Resonance assignments for the substrate binding domain of Hsp70 chaperone Ssa1 from Saccharomyces cerevisiae
Resonance assignments for the substrate binding domain of Hsp70 chaperone Ssa1 from Saccharomyces cerevisiae
复制标题
酿酒酵母 Hsp70 分子伴侣 Ssa1 底物结合域的共振分配
DOI：
10.1007/s12104-015-9603-5
复制
发表时间：
2015-10-01
影响因子：
0.9
通讯作者：
Perrett, Sarah
中科院分区：
文献类型：
--
作者：
Hu, Wanhui;Wu, Huiwen;Perrett, Sarah
Hsp 70分子伴侣蛋白在细胞中起着至关重要的作用。已经对细菌和哺乳动物Hsp 70进行了广泛的结构和功能研究。Ssa 1是酿酒酵母（Saccharomycescerevisiae）中Hsp 70家族的成员。对Ssa 1的体内和生物化学研究表明，它调节朊病毒的繁殖和细胞周期。然而，到目前为止，还没有获得Ssa 1的结构数据。在这里，我们报告了几乎完整的（96%）（1）H，（13）C，（15）N骨架和侧链NMR指定的18.8 kDa的Ssa 1底物结合结构域。该构建体包括残基382-554，其对应于整个底物结合结构域和同源结构中的两个后续α-螺旋。从指定的化学位移预测的二级结构是一致的同源热休克蛋白70底物结合域。
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 %) (1)H, (13)C, (15)N backbone and side chain NMR assignment of the 18.8 kDa Ssa1 substrate binding domain. The construct includes residues 382-554, 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.