  start-page: 1658
  year: 2010
  end-page: 1662
  ident: bib18
  publication-title: Biochem. Biophys. Res. Commun.
  contributor:
    fullname: Clarke
– volume: 278
  start-page: 1457
  year: 1997
  end-page: 1462
  ident: bib26
  publication-title: Science
  contributor:
    fullname: Thauer
– volume: 99
  start-page: 5942
  year: 2002
  end-page: 5947
  ident: bib12
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  contributor:
    fullname: Smith
– volume: 349
  start-page: 113
  year: 2005
  end-page: 125
  ident: bib28
  publication-title: J. Mol. Biol.
  contributor:
    fullname: Veigel
– volume: 317
  start-page: 577
  year: 2002
  end-page: 589
  ident: bib30
  publication-title: J. Mol. Biol.
  contributor:
    fullname: Lindberg
– volume: 303
  start-page: 808
  year: 2004
  end-page: 813
  ident: bib63
  publication-title: Science
  contributor:
    fullname: Boone
– volume: 36
  start-page: 6175
  year: 2008
  end-page: 6186
  ident: bib54
  publication-title: Nucleic Acids Res.
  contributor:
    fullname: Dinman
– volume: 196
  start-page: 829
  year: 1962
  end-page: 831
  ident: bib45
  publication-title: Nature
  contributor:
    fullname: Freese
– volume: 370
  start-page: 105
  year: 1999
  end-page: 111
  ident: bib29
  publication-title: Arch. Biochem. Biophys.
  contributor:
    fullname: Rubenstein
– volume: 154
  start-page: 175
  year: 1977
  end-page: 180
  ident: bib55
  publication-title: Mol. Gen. Genetics
  contributor:
    fullname: Colson
– volume: 10
  start-page: 229
  year: 1971
  end-page: 236
  ident: bib20
  publication-title: Biochemistry
  contributor:
    fullname: Elzinga
– volume: 79
  start-page: 155
  year: 2010
  end-page: 179
  ident: bib10
  publication-title: Annu. Rev. Biochem.
  contributor:
    fullname: Shi
– volume: 252
  start-page: 3214
  year: 1977
  end-page: 3218
  ident: bib42
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Adler
– start-page: 121
  year: 2006
  end-page: 149
  ident: bib1
  publication-title: Post-translational Modification of Proteins: Expanding Nature's Inventory
  contributor:
    fullname: Walsh
– volume: 280
  start-page: 34590
  year: 2005
  end-page: 34598
  ident: bib15
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Clarke
– volume: 33
  start-page: 1
  year: 2009
  end-page: 13
  ident: bib3
  publication-title: Mol. Cell
  contributor:
    fullname: Clarke
– volume: 274
  start-page: 37443
  year: 1999
  end-page: 37449
  ident: bib4
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Rubenstein
– volume: 10
  start-page: 224
  year: 1971
  end-page: 229
  ident: bib19
  publication-title: Biochemistry
  contributor:
    fullname: Elzinga
– volume: 25
  start-page: 835
  year: 2008
  end-page: 847
  ident: bib61
  publication-title: Yeast
  contributor:
    fullname: Gorwa-Grauslund
– volume: 219
  start-page: 43
  year: 1994
  end-page: 47
  ident: bib64
  publication-title: Eur. J. Biochem.
  contributor:
    fullname: Schulz
– volume: 2
  start-page: 525
  year: 2003
  end-page: 540
  ident: bib37
  publication-title: Mol. Cell Proteomics
  contributor:
    fullname: Clarke
– volume: 297
  start-page: 395
  year: 2002
  end-page: 400
  ident: bib59
  publication-title: Science
  contributor:
    fullname: Tyers
– volume: 282
  start-page: 12368
  year: 2007
  end-page: 12376
  ident: bib17
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Clarke
– volume: 310
  start-page: 827
  year: 2005
  end-page: 834
  ident: bib50
  publication-title: Science
  contributor:
    fullname: Cate
– volume: 577
  start-page: 181
  year: 2004
  end-page: 186
  ident: bib40
  publication-title: FEBS Lett.
