Cloning the Drosophila homolog of the xeroderma pigmentosum complementation group C gene reveals homology between the predicted human and drosophila polypeptides and that encoded by the yeast RAD4 gene

Karla A. Henning, Carolyn Peterson, Randy Legerski, Errol C. Friedberg

Research output: Contribution to journalArticle

20 Scopus citations


A human xeroderma pigmentosum group C (XPC) cDNA has been previously isolated by functional complementation (Legerski and Peterson, Nature, 359, 70-73, 1992). Sequence analysis did not reveal protein motifs which might suggest a possible biochemical function for the putative XPC protein. In order to identify functional domains in the translated XPC sequence the homologous gene from Drosophila melanogaster, designated XPCDM, was cloned by DNA hybridization. Sequence analysis of an apparently full-length cDNA revealed an open reading frame which can encode a predicted polypeptide of 1293 amino acids. Significant homology of the C-terminal 346 amino acids with both the human XPC and Saccharomyces cerevlslae Rad4 protein sequences is observed, suggesting that these proteins are functional homologs.

Original languageEnglish (US)
Pages (from-to)257-261
Number of pages5
JournalNucleic acids research
Issue number3
StatePublished - Feb 11 1994


ASJC Scopus subject areas

  • Genetics

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