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Human DNA polymerase alpha gene expression is cell proliferation dependent and its primary structure is similar to both prokaryotic and eukaryotic replicative DNA polymerases.
Author(s) -
Wong S. W.,
Wahl A. F.,
Yuan P. M.,
Arai N.,
Pearson B. E.,
Arai K.,
Korn D.,
Hunkapiller M. W.,
Wang T. S.
Publication year - 1988
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1988.tb02781.x
Subject(s) - biology , dna polymerase , dna polymerase ii , microbiology and biotechnology , dna clamp , polymerase , dna polymerase mu , dna polymerase i , dna polymerase delta , dna replication , eukaryotic dna replication , dna , gene , genetics , rna , circular bacterial chromosome , reverse transcriptase
We have isolated cDNA clones encoding the human DNA polymerase alpha catalytic polypeptide. Studies of the human DNA polymerase alpha steady‐state mRNA levels in quiescent cells stimulated to proliferate, or normal cells compared to transformed cells, demonstrate that the polymerase alpha mRNA, like its enzymatic activity and de novo protein synthesis, positively correlates with cell proliferation and transformation. Analysis of the deduced 1462‐amino‐acid sequence reveals six regions of striking similarity to yeast DNA polymerase I and DNA polymerases of bacteriophages T4 and phi 29, herpes family viruses, vaccinia virus and adenovirus. Three of these conserved regions appear to comprise the functional active site required for deoxynucleotide interaction. Two putative DNA interacting domains are also identified.