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
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14 references, click to expand
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