Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria.

doi:10.1083/jcb.126.2.305

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Article

Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria.

The Journal of cell biology - 1 Jul 1994

Höhfeld J, Hartl F U

Abstract excerpt

Protein folding in mitochondria is mediated by the chaperonin Hsp60, the homologue of E. coli GroEL. Mitochondria also contain a homologue of the cochaperonin GroES, called Hsp10, which is a functional regulator of the chaperonin. To define the in vivo role of the co-chaperonin, we have used the genetic and biochemical potential of the yeast S. cerevisiae. The HSP10 gene was cloned and sequenced and...

Topics

Amino Acid Sequence
Base Sequence
Chaperonin 10
Chaperonin 60
Chaperonins
Cloning, Molecular
Fungal Proteins
Gene Expression Regulation, Fungal
Genes, Fungal
Heat-Shock Proteins
Mitochondria

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutation

Protein Binding

Protein Folding

Protein Precursors

Proteins

Recombinant Fusion Proteins

Source

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Identifiers

PMID: 7913473
DOI: 10.1083/jcb.126.2.305
PMCID: PMC2200036

Genes

DHFR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7913473-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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