The catalytic activity of the translation termination factor methyltransferase Mtq2-Trm112 complex is required for large ribosomal subunit biogenesis.
Binding Sites
Biocatalysis
Cloning, Molecular
Crystallography, X-Ray
Escherichia coli
/ genetics
Gene Expression Regulation, Fungal
Genetic Vectors
/ chemistry
Methyltransferases
/ chemistry
Models, Molecular
Organelle Biogenesis
Peptide Chain Termination, Translational
Peptide Termination Factors
/ genetics
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
RNA, Ribosomal
/ biosynthesis
RNA, Ribosomal, 5.8S
/ biosynthesis
Recombinant Proteins
/ chemistry
Ribosome Subunits, Large, Eukaryotic
/ genetics
Saccharomyces cerevisiae
/ genetics
Saccharomyces cerevisiae Proteins
/ chemistry
Substrate Specificity
tRNA Methyltransferases
/ chemistry
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
02 12 2020
02 12 2020
Historique:
accepted:
09
10
2020
revised:
05
10
2020
received:
14
02
2019
pubmed:
10
11
2020
medline:
30
12
2020
entrez:
9
11
2020
Statut:
ppublish
Résumé
The Mtq2-Trm112 methyltransferase modifies the eukaryotic translation termination factor eRF1 on the glutamine side chain of a universally conserved GGQ motif that is essential for release of newly synthesized peptides. Although this modification is found in the three domains of life, its exact role in eukaryotes remains unknown. As the deletion of MTQ2 leads to severe growth impairment in yeast, we have investigated its role further and tested its putative involvement in ribosome biogenesis. We found that Mtq2 is associated with nuclear 60S subunit precursors, and we demonstrate that its catalytic activity is required for nucleolar release of pre-60S and for efficient production of mature 5.8S and 25S rRNAs. Thus, we identify Mtq2 as a novel ribosome assembly factor important for large ribosomal subunit formation. We propose that Mtq2-Trm112 might modify eRF1 in the nucleus as part of a quality control mechanism aimed at proof-reading the peptidyl transferase center, where it will subsequently bind during translation termination.
Identifiants
pubmed: 33166396
pii: 5964072
doi: 10.1093/nar/gkaa972
pmc: PMC7708063
doi:
Substances chimiques
Peptide Termination Factors
0
RNA, Ribosomal
0
RNA, Ribosomal, 5.8S
0
Recombinant Proteins
0
SUP45 protein, S cerevisiae
0
Saccharomyces cerevisiae Proteins
0
RNA, ribosomal, 25S
130527-23-0
MTQ2 protein, S cerevisiae
EC 2.1.1.-
Methyltransferases
EC 2.1.1.-
tRNA Methyltransferases
EC 2.1.1.-
Trm112 protein, S cerevisiae
EC 2.1.1.214
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
12310-12325Informations de copyright
© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.
Références
Genes Dev. 2009 Apr 15;23(8):963-74
pubmed: 19390089
Proc Natl Acad Sci U S A. 2014 Dec 23;111(51):E5518-26
pubmed: 25489090
Biochem J. 2017 Jan 15;474(2):195-214
pubmed: 28062837
Nucleic Acids Res. 2015 Feb 27;43(4):2242-58
pubmed: 25653167
FEBS Lett. 2006 May 29;580(13):3179-84
pubmed: 16684535
Biochimie. 2012 Jul;94(7):1521-32
pubmed: 22342225
Methods Enzymol. 2008;447:65-82
pubmed: 19161838
Annu Rev Biochem. 2019 Jun 20;88:281-306
pubmed: 30566372
Nucleic Acids Res. 2017 May 5;45(8):4853-4865
pubmed: 28115637
Mol Cell Biol. 2008 May;28(10):3151-61
pubmed: 18332120
Mol Biol Rep. 2009 Nov;36(8):2221-8
pubmed: 19116772
Nucleic Acids Res. 2011 Aug;39(14):6249-59
pubmed: 21478168
Biochemistry. 2003 May 20;42(19):5592-9
pubmed: 12741815
Nucleic Acids Res. 2018 Sep 19;46(16):8483-8499
pubmed: 30010922
Mol Cell. 2005 Dec 22;20(6):917-27
pubmed: 16364916
Science. 2016 Jun 17;352(6292):1408-12
pubmed: 27313037
J Mol Biol. 1998 Dec 4;284(3):579-90
pubmed: 9826500
J Biol Chem. 2007 Dec 7;282(49):35638-45
