Solution structure of the Vts1 SAM domain in the presence of RNA

被引:14
作者
Edwards, TA
Butterwick, JA
Zeng, L
Gupta, YK
Wang, X
Wharton, RP
Palmer, AG
Aggarwal, AK
机构
[1] Columbia Univ, Dept Biochem & Mol Biophys, New York, NY 10032 USA
[2] Mt Sinai Sch Med, Struct Biol Program, Dept Physiol & Biophys, New York, NY 10029 USA
[3] Duke Univ, Med Ctr, Howard Hughes Med Inst, Dept Mol Genet & Microbiol, Durham, NC 27710 USA
关键词
Vts1; SAM domain; Smaug; RNA-binding protein; translational control;
D O I
10.1016/j.jmb.2005.12.004
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 yeast Vts1 SAM (sterile alpha motif) domain is a member of a new class of SAM domains that specifically bind RNA. To elucidate the structural basis for RNA binding, the solution structure of the Vts1 SAM domain, in the presence of a specific target RNA, has been solved by multidimensional heteronuclear NMR spectroscopy. The Vts1 SAM domain retains the "core" five-helix-bundle architecture of traditional SAM domains, but has additional short helices at N and C termini, comprising a small substructure that caps the core helices. The RNA-binding surface of Vts1, determined by chemical shift perturbation, maps near the ends of three of the core helices, in agreement with mutational data and the electrostatic properties of the molecule. These results provide a structural basis for the versatility of the SAM domain in protein and RNA-recognition. (c) 2005 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1065 / 1072
页数:8
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