期刊名称:Proceedings of the National Academy of Sciences
印刷版ISSN:0027-8424
电子版ISSN:1091-6490
出版年度:2007
卷号:104
期号:9
页码:3119-3124
DOI:10.1073/pnas.0700070104
语种:English
出版社:The National Academy of Sciences of the United States of America
摘要:The double-ring chaperonin GroEL mediates protein folding, in conjunction with its helper protein GroES, by undergoing ATP-induced conformational changes that are concerted within each heptameric ring. Here we have examined whether the concerted nature of these transitions is responsible for protein substrate release in an all-or-none manner. Two chimeric substrates were designed, each with two different reporter activities that were recovered after denaturation in GroES-dependent and independent fashions, respectively. The refolding of the chimeras was monitored in the presence of GroEL variants that undergo ATP-induced intraring conformational changes that are either sequential (F44W/D155A) or concerted (F44W). Our results show that release of a protein substrate from GroEL in a domain-by-domain fashion is favored when the intraring allosteric transitions of GroEL are sequential and not concerted.
关键词:allostery ; chaperonins ; cooperativity ; protein folding