Institute of Chemistry, University of Campinas-UNICAMP, PO Box 6154, 13083-970, Campinas, SP, Brazil.
Int J Biol Macromol. 2011 Dec 1;49(5):1022-30. doi: 10.1016/j.ijbiomac.2011.08.027. Epub 2011 Aug 31.
The Clp/Hsp100 AAA+ chaperone family is involved in recovering aggregated proteins and little is known about other orthologs of the well studied ClpB from Escherichia coli and Hsp104 from Saccharomyces cerevisiae. Plant Hsp101 is a good model for understanding the relationship between the structure and function of Hsp100 proteins and to investigate the role of these chaperones in disaggregation processes. Here, we present the cloning and purification of a sugarcane ortholog, SHsp101, which is expressed in sugarcane cells and is a folded hexamer that is capable of binding nucleotides. Thus SHsp101 has the structural and functional characteristics of the Clp/Hsp100 AAA+ family.
Clp/Hsp100 AAA+ 伴侣家族参与回收聚集的蛋白质，而对于大肠杆菌中研究充分的 ClpB 和酿酒酵母中的 Hsp104 的其他同源物，人们知之甚少。植物 Hsp101 是理解 Hsp100 蛋白结构和功能之间关系的良好模型，并且可用于研究这些伴侣在解聚过程中的作用。在这里，我们介绍了甘蔗同源物 SHsp101 的克隆和纯化，该同源物在甘蔗细胞中表达，是一种折叠的六聚体，能够结合核苷酸。因此，SHsp101 具有 Clp/Hsp100 AAA+ 家族的结构和功能特征。
