Molecular cloning of human XPAC gene homologs from chicken, Xenopus laevis and Drosophila melanogaster.
We cloned homologs of the human Xeroderma Pigmentosum Group A complementing (XPAC) gene from chicken, Xenopus laevis and Drosophila melanogaster. A comparison of the amino acid sequences of these homologs with that of the human XPAC protein revealed that in the NH2-terminal domain there are only two conserved regions, one of which is presumed to function as the nuclear localization signal, whereas the COOH-terminal domain is highly conserved, the frequency of identical amino acids in all four XPAC proteins being 50%, and the four cysteine residues predicted to form a zinc-finger motif, and three other cysteine residues are all conserved. These results strongly suggest that the COOH-terminal domain containing a zinc-finger motif plays an important role in the function of these proteins.
Shimamoto
T
T
Institute for Molecular and Cellular Biology, Osaka University, Japan.
Kohno
K
K
Tanaka
K
K
Okada
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002645:Chickens / Q000235:genetics; D003001:Cloning, Molecular; D004268:DNA-Binding Proteins / Q000235:genetics*; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000235:genetics; D015723:Gene Library; D006801:Humans; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides; D016133:Polymerase Chain Reaction / Q000379:methods; D012689:Sequence Homology, Nucleic Acid; D014982:Xenopus laevis / Q000235:genetics; D014983:Xeroderma Pigmentosum / Q000235:genetics*; D051760:Xeroderma Pigmentosum Group A Protein; D016335:Zinc Fingers / Q000235:genetics
D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D009838:Oligodeoxyribonucleotides; C497314:XPA protein, human; D051760:Xeroderma Pigmentosum Group A Protein; C497316:Xpac protein, Drosophila