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Primary Structure of the Catalytic Subunit of Human DNA Polymerase δ and Chromosomal Location of the Gene
Dominic W. Chung, Jian Zhang, Cheng-Keat Tan, Earl W. Davie, Antero G. So and Kathleen M. Downey
Proceedings of the National Academy of Sciences of the United States of America
Vol. 88, No. 24 (Dec. 15, 1991), pp. 11197-11201
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/2359211
Page Count: 5
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The catalytic subunit (Mr ≈ 124,000) of human DNA polymerase δ 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 δ. 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 δ 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 δ was localized to chromosome 19.
Proceedings of the National Academy of Sciences of the United States of America © 1991 National Academy of Sciences