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Papers In Press, published online ahead of print August 14, 2001
Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706-1544
Corresponding Author: cox{at}biochem.wisc.edu
The bacterial RecA protein and the homologous Rad51 protein in eukaryotes both bind to single-stranded DNA (ssDNA), align it with a homologous duplex, and promote an extensive strand exchange between them. Both reactions have properties, including a tolerance of base analog substitutions that tend to eliminate the potential for major groove hydrogen bonding, that suggest a common molecular process underlies the DNA strand exchange promoted by RecA and Rad51. However, optimal conditions for the DNA pairing and DNA strand exchange reactions promoted by the RecA and Rad51 proteins in vitro are substantially different. When conditions are optimized independently for both proteins, RecA promotes DNA pairing reactions with short oligonucleotides at a faster rate than Rad51. For both proteins, conditions that improve DNA pairing can inhibit extensive DNA strand exchange reactions in the absence of ATP hydrolysis. Extensive strand exchange requires a spooling of duplex DNA into a recombinase-ssDNA complex, a process that can be halted by any interaction elsewhere on the same duplex that restricts free rotation of the duplex and/or complex; ie., the reaction can get stuck. Optimization of an extensive DNA strand exchange without ATP hydrolysis requires conditions that decrease nonproductive interactions of recombinase-ssDNA complexes with the duplex DNA substrate.
J. Biol. Chem, 10.1074/jbc.M105678200
Submitted on June 20, 2001
Revised on August 7, 2001
Accepted on August 13, 2001
DNA pairing and strand exchange by the E. coli REcA and yeast Rad41 proteins: On the importance of not getting stuck
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