  contributor:
    fullname: Clarke
– volume: 281
  start-page: 35835
  year: 2006
  end-page: 35845
  ident: bib16
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Clarke
– volume: 39
  start-page: 1276
  year: 1967
  end-page: 1281
  ident: bib46
  publication-title: Anal. Chem.
  contributor:
    fullname: Szczepanik
– volume: 167
  start-page: 35
  year: 2004
  end-page: 49
  ident: bib62
  publication-title: Genetics
  contributor:
    fullname: Bussey
– volume: 121
  start-page: 33
  year: 1981
  end-page: 37
  ident: bib56
  publication-title: Eur. J. Biochem.
  contributor:
    fullname: Colson
– start-page: C-125
  year: 1970
  ident: bib39
  publication-title: Handbook of Biochemistry: Selected Data for Molecular Biology
  contributor:
    fullname: Hirs
– volume: 25
  start-page: 10863
  year: 2005
  end-page: 10874
  ident: bib52
  publication-title: Mol. Cell Biol.
  contributor:
    fullname: Dinman
– volume: 16
  start-page: 753
  year: 2006
  end-page: 760
  ident: bib8
  publication-title: Curr. Opin. Struct. Biol.
  contributor:
    fullname: Trievel
– volume: 283
  start-page: 35561
  year: 2008
  end-page: 35568
  ident: bib14
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Clarke
– volume: 106
  start-page: 330
  year: 1984
  end-page: 344
  ident: bib43
  publication-title: Methods Enzymol.
  contributor:
    fullname: Lou
– volume: 10
  start-page: 457
  year: 2010
  end-page: 469
  ident: bib9
  publication-title: Nat. Rev. Cancer
  contributor:
    fullname: Wang
– volume: 500
  start-page: 137
  year: 2010
  end-page: 143
  ident: bib13
  publication-title: Arch. Biochem. Biophys.
  contributor:
    fullname: Clarke
– volume: 19
  start-page: 3509
  year: 2000
  end-page: 3519
  ident: bib48
  publication-title: EMBO J.
  contributor:
    fullname: Cheng
– volume: 13
  start-page: 699
  year: 2003
  end-page: 705
  ident: bib7
  publication-title: Curr. Opin. Struct. Biol.
  contributor:
    fullname: Gamblin
– start-page: 212
  year: 1960
  end-page: 221
  ident: bib34
  publication-title: Chromatographic and Electrophoretic Techniques, Volume I, Chromatography
  contributor:
    fullname: Birchenough
– volume: 5
  start-page: 711
  year: 2008
  end-page: 718
  ident: bib58
  publication-title: Nature Methods
  contributor:
    fullname: Weissman
– volume: 25
  start-page: 877
  year: 2007
  end-page: 888
  ident: bib53
  publication-title: Mol. Cell
  contributor:
    fullname: Dinman
– volume: 274
  start-page: 37035
  year: 1999
  end-page: 37040
  ident: bib35
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Sherman
– volume: 340
  start-page: 141
  year: 2004
  end-page: 177
  ident: bib51
  publication-title: J. Mol. Biol.
  contributor:
    fullname: Steitz
– volume: 923
  start-page: 156
  year: 1987
  end-page: 165
  ident: bib31
  publication-title: Biochim. Biophys. Acta
  contributor:
    fullname: Rao
– volume: 271
  start-page: 12585
  year: 1996
  end-page: 12594
  ident: bib44
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Clarke
– volume: 115
  start-page: 909
  year: 1994
  end-page: 926
  ident: bib22
  publication-title: J. Biochem.
  contributor:
    fullname: Maita
– volume: 1
  start-page: 163
  year: 2009
  end-page: 175
  ident: bib33
  publication-title: Epigenomics
  contributor:
    fullname: Clarke
– volume: 316
  start-page: 285
  year: 1996
  end-page: 293
  ident: bib24
  publication-title: Biochem. J.
