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Article

A mutation in GroEL interferes with protein folding by reducing the rate of discharge of sequestered polypeptides.

The Journal of biological chemistry - 5 Jun 1992

Baneyx F, Gatenby A A

Abstract excerpt

GroEL140, a mutant Escherichia coli chaperonin unable to support bacteriophage lambda head assembly, was purified to near homogeneity and compared to wild type GroEL (cpn60). GroEL140 exhibited a 1.5-fold lower ATPase activity relative to the wild type protein. The hydrolysis of ATP by both polypeptides was fully inhibited by an excess of ATP gamma S and partially inhibited by ADP and 5'-adenylylimidodiphosphate,...

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Identifiers

PMID: 1350786

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

A mutation in GroEL interferes with protein folding by reducing the rate of discharge of sequestered polypeptides.PMID 1350786Read ↗

The strongly conserved carboxyl-terminus glycine-methionine motif of the Escherichia coli GroEL chaperonin is dispensable.Semantic proximity Read ↗

Effective ATPase activity and moderate chaperonin-cochaperonin interaction are important for the functional single-ring chaperonin system.Semantic proximity Read ↗

Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysis.Semantic proximity Read ↗

Characterisation of a GroEL single-ring mutant that supports growth of Escherichia coli and has GroES-dependent ATPase activity.Semantic proximity Read ↗

Triggering protein folding within the GroEL-GroES complex.Semantic proximity Read ↗

Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation.Semantic proximity Read ↗

Dynamics of the GroEL-protein complex: effects of nucleotides and folding mutants.Semantic proximity Read ↗

Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli.Semantic proximity Read ↗

Functional communications between the apical and equatorial domains of GroEL through the intermediate domain.Semantic proximity Read ↗

Replacement of GroEL in Escherichia coli by the Group II Chaperonin from the Archaeon Methanococcus maripaludis.Semantic proximity Read ↗

Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL.Semantic proximity Read ↗

GroEL Ring Separation and Exchange in the Chaperonin Reaction.Semantic proximity Read ↗

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