Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer

Abdussalam Azem; Martin Kessel; Pierre Goloubinoff

doi:10.1126/science.7913553

Characterization of a functional GroEL₁₄(GroES₇)₂ chaperonin hetero-oligomer

Abdussalam Azem, Martin Kessel, Pierre Goloubinoff^*

^*Corresponding author for this work

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

152 Scopus citations

Abstract

Chaperonins GroEL and GroES form two types of hetero-oligomers in vitro that can mediate the folding of proteins. Chemical cross-linking and electron microscopy showed that in the presence of adenosine triphosphate (ATP), two GroES₇ rings can successively bind a single GroEL₁₄ core oligomer. The symmetric GmEL₁₄(GroES₇)₂ chaperonin, whose central cavity appears obstructed by two GroES₇ rings, can nonetheless stably bind and assist the ATP-dependent refolding of RuBisCO enzyme. Thus, unfolded proteins first bind and possibly fold on the external envelope of the chaperonin hetero-oligomer.

Original language	English
Pages (from-to)	653-656
Number of pages	4
Journal	Science
Volume	265
Issue number	5172
DOIs	https://doi.org/10.1126/science.7913553
State	Published - 29 Jul 1994

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title = "Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer",

abstract = "Chaperonins GroEL and GroES form two types of hetero-oligomers in vitro that can mediate the folding of proteins. Chemical cross-linking and electron microscopy showed that in the presence of adenosine triphosphate (ATP), two GroES7 rings can successively bind a single GroEL14 core oligomer. The symmetric GmEL14(GroES7)2 chaperonin, whose central cavity appears obstructed by two GroES7 rings, can nonetheless stably bind and assist the ATP-dependent refolding of RuBisCO enzyme. Thus, unfolded proteins first bind and possibly fold on the external envelope of the chaperonin hetero-oligomer.",

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N2 - Chaperonins GroEL and GroES form two types of hetero-oligomers in vitro that can mediate the folding of proteins. Chemical cross-linking and electron microscopy showed that in the presence of adenosine triphosphate (ATP), two GroES7 rings can successively bind a single GroEL14 core oligomer. The symmetric GmEL14(GroES7)2 chaperonin, whose central cavity appears obstructed by two GroES7 rings, can nonetheless stably bind and assist the ATP-dependent refolding of RuBisCO enzyme. Thus, unfolded proteins first bind and possibly fold on the external envelope of the chaperonin hetero-oligomer.

AB - Chaperonins GroEL and GroES form two types of hetero-oligomers in vitro that can mediate the folding of proteins. Chemical cross-linking and electron microscopy showed that in the presence of adenosine triphosphate (ATP), two GroES7 rings can successively bind a single GroEL14 core oligomer. The symmetric GmEL14(GroES7)2 chaperonin, whose central cavity appears obstructed by two GroES7 rings, can nonetheless stably bind and assist the ATP-dependent refolding of RuBisCO enzyme. Thus, unfolded proteins first bind and possibly fold on the external envelope of the chaperonin hetero-oligomer.

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Characterization of a functional GroEL₁₄(GroES₇)₂ chaperonin hetero-oligomer

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