  contributor:
    fullname: Geczy
– volume: 49
  start-page: 5225
  year: 2010
  end-page: 5235
  ident: bib6
  publication-title: Biochemistry
  contributor:
    fullname: Clarke
– volume: 11
  start-page: 509
  year: 2003
  end-page: 520
  ident: bib49
  publication-title: Structure
  contributor:
    fullname: Cheng
– volume: 8
  start-page: 1516
  year: 2009
  end-page: 1526
  ident: bib38
  publication-title: Mol. Cell Proteomics
  contributor:
    fullname: Clarke
– volume: 98
  start-page: 7645
  year: 1976
  end-page: 7648
  ident: bib57
  publication-title: J. Amer. Chem. Soc.
  contributor:
    fullname: Boschcov
– volume: 313
  start-page: 1103
  year: 2001
  end-page: 1116
  ident: bib47
  publication-title: J. Mol. Biol.
  contributor:
    fullname: Yeates
– volume: 210
  start-page: 311
  year: 1992
  end-page: 318
  ident: bib32
  publication-title: Eur. J. Biochem.
  contributor:
    fullname: Schutt
– volume: 368
  start-page: 1607
  year: 1987
  end-page: 1611
  ident: bib23
  publication-title: Biol. Chem. Hoppe Seyler
  contributor:
    fullname: Mayr
– volume: Vol. 24
  start-page: 3
  year: 2006
  end-page: 493
  ident: bib5
  publication-title: The Enzymes, Third Edition
– volume: 65
  start-page: 590
  year: 2007
  end-page: 606
  ident: bib11
  publication-title: Mol. Microbiol.
  contributor:
    fullname: Sherman
– volume: 278
  start-page: 1457
  year: 1997
  ident: 10.1074/jbc.M110.170787_bib26
  publication-title: Science
  doi: 10.1126/science.278.5342.1457
  contributor:
    fullname: Ermler
– volume: 368
  start-page: 1607
  year: 1987
  ident: 10.1074/jbc.M110.170787_bib23
  publication-title: Biol. Chem. Hoppe Seyler
  doi: 10.1515/bchm3.1987.368.2.1607
  contributor:
    fullname: Meyer
– volume: 159
  start-page: 227
  year: 1978
  ident: 10.1074/jbc.M110.170787_bib41
  publication-title: J. Chromatogr.
  doi: 10.1016/S0021-9673(00)93923-2
  contributor:
    fullname: Horakova
– volume: 13
  start-page: 699
  year: 2003
  ident: 10.1074/jbc.M110.170787_bib7
  publication-title: Curr. Opin. Struct. Biol.
  doi: 10.1016/j.sbi.2003.10.003
  contributor:
    fullname: Xiao
– volume: 391
  start-page: 1658
  year: 2010
  ident: 10.1074/jbc.M110.170787_bib18
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2009.12.112
  contributor:
    fullname: Lipson
– volume: 36
  start-page: 6175
  year: 2008
  ident: 10.1074/jbc.M110.170787_bib54
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkn642
  contributor:
    fullname: Meskauskas
– volume: 577
  start-page: 181
  year: 2004
  ident: 10.1074/jbc.M110.170787_bib40
  publication-title: FEBS Lett.
