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 journalArticlepeer-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 languageEnglish
Pages (from-to)653-656
Number of pages4
JournalScience
Volume265
Issue number5172
DOIs
StatePublished - 29 Jul 1994

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