DNA primase activity found in an alpha-like DNA polymerase obtained from Halobacterium halobium

Eur J Biochem. 1988 Aug 1;175(2):265-70. doi: 10.1111/j.1432-1033.1988.tb14192.x.

Abstract

An aphidicolin-sensitive DNA polymerase was purified from extracts of Halobacterium halobium. The analysis of this alpha-like DNA polymerase on polyacrylamide gels under denaturing conditions revealed two peptides with molecular masses of 70 kDa and 60 kDa in equal amounts. Like the DNA polymerase alpha isolated from eukaryotes, the alpha-like DNA polymerase possesses primase activity using UTP and polydeoxyadenylate as template. The primase activity was sensitive to aphidicolin and inhibited by an antiserum against the alpha-like DNA polymerase of H. halobium. The primase activity was dependent on the presence of high salt concentrations.

MeSH terms

  • Antibodies
  • DNA Polymerase II / isolation & purification*
  • DNA Polymerase II / metabolism
  • DNA Primase
  • Halobacterium / enzymology*
  • Kinetics
  • Poly A
  • RNA Nucleotidyltransferases / isolation & purification*
  • RNA Nucleotidyltransferases / metabolism
  • Templates, Genetic

Substances

  • Antibodies
  • Poly A
  • DNA Primase
  • RNA Nucleotidyltransferases
  • DNA Polymerase II