The yeast Pan2 protein is required for poly(A)-binding protein-stimulated poly(A)-nuclease activity.
about
Conservation of the deadenylase activity of proteins of the Caf1 family in humanIdentification of a human cytoplasmic poly(A) nuclease complex stimulated by poly(A)-binding proteinThe deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes.EDEN and EDEN-BP, a cis element and an associated factor that mediate sequence-specific mRNA deadenylation in Xenopus embryos.The proofreading domain of Escherichia coli DNA polymerase I and other DNA and/or RNA exonuclease domainsYeast transcripts cleaved by an internal ribozyme provide new insight into the role of the cap and poly(A) tail in translation and mRNA decayExoribonuclease superfamilies: structural analysis and phylogenetic distributionCap-dependent deadenylation of mRNAInteraction between a poly(A)-specific ribonuclease and the 5' cap influences mRNA deadenylation rates in vitroPoly(A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expressionMechanisms of deadenylation-dependent decayProteins involved in the degradation of cytoplasmic mRNA in the major eukaryotic model systemsHeterogeneity and complexity within the nuclease module of the Ccr4-Not complexSolution structure of the orphan PABC domain from Saccharomyces cerevisiae poly(A)-binding proteinStructure of a nucleotide-bound Clp1-Pcf11 polyadenylation factorStructural basis for Pan3 binding to Pan2 and its function in mRNA recruitment and deadenylationAn asymmetric PAN3 dimer recruits a single PAN2 exonuclease to mediate mRNA deadenylation and decayThe structure of the Pan2-Pan3 core complex reveals cross-talk between deadenylase and pseudokinasePAN3 encodes a subunit of the Pab1p-dependent poly(A) nuclease in Saccharomyces cerevisiaeDisruption and phenotypic analysis of six open reading frames from the left arm of Saccharomyces cerevisiae chromosome VII.Saccharomyces cerevisiae Ngl3p is an active 3'-5' exonuclease with a specificity towards poly-A RNA reminiscent of cellular deadenylases.Three conserved members of the RNase D family have unique and overlapping functions in the processing of 5S, 5.8S, U4, U5, RNase MRP and RNase P RNAs in yeast.The Saccharomyces cerevisiae RNA-binding protein Rbp29 functions in cytoplasmic mRNA metabolism.Characterization of nuclear localization and nuclear export signals of yeast actin-binding protein Pan1.Tpa1p is part of an mRNP complex that influences translation termination, mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae.A nuclear 3'-5' exonuclease involved in mRNA degradation interacts with Poly(A) polymerase and the hnRNA protein Npl3pThe yeast POP2 gene encodes a nuclease involved in mRNA deadenylation.A novel fluorescence-activated cell sorter-based screen for yeast endocytosis mutants identifies a yeast homologue of mammalian eps15.The yeast Apq12 protein affects nucleocytoplasmic mRNA transport.EH domain proteins Pan1p and End3p are components of a complex that plays a dual role in organization of the cortical actin cytoskeleton and endocytosis in Saccharomyces cerevisiae.A specific role for the C-terminal region of the Poly(A)-binding protein in mRNA decayThe EH-domain-containing protein Pan1 is required for normal organization of the actin cytoskeleton in Saccharomyces cerevisiae.Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation.Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)-binding protein, regulates polyadenylationIdentification of factors regulating poly(A) tail synthesis and maturation.MAPKAP kinase 2 blocks tristetraprolin-directed mRNA decay by inhibiting CAF1 deadenylase recruitmentISG20L2, a novel vertebrate nucleolar exoribonuclease involved in ribosome biogenesisA 54-kDa fragment of the Poly(A)-specific ribonuclease is an oligomeric, processive, and cap-interacting Poly(A)-specific 3' exonucleaseThe mRNA cap structure stimulates rate of poly(A) removal and amplifies processivity of degradationConcerted action of poly(A) nucleases and decapping enzyme in mammalian mRNA turnover
P2860
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P2860
The yeast Pan2 protein is required for poly(A)-binding protein-stimulated poly(A)-nuclease activity.
description
1996 nî lūn-bûn
@nan
1996 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
The yeast Pan2 protein is requ ...... ted poly(A)-nuclease activity.
@ast
The yeast Pan2 protein is requ ...... ted poly(A)-nuclease activity.
@en
The yeast Pan2 protein is requ ...... ted poly(A)-nuclease activity.
@nl
type
label
The yeast Pan2 protein is requ ...... ted poly(A)-nuclease activity.
@ast
The yeast Pan2 protein is requ ...... ted poly(A)-nuclease activity.
@en
The yeast Pan2 protein is requ ...... ted poly(A)-nuclease activity.
@nl
prefLabel
The yeast Pan2 protein is requ ...... ted poly(A)-nuclease activity.
@ast
The yeast Pan2 protein is requ ...... ted poly(A)-nuclease activity.
@en
The yeast Pan2 protein is requ ...... ted poly(A)-nuclease activity.
@nl
P2093
P2860
P356
P1476
The yeast Pan2 protein is requ ...... ted poly(A)-nuclease activity.
@en
P2093
P2860
P356
10.1074/JBC.271.1.432
P407
P577
1996-01-05T00:00:00Z