Strand pairing by Rad54 and Rad51 is enhanced by chromatin.
We investigated the role of chromatin in the catalysis of homologous strand pairing by Rad54 and Rad51. Rad54 is related to the ATPase subunits of chromatin-remodeling factors, whereas Rad51 is related to bacterial RecA. In the absence of superhelical tension, we found that the efficiency of strand pairing with chromatin is >100-fold higher than that with naked DNA. In addition, we observed that Rad54 and Rad51 function cooperatively in the ATP-dependent remodeling of chromatin. These findings indicate that Rad54 and Rad51 have evolved to function with chromatin, the natural substrate, rather than with naked DNA.
Alexiadis
Vassilios
V
Section of Molecular Biology, University of California, San Diego, La Jolla, California 92093-0347, USA.
Kadonaga
James T
JT
D000818:Animals; D020029:Base Pairing / Q000235:genetics; D002843:Chromatin / Q000235:genetics* / Q000378:metabolism; D004265:DNA Helicases; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism; D004330:Drosophila; D029721:Drosophila Proteins; D004527:Egg Proteins; D051135:Rad51 Recombinase
D002843:Chromatin; D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D004527:Egg Proteins; D051135:Rad51 Recombinase; C495149:spn-A protein, Drosophila; C108443:okr protein, Drosophila; D004265:DNA Helicases