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J. Biol. Chem., Vol. 261, Issue 18, 8276-8282, Jun, 1986
SK Neuendorf and MM Cox
We have examined the exchange of recA protein between stable complexes
formed with single-stranded DNA (ssDNA) and (a) other complexes and (b) a
pool of free recA protein. We have also examined the relationship of ATP
hydrolysis to these exchange reactions. Exchange was observed between two
different recA X ssDNA complexes in the presence of ATP. Complete
equilibration between two sets of complexes occurred with a t1/2 of 3-7 min
under a set of conditions previously found to be optimal for recA
protein-promoted DNA strand exchange. Approximately 200 ATPs were
hydrolyzed for every detected migration of a recA monomer from one complex
to another. This exchange occurred primarily between adjacent complexes,
however. Little or no exchange was observed between recA X ssDNA complexes
and the free recA protein pool, even after several hundred molecules of ATP
had been hydrolyzed for every recA monomer present. ATP hydrolysis is not
coupled to complete dissociation or association of recA protein from or
with recA X ssDNA complexes under these conditions.
Exchange of recA protein between adjacent recA protein-single-stranded DNA complexes
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Q. Shan and M. M. Cox RecA Filament Dynamics during DNA Strand Exchange Reactions J. Biol. Chem., April 25, 1997; 272(17): 11063 - 11073. [Abstract] [Full Text] [PDF]
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Q. Shan, M. M. Cox, and R. B. Inman DNA Strand Exchange Promoted by RecA K72R J. Biol. Chem., March 8, 1996; 271(10): 5712 - 5724. [Abstract] [Full Text] [PDF]
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L. E. Iype, R. B. Inman, and M. M. Cox Blocked RecA Protein-mediated DNA Strand Exchange Reactions Are Reversed by the RuvA and RuvB Proteins J. Biol. Chem., August 18, 1995; 270(33): 19473 - 19480. [Abstract] [Full Text] [PDF]
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