Human RAD52 Exhibits Two Modes of Self-association

Wasantha Ranatunga, Doba Jackson, Janice A. Lloyd, Anthony L. Forget, Kendall L. Knight, Gloria E.O. Borgstahl

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45 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)15876-15880
Number of pages5
JournalJournal of Biological Chemistry
Volume276
Issue number19
DOIs
Publication statusPublished - May 11 2001

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Ranatunga, W., Jackson, D., Lloyd, J. A., Forget, A. L., Knight, K. L., & Borgstahl, G. E. O. (2001). Human RAD52 Exhibits Two Modes of Self-association. Journal of Biological Chemistry, 276(19), 15876-15880. https://doi.org/10.1074/jbc.M011747200