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PMID: 6941272 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

recA protein promotes homologous-pairing and strand-exchange reactions between duplex DNA molecules.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 78 ·No. 4 ·1981-04-00 ·Pages 2100-4

West SC, Cassuto E, Howard-Flanders P

Abstract

Purified recA protein, product of the recA+ gene, promotes homologous pairing between intact covalent circular duplex DNA and circular single-stranded DNA carrying a short hybridized fragment [West, S. C., Cassuto, E. & Howard-Flanders, P. (1981) Nature (London) 290, 29-33.]. In this paper we investigate the interaction of duplex fragments with circular single-stranded DNA carrying the hybridized fragment and find that recA protein promotes an efficient strand-exchange reaction between interacting DNA molecules. The exchange is dependent upon linear duplex DNA fragments that are homologous to, but extend beyond, the short fragment present on the hybridized DNA substrate. The reactions require stoichiometric amounts of recA protein and the presence of ATP.

MeSH Terms
Bacterial Proteins/metabolism DNA, Circular/metabolism DNA, Single-Stranded/metabolism Kinetics Nucleic Acid Conformation Protein Binding Rec A Recombinases Recombination, Genetic
Chemicals
Bacterial Proteins DNA, Circular DNA, Single-Stranded Rec A Recombinases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
West S C
Cassuto E
Howard-Flanders P
References (20)
20 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.78.4.2100
Published
1981-04-00
Pages
2100-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC319291
Subset
IM
Grants
NIADDK NIH HHS · AM 09397 · United States
NCI NIH HHS · CA 06519 · United States
NIGMS NIH HHS · GM 11014 · United States
External Links
PubMed source DOI: 10.1073/pnas.78.4.2100 PMC Full Text View journal details
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