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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-31256

Enzlin, J H; Schärer, O D (2002). The active site of the DNA repair endonuclease XPF-ERCC1 forms a highly conserved nuclease motif. EMBO Journal, 21(8):2045-2053.

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XPF-ERCC1 is a structure-specific endonuclease involved in nucleotide excision repair, interstrand crosslink repair and homologous recombination. So far, it has not been shown experimentally which subunit of the heterodimer harbors the nuclease activity and which amino acids contribute to catalysis. We used an affinity cleavage assay and located the active site to amino acids 670-740 of XPF. Point mutations generated in this region were analyzed for their role in nuclease activity, metal coordination and DNA binding. Several acidic and basic residues turned out to be required for nuclease activity, but not DNA binding. The separation of substrate binding and catalysis by XPF-ERCC1 will be invaluable in studying the role of this protein in various DNA repair processes. Alignment of the active site region of XPF with proteins belonging to the Mus81 family and a putative archaeal RNA helicase family reveals that seven of the residues of XPF involved in nuclease activity are absolutely conserved in the three protein families, indicating that they share a common nuclease motif.


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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Institute of Molecular Cancer Research
07 Faculty of Science > Institute of Molecular Cancer Research
Dewey Decimal Classification:570 Life sciences; biology
Deposited On:09 Jul 2010 09:12
Last Modified:05 Apr 2016 13:57
Publisher:Nature Publishing Group
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:10.1093/emboj/21.8.2045
PubMed ID:11953324

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