Pby1 is a direct partner of the Dcp2 decapping enzyme.
Adenosine Triphosphate
/ metabolism
Catalytic Domain
DNA-Binding Proteins
/ chemistry
Endopeptidases
/ chemistry
Endoribonucleases
/ chemistry
Holoenzymes
/ chemistry
Ligases
/ metabolism
Models, Molecular
Organelles
/ enzymology
Protein Binding
Protein Domains
Saccharomyces cerevisiae
/ cytology
Saccharomyces cerevisiae Proteins
/ chemistry
Transcription Factors
/ chemistry
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
19 06 2020
19 06 2020
Historique:
accepted:
23
04
2020
revised:
17
04
2020
received:
24
02
2020
pubmed:
13
5
2020
medline:
9
9
2020
entrez:
13
5
2020
Statut:
ppublish
Résumé
Most eukaryotic mRNAs harbor a characteristic 5' m7GpppN cap that promotes pre-mRNA splicing, mRNA nucleocytoplasmic transport and translation while also protecting mRNAs from exonucleolytic attacks. mRNA caps are eliminated by Dcp2 during mRNA decay, allowing 5'-3' exonucleases to degrade mRNA bodies. However, the Dcp2 decapping enzyme is poorly active on its own and requires binding to stable or transient protein partners to sever the cap of target mRNAs. Here, we analyse the role of one of these partners, the yeast Pby1 factor, which is known to co-localize into P-bodies together with decapping factors. We report that Pby1 uses its C-terminal domain to directly bind to the decapping enzyme. We solved the structure of this Pby1 domain alone and bound to the Dcp1-Dcp2-Edc3 decapping complex. Structure-based mutant analyses reveal that Pby1 binding to the decapping enzyme is required for its recruitment into P-bodies. Moreover, Pby1 binding to the decapping enzyme stimulates growth in conditions in which decapping activation is compromised. Our results point towards a direct connection of Pby1 with decapping and P-body formation, both stemming from its interaction with the Dcp1-Dcp2 holoenzyme.
Identifiants
pubmed: 32396195
pii: 5836192
doi: 10.1093/nar/gkaa337
pmc: PMC7293026
doi:
Substances chimiques
DNA-Binding Proteins
0
Holoenzymes
0
PBY1 protein, S cerevisiae
0
Saccharomyces cerevisiae Proteins
0
Transcription Factors
0
Adenosine Triphosphate
8L70Q75FXE
DCP2 protein, S cerevisiae
EC 3.1.-
Endoribonucleases
EC 3.1.-
Endopeptidases
EC 3.4.-
dipeptidyl carboxypeptidase
EC 3.4.15.-
Ligases
EC 6.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
6353-6366Informations de copyright
© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.
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