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Article

Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation.

The Journal of biological chemistry - 9 Jan 2004

Figueiredo Luis, Klunker Daniel, Ang Debbie, Naylor Dean J, Kerner Michael J, Georgopoulos Costa, Hartl F Ulrich, Hayer-Hartl Manajit

Abstract excerpt

In all three kingdoms of life chaperonins assist the folding of a range of newly synthesized proteins. As shown recently, Archaea of the genus Methanosarcina contain both group I (GroEL/GroES) and group II (thermosome) chaperonins in the cytosol. Here we report on a detailed functional analysis of the archaeal GroEL/GroES system of Methanosarcina mazei (Mm) in comparison to its bacterial counterpart from...

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PMID: 14576149
DOI: 10.1074/jbc.M310914200

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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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Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation.PMID 14576149Read ↗

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Revisiting the contribution of negative charges on the chaperonin cage wall to the acceleration of protein folding.Semantic proximity Read ↗

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

Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE.Semantic proximity Read ↗

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

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

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