Domains in the XPA protein important in its role as a processivity factor

Claudine L. Bartels, Muriel W. Lambert

Research output: Contribution to journalArticlepeer-review

24 Scopus citations

Abstract

XPA is a protein essential for nucleotide excision repair (NER) where it is thought to function in damage recognition/verification. We have proposed an additional role, that of a processivity factor, conferring a processive mechanism of action on XPF and XPG, the endonucleases, involved in NER. The present study was undertaken to examine the domain(s) in the XPA gene that are important for the ability of the XPA protein to function as a processivity factor. Using site-directed mutagenesis, mutations were created in several of the exons of XPA and mutant XPA proteins produced. The results showed that the DNA binding domain of XPA is critical for its ability to act as a processivity factor. Mutations in both the zinc finger motif and the large basic cleft in this domain eliminated the ability of XPA to confer a processive mechanism of action on the endonucleases involved in NER.

Original languageEnglish (US)
Pages (from-to)219-225
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume356
Issue number1
DOIs
StatePublished - Apr 27 2007

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Keywords

  • DNA repair
  • Processive mechanism of action
  • XPA protein
  • Xeroderma pigmentosum

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