GroES binding regulates GroEL chaperonin activity under heat shock

Pierre Goloubinoff; Sophia Diamant; Celeste Weiss; Abdussalam Azem

doi:10.1016/S0014-5793(97)00348-7

GroES binding regulates GroEL chaperonin activity under heat shock

Pierre Goloubinoff^*, Sophia Diamant, Celeste Weiss, Abdussalam Azem

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	215-219
Number of pages	5
Journal	FEBS Letters
Volume	407
Issue number	2
DOIs	https://doi.org/10.1016/S0014-5793(97)00348-7
State	Published - 28 Apr 1997
Externally published	Yes

Keywords

GroE chaperone
Heat shock
Molecular thermometer
Protein folding

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10.1016/S0014-5793(97)00348-7

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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. ",

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doi = "10.1016/S0014-5793(97)00348-7",

language = "אנגלית",

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T1 - GroES binding regulates GroEL chaperonin activity under heat shock

AU - Goloubinoff, Pierre

AU - Diamant, Sophia

AU - Weiss, Celeste

AU - Azem, Abdussalam

N1 - 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.

PY - 1997/4/28

Y1 - 1997/4/28

N2 - 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.

AB - 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.

KW - GroE chaperone

KW - Heat shock

KW - Molecular thermometer

KW - Protein folding

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JO - FEBS Letters

JF - FEBS Letters

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ER -

GroES binding regulates GroEL chaperonin activity under heat shock

Abstract

Keywords

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