Alternative RNA degradation pathways by the exonuclease Pop2p from
Adenosine Monophosphate
/ metabolism
Amino Acid Substitution
Amino Acids
/ chemistry
Binding Sites
Catalytic Domain
Cloning, Molecular
Escherichia coli
/ genetics
Gene Expression
Genetic Vectors
/ chemistry
Models, Molecular
Mutation
Phosphates
/ metabolism
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
RNA Stability
RNA, Messenger
/ genetics
Recombinant Proteins
/ chemistry
Repressor Proteins
/ chemistry
Ribonucleases
/ chemistry
Saccharomyces cerevisiae
/ enzymology
Saccharomyces cerevisiae Proteins
/ chemistry
Substrate Specificity
RNA
deadenylation
nuclease
processivity
Journal
RNA (New York, N.Y.)
ISSN: 1469-9001
Titre abrégé: RNA
Pays: United States
ID NLM: 9509184
Informations de publication
Date de publication:
04 2021
04 2021
Historique:
received:
05
10
2020
accepted:
31
12
2020
pubmed:
8
1
2021
medline:
22
4
2021
entrez:
7
1
2021
Statut:
ppublish
Résumé
The 3' to 5' exonuclease Pop2p (Caf1p) is part of the CCR4-NOT deadenylation complex that removes poly(A) tails from mRNAs in cells. Pop2p is structurally conserved in eukaryotes, but
Identifiants
pubmed: 33408095
pii: rna.078006.120
doi: 10.1261/rna.078006.120
pmc: PMC7962489
doi:
Substances chimiques
Amino Acids
0
Phosphates
0
RNA, Messenger
0
Recombinant Proteins
0
Repressor Proteins
0
Saccharomyces cerevisiae Proteins
0
Adenosine Monophosphate
415SHH325A
Ribonucleases
EC 3.1.-
POP2 protein, S cerevisiae
EC 3.1.13.4
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
465-476Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM118088
Pays : United States
Informations de copyright
© 2021 Ye et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society.
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