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J. Biol. Chem., Vol. 276, Issue 19, 15876-15880, May 11, 2001
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From the The human RAD52 protein plays an important role
in the earliest stages of chromosomal double-strand break repair via
the homologous recombination pathway. Individual subunits of RAD52
self-associate into rings that can then form higher order complexes.
RAD52 binds to double-strand DNA ends, and recent studies suggest that
the higher order self-association of the rings promotes DNA
end-joining. Earlier studies defined the self-association domain of
RAD52 to a unique region in the N-terminal half of the protein. Here we show that there are in fact two experimentally separable
self-association domains in RAD52. The N-terminal self-association
domain mediates the assembly of monomers into rings, and the previously
unidentified domain in the C-terminal half of the protein mediates
higher order self-association of the rings.
Human RAD52 Exhibits Two Modes of Self-association*
§,§,
Department of Chemistry, University of
Toledo, Toledo, Ohio 43606-3390 and the ¶ Department of
Biochemistry and Molecular Pharmacology, University of Massachusetts
Medical School, Worcester, Massachusetts 01655-0103
*
This work was supported by the United States Army Medical
Research and Material Command under DAMD17-98-1-8251 (to
G. E. O. B.) and National Institutes of Health Grant GM44772 (to
K. L. K.). Brookhaven National Laboratory STEM is supported by
National Institutes of Health Grant P41-RR01777 and partially supported by the Department of Energy and Office of Biological and Environmental Research.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of
Chemistry, University of Toledo, 2801 W. Bancroft St., Toledo, OH
43606-3390. Tel.: 419-530-1501; Fax: 419-530-4033; E-mail:
gborgst@uoft02.utoledo.edu.
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