The conserved RNA recognition motif 3 of U2 snRNA auxiliary factor (U2AF 65) is essential in vivo but dispensable for activity in vitro
about
Splicing factor hSlu7 contains a unique functional domain required to retain the protein within the nucleusNuclear inhibitor of protein phosphatase-1 (NIPP1) directs protein phosphatase-1 (PP1) to dephosphorylate the U2 small nuclear ribonucleoprotein particle (snRNP) component, spliceosome-associated protein 155 (Sap155)U2AF homology motifs: protein recognition in the RRM worldAlternative Conformations at the RNA-binding Surface of the N-terminal U2AF65 RNA Recognition MotifMulti-domain conformational selection underlies pre-mRNA splicing regulation by U2AFU2AF65 adapts to diverse pre-mRNA splice sites through conformational selection of specific and promiscuous RNA recognition motifs.Analysis of mutant phenotypes and splicing defects demonstrates functional collaboration between the large and small subunits of the essential splicing factor U2AF in vivo.Comparative analysis of information contents relevant to recognition of introns in many speciesMajor phosphorylation of SF1 on adjacent Ser-Pro motifs enhances interaction with U2AF65.Multiple U2AF65 binding sites within SF3b155: thermodynamic and spectroscopic characterization of protein-protein interactions among pre-mRNA splicing factors.Structural basis for polypyrimidine tract recognition by the essential pre-mRNA splicing factor U2AF65.Large-scale comparative analysis of splicing signals and their corresponding splicing factors in eukaryotes.A conditional role of U2AF in splicing of introns with unconventional polypyrimidine tractsCrystallization and preliminary X-ray analysis of a U2AF65 variant in complex with a polypyrimidine-tract analogue by use of protein engineeringSolution conformation and thermodynamic characteristics of RNA binding by the splicing factor U2AF65Recognition of the 3' splice site RNA by the U2AF heterodimer involves a dynamic population shiftFRET analyses of the U2AF complex localize the U2AF35/U2AF65 interaction in vivo and reveal a novel self-interaction of U2AF35.Identification of motifs that function in the splicing of non-canonical introns.Genomic mRNA profiling reveals compensatory mechanisms for the requirement of the essential splicing factor U2AF.Architecture and Distribution of Introns in Core Genes of Four Fusarium Species.
P2860
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P2860
The conserved RNA recognition motif 3 of U2 snRNA auxiliary factor (U2AF 65) is essential in vivo but dispensable for activity in vitro
description
2004 nî lūn-bûn
@nan
2004 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
The conserved RNA recognition ...... pensable for activity in vitro
@ast
The conserved RNA recognition ...... pensable for activity in vitro
@en
The conserved RNA recognition ...... pensable for activity in vitro
@nl
type
label
The conserved RNA recognition ...... pensable for activity in vitro
@ast
The conserved RNA recognition ...... pensable for activity in vitro
@en
The conserved RNA recognition ...... pensable for activity in vitro
@nl
prefLabel
The conserved RNA recognition ...... pensable for activity in vitro
@ast
The conserved RNA recognition ...... pensable for activity in vitro
@en
The conserved RNA recognition ...... pensable for activity in vitro
@nl
P2093
P2860
P356
P1433
P1476
The conserved RNA recognition ...... pensable for activity in vitro
@en
P2093
Andrew Rahn
Bharat Gawande
Hiren Banerjee
Ravinder Singh
Sabine Guth
P2860
P304
P356
10.1261/RNA.5153204
P407
P577
2004-02-01T00:00:00Z