E. coli recA protein possesses a strand separating activity on short duplex DNAs.

M. Bianchi, B. Riboli, G. Magni

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

RecA protein was found to catalyze the dissociation of the strands of a DNA substrate consisting of a 20-nucleotide primer annealed to circular single-stranded M13mp DNA. The strand separation reaction requires ATP hydrolysis and the presence of single-stranded DNA flanking the duplex DNA region to be unwound. RecA-catalyzed strand separation is effective only for very short duplexes, not exceeding 30 bp, and is not stimulated by single-stranded DNA-binding protein. These results are consistent with the ability of recA protein to disrupt regions of secondary structure in single-stranded DNA and to incorporate large non-homologies into heteroduplex DNA.

Original languageEnglish
Pages (from-to)3025-3030
Number of pages6
JournalEMBO Journal
Volume4
Issue number11
Publication statusPublished - Nov 1985

Fingerprint

Rec A Recombinases
Escherichia coli Proteins
Single-Stranded DNA
Escherichia coli
DNA
Nucleic Acid Heteroduplexes
Circular DNA
DNA-Binding Proteins
Hydrolysis
Nucleotides
Adenosine Triphosphate
Substrates

ASJC Scopus subject areas

  • Cell Biology
  • Genetics

Cite this

E. coli recA protein possesses a strand separating activity on short duplex DNAs. / Bianchi, M.; Riboli, B.; Magni, G.

In: EMBO Journal, Vol. 4, No. 11, 11.1985, p. 3025-3030.

Research output: Contribution to journalArticle

Bianchi, M. ; Riboli, B. ; Magni, G. / E. coli recA protein possesses a strand separating activity on short duplex DNAs. In: EMBO Journal. 1985 ; Vol. 4, No. 11. pp. 3025-3030.
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