Interaction of the RecA protein of Escherichia coli with single-stranded oligodeoxyribonucleotides

Piero R. Bianco, George M. Weinstock

Research output: Contribution to journalArticlepeer-review

32 Scopus citations

Abstract

The RecA protein of Escherichia coli performs a number of ATP-dependent, in vitro reactions and is a DNA-dependent ATPase. Small oligodeoxyribonucleotides were used as DNA cofactors in a kinetic analysis of the ATPase reaction. Polymers of deoxythymidilic acid as well as oligonucleotides of mixed base composition stimulated the RecA ATPase activity in a length-dependent fashion. Both the initial rate and the extent of the reaction were affected by chain length. Full activity was seen with chain lengths ≤ 30 nt. Partial activity was seen with chain lengths of 15-30 nt. The lower activity of shorter oligonucleotides was not simply due to a reduced affinity for DNA, since effects of chain length on K(m)(ATP) and the Hill coefficient for ATP hydrolysis were also observed. The results also suggested that single-stranded DNA secondary structure frequently affects the ATPase activity of RecA protein with oligodeoxyribonucleotides.

Original languageEnglish (US)
Pages (from-to)4933-4939
Number of pages7
JournalNucleic acids research
Volume24
Issue number24
DOIs
StatePublished - Dec 15 1996
Externally publishedYes

ASJC Scopus subject areas

  • Genetics

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