The molecular chaperone, Atp12p, from Homo sapiens. In vitro studies with purified wild type and mutant (E240K) proteins.

doi:10.1074/jbc.M312631200

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Article

The molecular chaperone, Atp12p, from Homo sapiens. In vitro studies with purified wild type and mutant (E240K) proteins.

The Journal of biological chemistry - 5 Mar 2004

Hinton Ayana, Gatti Domenico L, Ackerman Sharon H

Abstract excerpt

Work in Saccharomyces cerevisiae has shown that Atp12p binds to unassembled alpha subunits of F(1) and in so doing prevents the alpha subunit from associating with itself in non-productive complexes during assembly of the F(1) moiety of the mitochondrial ATP synthase. We have developed a method to prepare recombinant Atp12p after expression of its human cDNA in bacterial cells. The molecular chaperone activity of...

Topics

Chaperonins
DNA, Complementary
Humans
Mitochondrial Proteins
Mitochondrial Proton-Translocating ATPases
Molecular Chaperones
Mutation
Protein Conformation
Proton-Translocating ATPases
Recombinant Proteins
Saccharomyces cerevisiae Proteins

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Identifiers

PMID: 14701807
DOI: 10.1074/jbc.M312631200

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