  doi: 10.1016/j.febslet.2004.09.080
  contributor:
    fullname: Miranda
– volume: 274
  start-page: 814
  year: 1999
  ident: 10.1074/jbc.M110.170787_bib36
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.274.2.814
  contributor:
    fullname: Niewmierzycka
– volume: 274
  start-page: 37443
  year: 1999
  ident: 10.1074/jbc.M110.170787_bib4
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.274.52.37443
  contributor:
    fullname: Yao
– volume: 10
  start-page: 457
  year: 2010
  ident: 10.1074/jbc.M110.170787_bib9
  publication-title: Nat. Rev. Cancer
  doi: 10.1038/nrc2876
  contributor:
    fullname: Chi
– volume: 196
  start-page: 829
  year: 1962
  ident: 10.1074/jbc.M110.170787_bib45
  publication-title: Nature
  doi: 10.1038/196829a0
  contributor:
    fullname: Gottschling
– volume: 317
  start-page: 577
  year: 2002
  ident: 10.1074/jbc.M110.170787_bib30
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.2002.5436
  contributor:
    fullname: Nyman
– volume: 25
  start-page: 835
  year: 2008
  ident: 10.1074/jbc.M110.170787_bib61
  publication-title: Yeast
  doi: 10.1002/yea.1638
  contributor:
    fullname: Bengtsson
– volume: 11
  start-page: 509
  year: 2003
  ident: 10.1074/jbc.M110.170787_bib49
  publication-title: Structure
  doi: 10.1016/S0969-2126(03)00071-6
  contributor:
    fullname: Zhang
– volume: 282
  start-page: 12368
  year: 2007
  ident: 10.1074/jbc.M110.170787_bib17
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M611896200
  contributor:
    fullname: Porras-Yakushi
– volume: 923
  start-page: 156
  year: 1987
  ident: 10.1074/jbc.M110.170787_bib31
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0304-4165(87)90139-5
  contributor:
    fullname: Vijayasarathy
– volume: 280
  start-page: 34590
  year: 2005
  ident: 10.1074/jbc.M110.170787_bib15
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M507672200
  contributor:
    fullname: Porras-Yakushi
– volume: 340
  start-page: 141
  year: 2004
  ident: 10.1074/jbc.M110.170787_bib51
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2004.03.076
  contributor:
    fullname: Klein
– volume: 303
  start-page: 808
  year: 2004
  ident: 10.1074/jbc.M110.170787_bib63
  publication-title: Science
  doi: 10.1126/science.1091317
  contributor:
    fullname: Tong
– volume: 106
  start-page: 330
  year: 1984
  ident: 10.1074/jbc.M110.170787_bib43
  publication-title: Methods Enzymol.
  doi: 10.1016/0076-6879(84)06033-X
  contributor:
    fullname: Clarke
– start-page: 212
  year: 1960
  ident: 10.1074/jbc.M110.170787_bib34
  contributor:
    fullname: Smith
– volume: 303
  start-page: 329
  year: 2000
  ident: 10.1074/jbc.M110.170787_bib25
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.2000.4136
  contributor:
    fullname: Grabarse
– volume: 25
  start-page: 10863
  year: 2005
  ident: 10.1074/jbc.M110.170787_bib52
  publication-title: Mol. Cell Biol.
  doi: 10.1128/MCB.25.24.10863-10874.2005
  contributor:
    fullname: Meskauskas
– volume: 283
  start-page: 35561
  year: 2008
  ident: 10.1074/jbc.M110.170787_bib14
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M806006200
  contributor:
    fullname: Webb
– volume: 98
  start-page: 7645
  year: 1976
  ident: 10.1074/jbc.M110.170787_bib57
  publication-title: J. Amer. Chem. Soc.
  doi: 10.1021/ja00440a033
  contributor:
    fullname: Paiva
– volume: 110
  start-page: 68
  year: 1991
  ident: 10.1074/jbc.M110.170787_bib21
  publication-title: J. Biochem.
  doi: 10.1093/oxfordjournals.jbchem.a123545
  contributor:
    fullname: Maita
– volume: 316
  start-page: 285
  year: 1996
  ident: 10.1074/jbc.M110.170787_bib24
  publication-title: Biochem. J.
  doi: 10.1042/bj3160285
  contributor:
    fullname: Raftery
– volume: 313
  start-page: 1103
  year: 2001
  ident: 10.1074/jbc.M110.170787_bib47
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.2001.5095
  contributor:
    fullname: Griffith
– volume: 65
  start-page: 590
  year: 2007
  ident: 10.1074/jbc.M110.170787_bib11
  publication-title: Mol. Microbiol.
