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Nucleic Acids Research, 1994, Vol. 22, No. 3 257-261
© 1994

MOLECULAR BIOLOGY

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 Peterson1, Randy Legerski1 and Errol C. Friedberg*

Laboratory of Molecular Pathology, Department of Pathology, University of Texas Southwestern Medical Center Dallas, TX 75235 1Department of Molecular Genetics, University of Texas M.D.Anderson Cancer Center Houston, TX 77030, USA

*To whom correspondence should be addressed

Received December 17, 1993. Accepted December 21, 1993.

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.


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