title: Strand pairing by Rad54 and Rad51 is enhanced by chromatin.
abstract: 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.
authors.affiliation: Section of Molecular Biology, University of California, San Diego, La Jolla, California 92093-0347, USA.
authors.forename: Vassilios
authors.initials: V
authors.lastname: Alexiadis
authors.forename: James T
authors.initials: JT
authors.lastname: Kadonaga
mesh_terms: 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
chemical_list: 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