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PMID: 2536712 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

The dnaB-dnaC replication protein complex of Escherichia coli. I. Formation and properties.

The Journal of biological chemistry ·Vol. 264 ·No. 5 ·1989-02-15 ·Pages 2463-8

Wahle E, Lasken RS, Kornberg A

Abstract

The complex formed between the dnaB and dnaC replication proteins of Escherichia coli is stabilized by ATP binding to dnaC. The dnaB6-dnaC6-ATP6 complex can be maintained without ATP hydrolysis at a concentration as low as 5 x 10(-10) M. The complex is also formed with adenosine 5'-(gamma-thio)triphosphate but generates little or no dnaB activity, suggesting a requirement for ATP hydrolysis in the subsequent stage of binding of the complex to DNA. In this step, dnaC is released, leaving dnaB to function on the associated DNA.

MeSH Terms
Adenosine Triphosphate/analogs & derivatives,metabolism Bacterial Proteins/metabolism DNA Replication Escherichia coli/genetics,metabolism Ethylmaleimide/pharmacology Kinetics Macromolecular Substances Molecular Weight
Chemicals
Bacterial Proteins Macromolecular Substances adenosine 5'-O-(3-thiotriphosphate) Adenosine Triphosphate Ethylmaleimide
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Wahle E
Department of Biochemistry, Stanford University School of Medicine, California 94305-5307.
Lasken R S
Kornberg A
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1989-02-15
Pages
2463-8
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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