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PMID: 7991609 Published · ppublish English Comparative Study Journal Article

A molecular chaperone, ClpA, functions like DnaK and DnaJ.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 91 ·No. 25 ·1994-12-06 ·Pages 12218-22

Wickner S, Gottesman S, Skowyra D, Hoskins J, McKenney K, Maurizi MR

Abstract

The two major molecular chaperone families that mediate ATP-dependent protein folding and refolding are the heat shock proteins Hsp60s (GroEL) and Hsp70s (DnaK). Clp proteins, like chaperones, are highly conserved, present in all organisms, and contain ATP and polypeptide binding sites. We discovered that ClpA, the ATPase component of the ATP-dependent ClpAP protease, is a molecular chaperone. ClpA performs the ATP-dependent chaperone function of DnaK and DnaJ in the in vitro activation of the plasmid P1 RepA replication initiator protein. RepA is activated by the conversion of dimers to monomers. We show that ClpA targets RepA for degradation by ClpP, demonstrating a direct link between the protein unfolding function of chaperones and proteolysis. In another chaperone assay, ClpA protects luciferase from irreversible heat inactivation but is unable to reactivate luciferase.

MeSH Terms
Adenosine Triphosphatases/isolation & purification,metabolism Adenosine Triphosphate/metabolism Animals Bacterial Proteins/isolation & purification,metabolism Cattle Chromatography, Gel DNA Helicases DNA-Binding Proteins Endopeptidase Clp Enzyme Activation Escherichia coli Proteins HSP40 Heat-Shock Proteins HSP70 Heat-Shock Proteins/metabolism Heat-Shock Proteins/metabolism Kinetics Macromolecular Substances Molecular Weight Proteins Serine Endopeptidases/metabolism Trans-Activators
Chemicals
Bacterial Proteins DNA-Binding Proteins DnaJ protein, E coli Escherichia coli Proteins HSP40 Heat-Shock Proteins HSP70 Heat-Shock Proteins Heat-Shock Proteins Macromolecular Substances Proteins Trans-Activators replication initiator protein Adenosine Triphosphate Serine Endopeptidases Endopeptidase Clp Adenosine Triphosphatases dnaK protein, E coli DNA Helicases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Wickner S
Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.
Gottesman S
Skowyra D
Hoskins J
McKenney K
Maurizi M R
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27 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.91.25.12218
Published
1994-12-06
Pages
12218-22
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC45408
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.91.25.12218 PMC Full Text View journal details
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