Human DNA polymerase alpha gene expression is cell proliferation dependent and its primary structure is similar to both prokaryotic and eukaryotic replicative DNA polymerases

EMBO J. 1988 Jan;7(1):37-47.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cell Division
  • Cloning, Molecular
  • DNA Polymerase II / genetics*
  • DNA Replication*
  • DNA-Directed DNA Polymerase / genetics*
  • Gene Expression Regulation*
  • Genes*
  • Humans
  • Molecular Sequence Data
  • RNA, Messenger / genetics*
  • Sequence Homology, Nucleic Acid
  • Transcription, Genetic*
  • Viruses / enzymology
  • Viruses / genetics

Substances

  • RNA, Messenger
  • DNA Polymerase II
  • DNA-Directed DNA Polymerase

Associated data

  • GENBANK/X06745