Super Spy variants implicate flexibility in chaperone action
作者单位：School of Biotechnology East China University of Science and Technology The State Key Laboratory of Bioreactor Engineering Howard Hughes Medical Institute Department of Molecular Cellular and Developmental Biology University of Michigan Department of Biochemistry and Microbiology University of Victoria-Genome British Columbia Proteomics Centre University of Victoria Department of Computational Medicine & Bioinformatics University of Michigan
会议名称：《中国生物化学与分子生物学会第十一次会员代表大会暨201...》
会议日期：2014年
学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 081704[工学-应用化学] 1001[医学-基础医学(可授医学、理学学位)] 07[理学] 08[工学] 0817[工学-化学工程与技术] 10[医学]
关 键 词：Spy Chaperone flexibility
摘 要：Experimental study of the role of disorder in protein function is *** has beenproposed that proteins utilizedisordered regions in the adaptive recognition of their variousbinding *** apart from a few exceptions,defining the importance ofdisorder in promiscuous binding interactions has proven to be *** is anemerging theme,not only among many hub proteins but also among molecular chaperones,which in general allow promiscuous substrate *** have utilized a genetic selection that links protein stability to antibiotic resistance toisolate variants of the newly discovered chaperone Spy that show an up to 7 fold improvedchaperone activity against a variety of *** on our biochemical and biophysicalevaluation of theseSuper Spyvariants,there appear to be multiple factors that resultin the increased chaperone *** addition to increasing binding site hydrophobicity,most of our super-Spy variants show tighter binding to client proteins and are generallymore unstable than is wild type *** variants also show increased levels of disorderin the absence of client proteins,indicating increases in apparent flexibility of these *** establish a good relationship between the degree of their instability and the improvementthey show in their chaperone *** results provide evidence for the importanceof disorder and apparent flexibility in chaperone action.