Abstract
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 cerevisiae Rad4 protein sequences is observed, suggesting that these proteins are functional homologs.
MeSH Terms
Amino Acid Sequence
Animals
Base Sequence
Cloning, Molecular
DNA, Complementary/genetics
DNA-Binding Proteins
Drosophila melanogaster/genetics
Fungal Proteins/genetics
Genes, Fungal
Genes, Insect
Humans
Molecular Sequence Data
Nuclear Proteins/chemistry,genetics
Restriction Mapping
Saccharomyces cerevisiae/genetics
Schizosaccharomyces pombe Proteins
Sequence Alignment
Sequence Homology, Amino Acid
Transglutaminases
Xeroderma Pigmentosum/genetics
Chemicals
DNA, Complementary
DNA-Binding Proteins
Fungal Proteins
Nuclear Proteins
RAD4 protein, S pombe
Schizosaccharomyces pombe Proteins
Transglutaminases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Henning K A
Department of Pathology, University of Texas Southwestern Medical Center, Dallas 75235.
Peterson C
Legerski R
Friedberg E C
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