@article{99a2490f55dd4ee7a2b2f0476416b1da,
title = "GroES binding regulates GroEL chaperonin activity under heat shock",
abstract = "Chaperonins GroEL14 and GroES7 are heat-shock proteins implicated in the molecular response to stress. Protein fluorescence, crosslinking and kinetic analysis revealed that the bond between the two otherwise thermoresistant oligomers is regulated by temperature. As temperature increased, the affinity of GroES7 and the release of bound proteins from the chaperonin concomitantly decreased. After heat shock, GroES7 rebinding to GroEL14 and GroEL14GroES7 particles correlated with the restoration of optimal protein folding/release activity. Chaperonins thus behave as a molecular thermometer which can inhibit the release of aggregation-prone proteins during heat shock and restore protein folding and release after heat shock.",
keywords = "GroE chaperone, Heat shock, Molecular thermometer, Protein folding",
author = "Pierre Goloubinoff and Sophia Diamant and Celeste Weiss and Abdussalam Azem",
note = "Funding Information: We thank E. Harel and P. Viitanen for useful discussions. This work was supported in part by a grant from the German-Israeli Foundation for Scientific Research and Development to P.G., from the L. Eshkol and Abisch-Frenkel Foundations to C.W. and from the G. Meir Foundation to A.A. ",
year = "1997",
month = apr,
day = "28",
doi = "10.1016/S0014-5793(97)00348-7",
language = "אנגלית",
volume = "407",
pages = "215--219",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "John Wiley and Sons Inc.",
number = "2",
}