Structure-function relationships of the polypyrimidine tract binding protein

被引：78

作者：

Auweter, S. D. ^{[1
]}

Allain, F. H. -T. ^{[1
]}

机构：

[1] ETH, Inst Mol Biol & Biophys, CH-8093 Zurich, Switzerland

来源：

CELLULAR AND MOLECULAR LIFE SCIENCES | 2008年 / 65卷 / 04期

关键词：

alternative splicing; translation regulation; polypyrimidine tract binding protein; RNA-protein complex; RNA-protein recognition; RNA recognition motifs; RBD; splicing regulation;

D O I：

10.1007/s00018-007-7378-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The polypyrimidine tract binding protein (PTB) is a 58-kDa RNA binding protein involved in multiple aspects of mRNA metabolism including splicing regulation, polyadenylation, 3'end formation, internal ribosomal entry site-mediated translation, RNA localization and stability. PTB contains four RNA recognition motifs (RRMs) separated by three linkers. In this review we summarize structural information on PTB in solution that has been gathered during the past 7 years using NMR spectroscopy and small-angle X-ray scattering. The structures of all RRMs of PTB in their free state and in complex with short pyrimidine tracts, as well as a structural model of PTB RRM2 in complex with a peptide, revealed unusual structural features that provided new insights into the mechanisms of action of PTB in the different processes of RNA metabolism and in particular splicing regulation.

引用

页码：516 / 527

页数：12

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