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J Biol Chem, Vol. 274, Issue 37, 25979-25982, September 10, 1999
From the Department of Biochemistry, The Johns Hopkins University,
School of Public Health, Baltimore, Maryland 21205
The x-ray crystal structure of the
Escherichia coli RecA protein indicates that the phosphate
groups of the nucleotide cofactor are bound by a loop whose amino acid
sequence (66GPESSGKT73) corresponds to a
consensus phosphate binding loop sequence (GXXXXGK[T/S]) found in many NTP-binding proteins. As part of an investigation of the
role of the P-loop in ATP hydrolysis, we prepared a mutant RecA protein
in which serine 69 was replaced by a glycine residue. We have found
that the [S69G]RecA mutation has a differential effect on the
hydrolysis of various nucleoside triphosphates. The [S69G]RecA
protein catalyzes the single-stranded DNA-dependent hydrolysis of rATP, ddATP, and dATP with turnover numbers of 10, 20, and 36 min
1, respectively. The wild type RecA protein, in
contrast, hydrolyzes each of these nucleoside triphosphates with
similar turnover numbers of 20-24 min1. Significantly,
the [S69G]RecA protein promotes strand exchange with all three
nucleoside triphosphates, and the rate of strand exchange is directly
proportional to the rate of hydrolysis of each of the nucleotide
cofactors. These findings with the [S69G]RecA protein provide support
for the existence of a mechanistic coupling between NTP hydrolysis and
DNA strand exchange.
This article has been cited by other articles:
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  F. S. Katz and F. R. Bryant Three-strand Exchange by the Escherichia coli RecA Protein Using ITP as a Nucleotide Cofactor: MECHANISTIC PARALLELS WITH THE ATP-DEPENDENT REACTION OF THE RecA PROTEIN FROM STREPTOCOCCUS PNEUMONIAE J. Biol. Chem., September 19, 2003; 278(38): 35889 - 35896. [Abstract] [Full Text] [PDF]
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S. E. Steffen, F. S. Katz, and F. R. Bryant Complete Inhibition of Streptococcus pneumoniae RecA Protein-catalyzed ATP Hydrolysis by Single-stranded DNA-binding Protein (SSB Protein). IMPLICATIONS FOR THE MECHANISM OF SSB PROTEIN-STIMULATED DNA STRAND EXCHANGE J. Biol. Chem., April 19, 2002; 277(17): 14493 - 14500. [Abstract] [Full Text] [PDF]
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 M. E. Robu, R. B. Inman, and M. M. Cox RecA protein promotes the regression of stalled replication forks in vitro PNAS, July 17, 2001; 98(15): 8211 - 8218. [Abstract] [Full Text] [PDF]
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E. A. Namsaraev and P. Berg Rad51 Uses One Mechanism to Drive DNA Strand Exchange in Both Directions J. Biol. Chem., February 11, 2000; 275(6): 3970 - 3976. [Abstract] [Full Text] [PDF]
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S. Nayak, E. L. Hildebrand, and F. R. Bryant ADP-dependent DNA Strand Exchange by the Mutant [P67G/E68A]RecA Protein. EVIDENCE FOR AN INVOLVEMENT OF ADP IN RecA PROTEIN-MEDIATED BRANCH MIGRATION J. Biol. Chem., April 27, 2001; 276(18): 14933 - 14938. [Abstract] [Full Text] [PDF]
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