  doi: 10.1111/j.1365-2958.2007.05831.x
  contributor:
    fullname: Polevoda
– volume: 271
  start-page: 12585
  year: 1996
  ident: 10.1074/jbc.M110.170787_bib44
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.271.21.12585
  contributor:
    fullname: Gary
– volume: 33
  start-page: 1
  year: 2009
  ident: 10.1074/jbc.M110.170787_bib3
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2008.12.013
  contributor:
    fullname: Bedford
– volume: 39
  start-page: 1276
  year: 1967
  ident: 10.1074/jbc.M110.170787_bib46
  publication-title: Anal. Chem.
  doi: 10.1021/ac60255a005
  contributor:
    fullname: Klein
– volume: 219
  start-page: 43
  year: 1994
  ident: 10.1074/jbc.M110.170787_bib64
  publication-title: Eur. J. Biochem.
  doi: 10.1111/j.1432-1033.1994.tb19912.x
  contributor:
    fullname: Bauer
– volume: 2
  start-page: 525
  year: 2003
  ident: 10.1074/jbc.M110.170787_bib37
  publication-title: Mol. Cell Proteomics
  doi: 10.1074/mcp.M300037-MCP200
  contributor:
    fullname: Katz
– volume: Vol. 24
  start-page: 3
  year: 2006
  ident: 10.1074/jbc.M110.170787_bib5
– volume: 154
  start-page: 175
  year: 1977
  ident: 10.1074/jbc.M110.170787_bib55
  publication-title: Mol. Gen. Genetics
  doi: 10.1007/BF00330833
  contributor:
    fullname: Lhoest
– volume: 618
  start-page: 102
  year: 2007
  ident: 10.1074/jbc.M110.170787_bib2
  publication-title: Mut. Res.
  doi: 10.1016/j.mrfmmm.2006.05.041
  contributor:
    fullname: Cheng
– volume: 49
  start-page: 5225
  year: 2010
  ident: 10.1074/jbc.M110.170787_bib6
  publication-title: Biochemistry
  doi: 10.1021/bi100428x
  contributor:
    fullname: Webb
– volume: 370
  start-page: 105
  year: 1999
  ident: 10.1074/jbc.M110.170787_bib29
  publication-title: Arch. Biochem. Biophys.
  doi: 10.1006/abbi.1999.1370
  contributor:
    fullname: Kalhor
– volume: 500
  start-page: 137
  year: 2010
  ident: 10.1074/jbc.M110.170787_bib13
  publication-title: Arch. Biochem. Biophys.
  doi: 10.1016/j.abb.2010.05.023
  contributor:
    fullname: Lipson
– volume: 115
  start-page: 909
  year: 1994
  ident: 10.1074/jbc.M110.170787_bib22
  publication-title: J. Biochem.
  doi: 10.1093/oxfordjournals.jbchem.a124439
  contributor:
    fullname: Nakayama
– volume: 252
  start-page: 3214
  year: 1977
  ident: 10.1074/jbc.M110.170787_bib42
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(17)40373-5
  contributor:
    fullname: Kleene
– volume: 259
  start-page: 7349
  year: 1984
  ident: 10.1074/jbc.M110.170787_bib27
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(17)39878-2
  contributor:
    fullname: Sussman
– volume: 167
  start-page: 35
  year: 2004
  ident: 10.1074/jbc.M110.170787_bib62
  publication-title: Genetics
  doi: 10.1534/genetics.167.1.35
  contributor:
    fullname: Lesage
– volume: 25
  start-page: 877
  year: 2007
  ident: 10.1074/jbc.M110.170787_bib53
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2007.02.015
  contributor:
    fullname: Meskauskas
– volume: 281
  start-page: 35835
  year: 2006
  ident: 10.1074/jbc.M110.170787_bib16
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M606578200
  contributor:
    fullname: Porras-Yakushi
– volume: 1
  start-page: 163
  year: 2009
  ident: 10.1074/jbc.M110.170787_bib33
  publication-title: Epigenomics
  doi: 10.2217/epi.09.3
  contributor:
    fullname: Petrossian
– volume: 10
  start-page: 224
  year: 1971
  ident: 10.1074/jbc.M110.170787_bib19
  publication-title: Biochemistry
  doi: 10.1021/bi00778a005
  contributor:
    fullname: Elzinga
– volume: 210
  start-page: 311
  year: 1992
  ident: 10.1074/jbc.M110.170787_bib32
  publication-title: Eur. J. Biochem.
