Nucleic Acids Research, Vol 24, Issue 24 4933-4939, Copyright © 1996 by Oxford University Press
PR Bianco and GM Weinstock
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 > or = 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 KmATP 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.
ARTICLES
Interaction of the RecA protein of Escherichia coli with single- stranded oligodeoxyribonucleotides
Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston 77225, USA.
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