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Strand pairing by Rad54 and Rad51 is enhanced by chromatin

descriptionPublicationkeyboard_double_arrow_right Article 01 Nov 2002 English Publisher:Cold Spring Harbor LaboratoryJournal:Genes & Development, volume 16, pages 2,767-2,771 (issn: 0890-9369, eissn: 1549-5477,

Authors: Vassilios Alexiadis; James T. Kadonaga;

doi: 10.1101/gad.1032102

pmid: 12414729

pmc: PMC187467

Strand pairing by Rad54 and Rad51 is enhanced by chromatin

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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.

Related Organizations

University of California, San Diego
United States

Keywords

DNA-Binding Proteins, DNA Repair, Egg Proteins, DNA Helicases, Animals, Drosophila Proteins, Drosophila, Rad51 Recombinase, Base Pairing, Chromatin

15 Research products, page 1 of 2

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