TY - JOUR
T1 - 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
AU - Henning, Karla A.
AU - Peterson, Carolyn
AU - Legerski, Randy
AU - Friedberg, Errol C.
N1 - Funding Information:
These studies were supported by research grants CA44247 (ECF) and CA52461 (RL) from the USPHS. We thank our laboratory colleagues for helpful discussions and review of the manuscript and Eh" Chikahide Masutani for communicating unpublished results.
PY - 1994/2/11
Y1 - 1994/2/11
N2 - 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.
AB - 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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U2 - 10.1093/nar/22.3.257
DO - 10.1093/nar/22.3.257
M3 - Article
C2 - 8127661
AN - SCOPUS:0028217601
SN - 0305-1048
VL - 22
SP - 257
EP - 261
JO - Nucleic acids research
JF - Nucleic acids research
IS - 3
ER -