  doi: 10.1111/j.1432-1033.1992.tb17423.x
  contributor:
    fullname: Raghavan
– volume: 16
  start-page: 753
  year: 2006
  ident: 10.1074/jbc.M110.170787_bib8
  publication-title: Curr. Opin. Struct. Biol.
  doi: 10.1016/j.sbi.2006.10.002
  contributor:
    fullname: Couture
– volume: 121
  start-page: 33
  year: 1981
  ident: 10.1074/jbc.M110.170787_bib56
  publication-title: Eur. J. Biochem.
  doi: 10.1111/j.1432-1033.1981.tb06425.x
  contributor:
    fullname: Lhoest
– start-page: C-125
  year: 1970
  ident: 10.1074/jbc.M110.170787_bib39
  contributor:
    fullname: Hirs
– start-page: 121
  year: 2006
  ident: 10.1074/jbc.M110.170787_bib1
  contributor:
    fullname: Walsh
– volume: 19
  start-page: 3509
  year: 2000
  ident: 10.1074/jbc.M110.170787_bib48
  publication-title: EMBO J.
  doi: 10.1093/emboj/19.14.3509
  contributor:
    fullname: Zhang
– volume: 310
  start-page: 827
  year: 2005
  ident: 10.1074/jbc.M110.170787_bib50
  publication-title: Science
  doi: 10.1126/science.1117230
  contributor:
    fullname: Schuwirth
– volume: 10
  start-page: 17682
  year: 2008
  ident: 10.1074/jbc.M110.170787_bib60
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  doi: 10.1073/pnas.0805642105
  contributor:
    fullname: Bockhorn
– volume: 99
  start-page: 5942
  year: 2002
  ident: 10.1074/jbc.M110.170787_bib12
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  doi: 10.1073/pnas.082119899
  contributor:
    fullname: Lee
– volume: 10
  start-page: 229
  year: 1971
  ident: 10.1074/jbc.M110.170787_bib20
  publication-title: Biochemistry
  doi: 10.1021/bi00778a006
  contributor:
    fullname: Huszar
– volume: 79
  start-page: 155
  year: 2010
  ident: 10.1074/jbc.M110.170787_bib10
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev.biochem.78.070907.103946
  contributor:
    fullname: Mosammaparast
– volume: 5
  start-page: 711
  year: 2008
  ident: 10.1074/jbc.M110.170787_bib58
  publication-title: Nature Methods
  doi: 10.1038/nmeth.1234
  contributor:
    fullname: Breslow
– volume: 349
  start-page: 113
  year: 2005
  ident: 10.1074/jbc.M110.170787_bib28
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2005.03.056
  contributor:
    fullname: Schmitz
– volume: 274
  start-page: 37035
  year: 1999
  ident: 10.1074/jbc.M110.170787_bib35
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.274.52.37035
  contributor:
    fullname: Arnold
– volume: 8
  start-page: 1516
  year: 2009
  ident: 10.1074/jbc.M110.170787_bib38
  publication-title: Mol. Cell Proteomics
  doi: 10.1074/mcp.M900025-MCP200
  contributor:
    fullname: Petrossian
– volume: 297
  start-page: 395
  year: 2002
  ident: 10.1074/jbc.M110.170787_bib59
  publication-title: Science
  doi: 10.1126/science.1070850
  contributor:
    fullname: Jorgensen
SSID ssj0000491
Score 2.3163683
Snippet We have shown that Rpl3, a protein of the large ribosomal subunit from baker's yeast (Saccharomyces cerevisiae), is stoichiometrically monomethylated at...
