GSBS Student Publications

Title

Human RAD52 exhibits two modes of self-association

GSBS Program

Biochemistry & Molecular Pharmacology

Publication Date

2001-03-30

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology

Document Type

Article

Disciplines

Life Sciences | Medicine and Health Sciences

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.

DOI of Published Version

10.1074/jbc.M011747200

Source

J Biol Chem. 2001 May 11;276(19):15876-80. Epub 2001 Feb 13. Link to article on publisher's site

Journal/Book/Conference Title

The Journal of biological chemistry

Related Resources

Link to article in PubMed

PubMed ID

11278978

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