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dc.contributor.authorRanatunga, Wasantha
dc.contributor.authorJackson, Doba
dc.contributor.authorLloyd, Janice A.
dc.contributor.authorForget, Anthony L.
dc.contributor.authorKnight, Kendall L.
dc.contributor.authorBorgstahl, Gloria E. O.
dc.date2022-08-11T08:08:56.000
dc.date.accessioned2022-08-23T16:13:13Z
dc.date.available2022-08-23T16:13:13Z
dc.date.issued2001-03-30
dc.date.submitted2008-05-12
dc.identifier.citationJ Biol Chem. 2001 May 11;276(19):15876-80. Epub 2001 Feb 13. <a href="http://dx.doi.org/10.1074/jbc.M011747200">Link to article on publisher's site</a>
dc.identifier.issn0021-9258 (Print)
dc.identifier.doi10.1074/jbc.M011747200
dc.identifier.pmid11278978
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33569
dc.description.abstractThe 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.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11278978&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1074/jbc.M011747200
dc.subjectDNA Repair; DNA-Binding Proteins; Humans; Kinetics; Microscopy, Electron; Mutagenesis; Peptide Fragments; Recombinant Proteins; Sequence Deletion; Thioredoxins
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleHuman RAD52 exhibits two modes of self-association
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume276
dc.source.issue19
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/24
dc.identifier.contextkey507280
html.description.abstract<p>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.</p>
dc.identifier.submissionpathgsbs_sp/24
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.source.pages15876-80


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