tRNA 2'-O-methylation by a duo of TRM7/FTSJ1 proteins modulates small RNA silencing in Drosophila.
Animals
Drosophila melanogaster
/ genetics
Gene Expression Regulation
/ genetics
Gene Silencing
Humans
Methylation
Methyltransferases
/ genetics
Nuclear Proteins
/ genetics
RNA Interference
RNA, Transfer
/ genetics
Saccharomyces cerevisiae
/ genetics
Saccharomyces cerevisiae Proteins
/ genetics
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
tRNA Methyltransferases
/ genetics
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
28 02 2020
28 02 2020
Historique:
accepted:
01
01
2020
revised:
30
12
2019
received:
17
07
2019
pubmed:
17
1
2020
medline:
19
3
2020
entrez:
17
1
2020
Statut:
ppublish
Résumé
2'-O-Methylation (Nm) represents one of the most common RNA modifications. Nm affects RNA structure and function with crucial roles in various RNA-mediated processes ranging from RNA silencing, translation, self versus non-self recognition to viral defense mechanisms. Here, we identify two Nm methyltransferases (Nm-MTases) in Drosophila melanogaster (CG7009 and CG5220) as functional orthologs of yeast TRM7 and human FTSJ1. Genetic knockout studies together with MALDI-TOF mass spectrometry and RiboMethSeq mapping revealed that CG7009 is responsible for methylating the wobble position in tRNAPhe, tRNATrp and tRNALeu, while CG5220 methylates position C32 in the same tRNAs and also targets additional tRNAs. CG7009 or CG5220 mutant animals were viable and fertile but exhibited various phenotypes such as lifespan reduction, small RNA pathways dysfunction and increased sensitivity to RNA virus infections. Our results provide the first detailed characterization of two TRM7 family members in Drosophila and uncover a molecular link between enzymes catalyzing Nm at specific tRNAs and small RNA-induced gene silencing pathways.
Identifiants
pubmed: 31943105
pii: 5707191
doi: 10.1093/nar/gkaa002
pmc: PMC7038984
doi:
Substances chimiques
Nuclear Proteins
0
Saccharomyces cerevisiae Proteins
0
RNA, Transfer
9014-25-9
FTSJ1 protein, human
EC 2.1.1.-
Methyltransferases
EC 2.1.1.-
Trm7 protein, S cerevisiae
EC 2.1.1.-
tRNA Methyltransferases
EC 2.1.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2050-2072Subventions
Organisme : Austrian Science Fund FWF
ID : P 29094
Pays : Austria
Informations de copyright
© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.
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