Resonance assignments for the substrate binding domain of Hsp70 chaperone Ssa1 from Saccharomyces cerevisiae

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• 作者：Wanhui Hu ; Huiwen Wu ; Hong Zhang ; Weibin Gong…
• 关键词：Ssa1 ; Saccharomyces ; Substrate binding domain ; NMR assignments ; Secondary structure
• 刊名：Biomolecular NMR Assignments
• 出版年：2015
• 出版时间：October 2015
• 年：2015
• 卷：9
• 期：2
• 页码：329-332
• 全文大小：2,049 KB
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• 作者单位：Wanhui Hu (1) (2)
  Huiwen Wu (1) (2)
  Hong Zhang (1)
  Weibin Gong (1)
  Sarah Perrett (1)
  
  1. National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China
  2. University of the Chinese Academy of Sciences, 19A Yuquan Road, Shijingshan District, Beijing, 100049, China
  
• 刊物类别：Physics and Astronomy
• 刊物主题：None Assigned
• 出版者：Springer Netherlands
• ISSN：1874-270X

文摘

Hsp70 chaperone proteins play crucial roles in the cell. Extensive structural and functional studies have been performed for bacterial and mammalian Hsp70s. Ssa1 from Saccharomyces cerevisiae is a member of the Hsp70 family. In vivo and biochemical studies on Ssa1 have revealed that it regulates prion propagation and the cell cycle. However, no structural data has been obtained for Ssa1 up to now. Here we report the almost complete (96 %) 1H, 13C, 15N backbone and side chain NMR assignment of the 18.8 kDa Ssa1 substrate binding domain. The construct includes residues 382-54, which corresponds to the entire substrate binding domain and two following α-helices in homologous structures. The secondary structure predicted from the assigned chemical shifts is consistent with that of homologous Hsp70 substrate binding domains. Keywords Ssa1 Saccharomyces Substrate binding domain NMR assignments Secondary structure