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TitleArchitecture of the human XPC DNA repair and stem cell coactivator complex.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 112, Issue 48, Page 14817-14822, Year 2015
Publish dateDec 1, 2015
AuthorsElisa T Zhang / Yuan He / Patricia Grob / Yick W Fong / Eva Nogales / Robert Tjian /
PubMed AbstractThe Xeroderma pigmentosum complementation group C (XPC) complex is a versatile factor involved in both nucleotide excision repair and transcriptional coactivation as a critical component of the ...The Xeroderma pigmentosum complementation group C (XPC) complex is a versatile factor involved in both nucleotide excision repair and transcriptional coactivation as a critical component of the NANOG, OCT4, and SOX2 pluripotency gene regulatory network. Here we present the structure of the human holo-XPC complex determined by single-particle electron microscopy to reveal a flexible, ear-shaped structure that undergoes localized loss of order upon DNA binding. We also determined the structure of the complete yeast homolog Rad4 holo-complex to find a similar overall architecture to the human complex, consistent with their shared DNA repair functions. Localized differences between these structures reflect an intriguing phylogenetic divergence in transcriptional capabilities that we present here. Having positioned the constituent subunits by tagging and deletion, we propose a model of key interaction interfaces that reveals the structural basis for this difference in functional conservation. Together, our findings establish a framework for understanding the structure-function relationships of the XPC complex in the interplay between transcription and DNA repair.
External linksProc Natl Acad Sci U S A / PubMed:26627236 / PubMed Central
MethodsEM (single particle)
Resolution24.0 - 25.0 Å
Structure data

EMDB-6495:
Electron microscopy of apo human XPC complex
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-6496:
Electron microscopy of apo yeast Rad4 (XPC homolog) complex
Method: EM (single particle) / Resolution: 24.0 Å

EMDB-6497:
Electron microscopy of apo human XPC complex
Method: EM (single particle) / Resolution: 24.0 Å

EMDB-6498:
Electron microscopy of DNA-bound human XPC complex
Method: EM (single particle) / Resolution: 24.0 Å

Source
  • Homo sapiens (human)
  • Saccharomyces cerevisiae (brewer's yeast)

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