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Article

From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL.

Journal of molecular biology - 15 Dec 2000

Chatellier J, Hill F, Foster N W, Goloubinoff P, Fersht A R

Abstract excerpt

The next step in our reductional analysis of GroEL was to study the activity of an isolated single seven-membered ring of the 14-mer. A known single-ring mutant, GroEL(SR1), contains four point mutations that prevent the formation of double-rings. That heptameric complex is functionally inactive because it is unable to release GroES. We found that the mutation E191G, which is responsible for the temperature...

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Identifiers

PMID: 11124035
DOI: 10.1006/jmbi.2000.4278

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Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL.PMID 11124035Read ↗

From minichaperone to GroEL 2: importance of avidity of the multisite ring structure.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 ↗

Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction.Semantic proximity Read ↗

Isolation and characterisation of mutants of GroEL that are fully functional as single rings.Semantic proximity Read ↗

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

Stimulating the substrate folding activity of a single ring GroEL variant by modulating the cochaperonin GroES.Semantic proximity Read ↗

Characterisation of mutations in GroES that allow GroEL to function as a single ring.Semantic proximity Read ↗

In vivo activities of GroEL minichaperones.Semantic proximity Read ↗

Stabilization of GroEL minichaperones by core and surface mutations.Semantic proximity Read ↗

Hydrophilic residues 526 KNDAAD 531 in the flexible C-terminal region of the chaperonin GroEL are critical for substrate protein folding within the central cavity.Semantic proximity Read ↗

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

In vivo and in vitro function of GroEL mutants with impaired allosteric properties.Semantic proximity Read ↗

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