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Rad54 protein possesses chromatin-remodeling activity stimulated by the Rad51-ssDNA nucleoprotein filament.
Alexeev A, Mazin A, Kowalczykowski SC
Nat Struct Biol 2003 Mar 10(3):182-6 [abstract on PubMed] [related articles] [order article]
Selected by | Peter Becker / Dale Ramsden
First evaluation 4 Apr 2003 | Latest evaluation 7 May 2003
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Faculty Comments
Faculty Member Comments
Peter Becker
Adolf-Butenandt-Institut, Germany
DEVELOPMENTAL BIOLOGY

New Finding
Sometimes one wonders how complex DNA recombination processes can occur with DNA wrapped up in nucleosomes. This paper shows that one of the protagonists of yeast recombinational repair, Rad54, is a remodeling ATPase able to induce sliding of nucleosomes on DNA. The sliding activity is stimulated by contact with a Rad51-ssDNA complex. Rad54 may, therefore, move nucleosomes during the search for sequences homologous to the DNA break. This is a nice example of how nucleosome remodeling is integrated into a more complex process.

Evaluated 7 May 2003
Dale Ramsden
University of North Carolina, United States
STRUCTURAL BIOLOGY

New Finding
This paper provides the first clear argument that the homologous recombination co-factor rad54 can restructure chromatin. The authors determine that Rad54 alone is sufficient to remodel mononucleosomes, but this activity is strongly stimulated by the additional presence of a Rad51 nucleoprotein filament. Together with other recent reports, a picture is emerging of a complex multi-protein machine well designed for recombination in the context of natural chromosomes.

Evaluated 4 Apr 2003
Faculty Comments

How to cite the Faculty of 1000 evaluation(s) for this paper

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Faculty of 1000: evaluations for Alexeev A et al Nat Struct Biol 2003 Mar 10 (3) :182-6 http://www.f1000biology.com/article/12577053/evaluation

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Peter Becker: Faculty of 1000, 7 May 2003 http://www.f1000biology.com/article/12577053/evaluation

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