We have shown that Rpl3, a protein of the large ribosomal subunit from baker's yeast ( Saccharomyces cerevisiae ), is stoichiometrically monomethylated at...
SourceID pubmedcentral
proquest
crossref
pubmed
fao
elsevier
SourceType Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 37598
SubjectTerms Actin
Amino Acid Sequence
Covalent Regulation
Mass Spectrometry (MS)
Methylhistidines - metabolism
Methyltransferase
Methyltransferases - chemistry
Methyltransferases - genetics
Methyltransferases - metabolism
Molecular Sequence Data
Post-translational Modification
Protein Methylation
Protein Synthesis and Degradation
Ribosomal Proteins - genetics
Ribosomal Proteins - metabolism
Ribosomes
S-adenosylmethionine (SAM)
Saccharomyces cerevisiae
Saccharomyces cerevisiae - chemistry
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Sequence Alignment
Translation
Yeast
Title A Novel 3-Methylhistidine Modification of Yeast Ribosomal Protein Rpl3 Is Dependent upon the YIL110W Methyltransferase
URI https://dx.doi.org/10.1074/jbc.M110.170787
https://www.ncbi.nlm.nih.gov/pubmed/20864530
https://search.proquest.com/docview/812134960
https://search.proquest.com/docview/839692361
https://search.proquest.com/docview/864957390
https://pubmed.ncbi.nlm.nih.gov/PMC2988365
Volume 285
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3Pb9MwGLXWXeCC2Aas_Jh8QIhL2sY_kvhYFaYNyDQGFdvJsh17BLVJtaaT9t_z2UkmhsYOSL1UtdNEz_b3PfvlfQi9dYYzxZSJIJRYIChMR0oXcWSZhdWPUmKc3xrIT5KjOft0zs-3EO_fhQmifaPLUbVYjqryZ9BWrpZm3OvExqf5jIgsowkfD9AgpbSn6P3yy7oyeV57QHjW-_mkbPxLm1Ee-2_e48bX3yOQ0TPuJdD3R6WBU_V9ueffEso_YtLhU_SkSybxtL3pHbRlq120N62ASC9v8Dsc5J1h33wXPZr1pd320PUUn9TXdoFplFtAauFdh0uIYhbndeHFQwEvXDt84Wv74LNS1-t6Cf916n0dygqfrRYUH6_xh66IboM3K-gB6SS-OP4CT_8Dt5duQmZsryBaPkPzw4_fZ0dRV4AhMlwkTaRUMXE6NowmVCvnnPL5CzdUF6rgqSbcCOYMSYTTQNu4owWsnxMOXZwCYkqfo-2qruw-ws6ITDNBChgSLKEmy4DoTJiBT0q04EP0vgdArlqfDRnOx1MmATbpYZMtbENEeoBklya04V9CFPh3p32AUqpLWDrl_BvxB7ZAVSFOiCHCPb4ScPAHJqqy9WYts-B3BxzvgSZUJMIb2DzQJAESmlIBV3nRDprbJ-yH3xCld4bTbQNv_n33F5gTwQS8mwMv_7vnK_Q4KCHiOCLJa7TdXG3sG0iwGn2ABp-_ZgdhWv0GExgkuA
link.rule.ids 230,315,733,786,790,891,27955,27956,53825,53827
linkProvider National Library of Medicine
