PRIMARY STRUCTURE OF THE CATALYTIC SUBUNIT OF HUMAN DNA POLYMERASE-DELTA AND CHROMOSOMAL LOCATION OF THE GENE

The catalytic subunit (M(r) almost-equal-to 124,000) of human DNA polymerase-delta has been cloned by PCR using poly(A)+ RNA from HepG2 cells and primers designed from the amino acid sequence of regions highly conserved between bovine and yeast DNA polymerase-delta. The human cDNA was 3443 nucleotides in length and coded for a polypeptide of 1107 amino acids. The enzyme was 94% identical to bovine DNA polymerase-delta and contained the numerous highly conserved regions previously observed in the bovine and yeast enzymes. The human enzyme also contained two putative zinc-finger domains in the carboxyl end of the molecule, as well as a putative nuclear localization signal at the amino-terminal end. The gene coding for human DNA polymerase-delta was localized to chromosome 19.