Auweter S D, Allain F H-T
Institute for Molecular Biology and Biophysics, ETH Zürich, 8093, Zürich, Switzerland.
Cell Mol Life Sci. 2008 Feb;65(4):516-27. doi: 10.1007/s00018-007-7378-2.
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.
多嘧啶序列结合蛋白(PTB)是一种58 kDa的RNA结合蛋白,参与mRNA代谢的多个方面,包括剪接调控、聚腺苷酸化、3'端形成、内部核糖体进入位点介导的翻译、RNA定位和稳定性。PTB包含四个由三个连接子分隔的RNA识别基序(RRMs)。在本综述中,我们总结了过去7年使用核磁共振光谱和小角X射线散射收集到的关于溶液中PTB的结构信息。PTB所有RRMs在游离状态下以及与短嘧啶序列结合时的结构,以及PTB RRM2与一种肽结合时的结构模型,揭示了不同寻常的结构特征,这些特征为PTB在RNA代谢不同过程,特别是剪接调控中的作用机制提供了新的见解。