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PMID: 6273839 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.

Directionality and polarity in recA protein-promoted branch migration.

Cox MM, Lehman IR

Abstract

The recA protein of Escherichia coli promotes the complete exchange of strands between full-length linear duplex and single-stranded circular phi X174 DNA molecules. Analysis of the reaction by electron microscopy confirms that D loops containing short heteroduplex regions are rapidly formed at the ends of the linear duplex, followed by a relatively slow branch migration that converts the D loops to nicked circular duplexes (RFII) and displaced linear single strands. Heteroduplex extension and displacement of the linear single strand are concerted. Heterologous sequences within the linear duplex halt branch migration and lead to the accumulation of D loops. Although D loops can be formed at either end of the linear duplex, recA protein-promoted branch migration proceeds uniquely in the 3' leads to 5' direction relative to the (--) strand of the linear duplex.

MeSH Terms
Bacterial Proteins/genetics,isolation & purification DNA Restriction Enzymes DNA, Single-Stranded/genetics DNA, Viral/genetics Escherichia coli/genetics Kinetics Microscopy, Electron Protein Conformation Rec A Recombinases
Chemicals
Bacterial Proteins DNA, Single-Stranded DNA, Viral Rec A Recombinases DNA Restriction Enzymes
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Cox M M
Lehman I R
References (14)
14 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
Published
1981-10-00
Pages
6018-22
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC348968
Subset
IM
Grants
NIGMS NIH HHS · GM-06196 · United States
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