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1bb9MwGLW28TBeuGzAytUPCPGStvEll8eqMLXQVNNYYXuybCeGQptUazoJfj2fnXhi05gEUl-i2Kkcn_j7TnxyPoReG82ZZFIHEEoKIChMBVLlYVCwAlY_Sok29tVANo1GM_bhlJ9uIe6_hXGifa3m3XKx7Jbzb05buVrqnteJ9Y6yIUmThEa8t43uwPNKuCfpfgFmbaE8qz4gPPGOPjHrfVe6m4X2yLrc2Ap8BHJ6xq0I-ua4tG1kdVP2eV1E-UdUOryPPvvxNGKUH91Nrbr61zWrx38e8AN0r81T8aA5_RBtFeUe2h-UwNGXP_Eb7JSj7pX8Htod-qpx--higKfVRbHANMgKAMHCGhrPIUAWOKtyq0tyUMCVwWe2bBA-nqtqXS3hv46sZcS8xMerBcXjNX7X1uet8WYFPSBTxWfjCdzWL7i5dO2S7uIcAvEjNDt8fzIcBW1th0DzNKoDKfO-UaFmNKJKGmOkTY24piqXOY8V4TplRpMoNQoYITc0h6nuc-hiJHBe-hjtlFVZHCBsdJoolpIc0MYiqpMEOFSfafjFRKW8g976mRWrxsJDuK33mAnAg7B4EA0eOoj4mRdtBtJkFgICzN87HQBGhPwKq7KYfSJ2LxhYMISgtIOwB46AebB7MbIsqs1aJM5KD-jjLU1oGqXWG-eWJhHw25imcJUnDRovR-hx3UHxFZxeNrC-4lfPAPqcv3iLtqf_3fMV2h2dZBMxGU8_PkN3neAiDAMSPUc79fmmeAF5XK1euqf2N4ZwRcI
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1bb9MwGLXYkIAXLhuwcvUDQrykF1-S-LHqqFZYq2pQsfFi2Y4NhTap1nQS_Ho-O8m0TWMPk_ISxU7k-MTfd-Kj8yH0zhnOFFMmglBigaAwHSmd9SLLLKx-lBLj_K-B8SQ-mLFPx_z4QqmvINo3et7OF8t2Pv8ZtJWrpek0OrHOdDwgIk1pzDurzHW20F34ZknSEPVmEWZ1sTyvQCA8bVx9Etb5pU173PNn3unGV-EjkNcz7oXQ18emLaeK6zLQq0LKC5Fp-Ah9b8ZUCVJ-tzelbpu_V-webzXox-hhna_iftXkCbpj8x2028-Bqy__4Pc4KEjDr_kddH_QVI_bRWd9PCnO7ALTaGwBDAtvbDyHQGnxuMi8PilAAhcOn_jyQfhorot1sYRnTb11xDzHR6sFxaM13q_r9JZ4s4IekLHik9EhvNpvuLp1GZJvewoB-SmaDT9-HRxEdY2HyHARl5FSWdfpnmE0plo555RPkbihOlMZTzThRjBnSCycBmbIHc1gurscujgF3Jc-Q9t5kds9hJ0RqWaCZIA6FlOTpsCluszAkRAteAt9aGZXriorDxm24BMmARPSY0JWmGgh0sy-rDORKsOQEGj-32kPcCLVD1id5ewL8XvCwIYhFIkWwg14JMyD35NRuS02a5kGSz2gkTc0oSIW3iPnhiYx8NyECrjL8wqR5yNssN1CySWsnjfw_uKXrwACg894jbgXt-75Ft2b7g_l4Wjy-SV6EHQXvV5E4ldouzzd2NeQzpX6Tfhw_wGxP0hC
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=A+Novel+3-Methylhistidine+Modification+of+Yeast+Ribosomal+Protein+Rpl3+Is+Dependent+upon+the+YIL110W+Methyltransferase&rft.jtitle=The+Journal+of+biological+chemistry&rft.au=Webb%2C+Kristofor+J.&rft.au=Zurita-Lopez%2C+Cecilia+I.&rft.au=Al-Hadid%2C+Qais&rft.au=Laganowsky%2C+Arthur&rft.date=2010-11-26&rft.pub=American+Society+for+Biochemistry+and+Molecular+Biology&rft.issn=0021-9258&rft.eissn=1083-351X&rft.volume=285&rft.issue=48&rft.spage=37598&rft.epage=37606&rft_id=info:doi/10.1074%2Fjbc.M110.170787&rft_id=info%3Apmid%2F20864530&rft.externalDBID=PMC2988365
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0021-9258&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0021-9258&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0021-9258&client=summon