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J. Biol. Chem., Vol. 265, Issue 16, 9043-9054, Jun, 1990
JE Lindsley and MM Cox
RecA protein primarily associates with and dissociates from opposite ends
of nucleoprotein filaments formed on linear duplex DNA. RecA nucleoprotein
filaments that are hydrolyzing ATP therefore engage in a dynamic process
under some conditions that has some of the properties of treadmilling. We
have also investigated whether the net polymerization of recA protein at
one end of the filament and/or a net depolymerization at the other end
drives unidirectional strand exchange. There is no demonstrable correlation
between recA protein association/dissociation and the strand exchange
reaction. RecA protein- mediated DNA strand exchange is affected minimally
by changes in reaction conditions (dilution, pH shift, or addition of small
amounts of adenosine-5'-O-(3-thiotriphosphate) that have large and
demonstrable effects on recA protein association, dissociation, or both.
Rather than driving strand exchange, these assembly and disassembly
processes may simply represent the mechanism by which recA nucleoprotein
filaments are recycled in the cell.
Assembly and disassembly of RecA protein filaments occur at opposite filament ends. Relationship to DNA strand exchange
Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin, Madison 53706.
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