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J. Biochem, 2003, Vol. 133, No. 5 593-597
© 2003 Japanese Biochemical Society

BIOCHEMISTRY

pH- and Salt-Dependent Self-Assembly of Human Rad51 Protein Analyzed as Fluorescence Resonance Energy Transfer between Labeled Proteins

Ken-ichi Yoshioka, Yoshiko Yumoto-Yoshioka, Fabrice Fleury and Masayuki Takahashi+

FRE2230, Laboratory of Biocatalysis, Centre National de la Recherche Scientifique and Universite de Nantes, F-44322 Nantes cedex 3, France

Human HsRad51 protein assembles on a DNA molecule through cooperative binding and forms a long filament for homologous recombination. We have characterized the self-assembly of HsRad51 by measuring the fluorescence resonance energy transfer from the fluorescein-labeled protein to the rhodamine-labeled protein. Self-assembly quickly reached equilibrium and can be described by the head-to-tail polymerization of monomers, like that of its procaryotic homologue, RecA. It depended strongly on pH and was inhibited by high salt concentrations, indicating that ionic interactions between negatively and positively charged aminoacid residues are important. By contrast, neither ATP nor ADP significantly affected the reaction.

+ To whom correspondence should be addressed. Tel and Fax: +33-2-51-12-56-36, E-mail: Masayuki.Takahashi{at}chimbio.univ-nantes.fr


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