pubmed: 17932046
Methods. 2001 Jul;24(3):218-29
pubmed: 11403571
Proc Natl Acad Sci U S A. 2002 Feb 5;99(3):1473-8
pubmed: 11805295
Trends Biochem Sci. 2010 May;35(5):267-77
pubmed: 20097077
Mol Cell Proteomics. 2016 Jan;15(1):164-76
pubmed: 26545399
Yeast. 2006 Aug;23(11):825-31
pubmed: 16921548
Trends Biochem Sci. 2002 Jul;27(7):344-51
pubmed: 12114023
Nucleic Acids Res. 2017 Jan 4;45(D1):D1100-D1106
pubmed: 27924013
Yeast. 1998 Jul;14(10):953-61
pubmed: 9717241
J Biol Chem. 2006 Feb 3;281(5):2562-71
pubmed: 16321977
Mol Cell Biol. 2000 Feb;20(4):1370-81
pubmed: 10648622
Mol Cell Biol. 2012 Jun;32(12):2254-67
pubmed: 22493060
RNA Biol. 2017 Sep 2;14(9):1138-1152
pubmed: 27911188
Genes Dev. 1995 Oct 15;9(20):2470-81
pubmed: 7590228
Cell. 2001 May 18;105(4):499-509
pubmed: 11371346
Nature. 2003 Oct 16;425(6959):737-41
pubmed: 14562106
Nucleic Acids Res. 2014 Sep;42(15):10005-22
pubmed: 25013175
Cell. 1978 Feb;13(2):329-34
pubmed: 75070
Proc Natl Acad Sci U S A. 2017 Dec 19;114(51):E10899-E10908
pubmed: 29208708
PLoS One. 2015 Jun 26;10(6):e0131426
pubmed: 26115316
Biochem Biophys Res Commun. 2016 Feb 12;470(3):552-557
pubmed: 26801560
Mol Cell Biol. 1992 Sep;12(9):4026-37
pubmed: 1508200
Bioinformatics. 2017 Jan 1;33(1):135-136
pubmed: 27605098
FEBS Lett. 2008 Jul 9;582(16):2352-6
pubmed: 18539146
Mol Biol Cell. 2012 Nov;23(21):4313-22
pubmed: 22956767
Arch Biochem Biophys. 2010 Aug 15;500(2):137-43
pubmed: 20510667
Nucleus. 2013 Jul-Aug;4(4):315-25
pubmed: 23782956
Genes Dev. 2007 Oct 15;21(20):2580-92
pubmed: 17938242
Nat Struct Mol Biol. 2017 Sep 7;24(9):689-699
pubmed: 28880863
J Cell Biol. 1999 Feb 8;144(3):389-401
pubmed: 9971735
RNA. 2009 Mar;15(3):406-19
pubmed: 19141608
Mol Cell. 2015 Dec 3;60(5):808-815
pubmed: 26638174
Biochemistry. 1978 Apr 4;17(7):1143-9
pubmed: 656378
RNA. 2013 Dec;19(12):1639-47
pubmed: 24129494
Nat Struct Mol Biol. 2016 Jan;23(1):37-44
pubmed: 26619264
J Biol Chem. 2005 Jan 28;280(4):2439-45
pubmed: 15509572
Nat Commun. 2017 Nov 27;8(1):1787
pubmed: 29176610
Biomolecules. 2017 Jan 27;7(1):
pubmed: 28134793
EMBO J. 2000 Dec 15;19(24):6900-7
pubmed: 11118225
Biochemistry. 1978 Apr 4;17(7):1149-53
pubmed: 656379
Mol Biol Cell. 2008 Feb;19(2):735-44
pubmed: 18077551
Science. 2018 Apr 13;360(6385):219-222
pubmed: 29519915
Bioinformatics. 2011 Jan 15;27(2):225-31
pubmed: 21098430
Oncotarget. 2016 Sep 13;7(37):59519-59534
pubmed: 27517747
J Biol Chem. 2016 Mar 18;291(12):6124-33
pubmed: 26797129
Mol Cell. 2001 Dec;8(6):1363-73
pubmed: 11779510
Cell. 2017 Dec 14;171(7):1599-1610.e14
pubmed: 29245012
Mol Cell Biol. 2012 Jan;32(2):430-44
pubmed: 22083961
RNA. 2016 Nov;22(11):1643-1662
pubmed: 27875256
Mol Cell Biol. 1998 Apr;18(4):2360-70
pubmed: 9528805
J Biol Chem. 2006 Nov 24;281(47):36140-8
pubmed: 17008308
Mol Cell Biol. 2010 Sep;30(17):4245-53
pubmed: 20606008
Nat Rev Mol Cell Biol. 2019 Feb;20(2):116-131
pubmed: 30467428
Protein Cell. 2019 Feb;10(2):120-130
pubmed: 29557065
Nucleic Acids Res. 2013 Jan;41(2):1151-63
pubmed: 23180764
J Biol Chem. 2014 Oct 31;289(44):30511-24
pubmed: 25231983
J Proteomics. 2019 Sep 15;207:103441
pubmed: 31301518
Methods Mol Biol. 2019;1959:225-246
pubmed: 30852826
Biochimie. 2012 Jul;94(7):1533-43
pubmed: 22266024
Trends Biochem Sci. 2015 Oct;40(10):560-575
pubmed: 26410597
Nat Methods. 2007 Nov;4(11):951-6
pubmed: 17922018
EMBO J. 2002 Feb 15;21(4):769-78
pubmed: 11847124
Nature. 2018 Apr 5;556(7699):126-129
pubmed: 29512650
Mol Microbiol. 2007 Aug;65(3):590-606
pubmed: 17610498
Nucleic Acids Res. 2008 Feb;36(2):629-39
pubmed: 18063569
J Biol Chem. 2018 Jul 6;293(27):10438-10446
pubmed: 29743234
Nat Struct Mol Biol. 2019 May;26(5):361-371
pubmed: 31061526