DC Field | Value | Language |
---|---|---|
dc.contributor.author | Pelton, JG | ko |
dc.contributor.author | Wemmer, DE | ko |
dc.contributor.author | Choi, Byong-Seok | ko |
dc.contributor.author | Choi, YJ | ko |
dc.contributor.author | Ryu, KS | ko |
dc.contributor.author | Ko, YM | ko |
dc.contributor.author | Chae, YK | ko |
dc.date.accessioned | 2013-03-07T19:31:31Z | - |
dc.date.available | 2013-03-07T19:31:31Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2005-08 | - |
dc.identifier.citation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.280, no.31, pp.28644 - 28652 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/10203/91090 | - |
dc.description.abstract | XPF and ERCC1 exist as a heterodimer to be stable and active in cells and catalyze DNA cleavage on the 5'-side of a lesion during nucleotide excision repair. To characterize the specific interaction between XPF and ERCC1, we expressed the human ERCC1 binding domain of XPF (XPF-EB) and the XPF binding domain of ERCC1 (ERCC1-FB) in Escherichia coli. Milligram quantities of a heterodimer were characterized with gel filtration chromatography, an Ni2+-NTA binding assay, and analytical ultracentrifugation. Cross-linking experiments at high salt concentrations revealed that XPF interacts with ERCC1 mainly through hydrophobic interactions. XPF-EB was also shown to homodimerize in the absence of ERCC1. NMR cross-saturation methods were applied to map the residues involved in formation of the XPF-(EBXPF)-X-.-EB homodimer and the XPF-EB -ERCC1-FB heterodimer. Helix H3 and the C-terminal region of XPF-EB were either within or in close proximity to the homodimer interface, whereas the ERCC1-FB binding site of XPF-EB was distributed across helix H1, a small part of H2, H3, and the C-terminal region, most of which exhibited large changes in chemical shift upon ERCC1 binding. The XPF-EB heterodimeric interface is larger than the XPF-EB homodimeric one, which could explain why XPF has a stronger affinity for ERCC1 than for a second molecule of XPF. The XPF binding sites of ERCC1 were located in helices H1 and H3 and in the C-terminal region, similar to the involved surface of XPF. We used cross-saturation data and the crystal structure of related proteins to model the two complexes. | - |
dc.language | English | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.subject | NUCLEOTIDE EXCISION-REPAIR | - |
dc.subject | PIGMENTOSUM GROUP-F | - |
dc.subject | XERODERMA-PIGMENTOSUM | - |
dc.subject | DNA-BINDING | - |
dc.subject | PROTEIN | - |
dc.subject | ERCC1 | - |
dc.subject | ENDONUCLEASE | - |
dc.subject | XPF | - |
dc.subject | NUCLEASE | - |
dc.subject | RECOGNITION | - |
dc.title | Biophysical characterization of the interaction domains and mapping of the contact residues in the XPF-ERCC1 complex | - |
dc.type | Article | - |
dc.identifier.wosid | 000230857300055 | - |
dc.identifier.scopusid | 2-s2.0-23344452570 | - |
dc.type.rims | ART | - |
dc.citation.volume | 280 | - |
dc.citation.issue | 31 | - |
dc.citation.beginningpage | 28644 | - |
dc.citation.endingpage | 28652 | - |
dc.citation.publicationname | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.identifier.doi | 10.1074/jbc.M501083200 | - |
dc.contributor.localauthor | Choi, Byong-Seok | - |
dc.contributor.nonIdAuthor | Pelton, JG | - |
dc.contributor.nonIdAuthor | Wemmer, DE | - |
dc.contributor.nonIdAuthor | Choi, YJ | - |
dc.contributor.nonIdAuthor | Ryu, KS | - |
dc.contributor.nonIdAuthor | Ko, YM | - |
dc.contributor.nonIdAuthor | Chae, YK | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | NUCLEOTIDE EXCISION-REPAIR | - |
dc.subject.keywordPlus | PIGMENTOSUM GROUP-F | - |
dc.subject.keywordPlus | XERODERMA-PIGMENTOSUM | - |
dc.subject.keywordPlus | DNA-BINDING | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | ERCC1 | - |
dc.subject.keywordPlus | ENDONUCLEASE | - |
dc.subject.keywordPlus | XPF | - |
dc.subject.keywordPlus | NUCLEASE | - |
dc.subject.keywordPlus | RECOGNITION | - |
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