A DNA primase that copurifies with the major DNA polymerase from the yeast Saccharomyces cerevisiae

J Biol Chem. 1984 Jun 25;259(12):7936-40.


Biochemical fractionation of the yeast Saccharomyces cerevisiae has revealed a novel DNA primase activity that copurifies with the major DNA polymerase activity. In the presence of RNA precursors and single-stranded DNA (poly(dT), M13), the DNA primase synthesizes discrete length oligoribonucleotides (apparent length, 8-12 nucleotides) as well as longer RNA chains that appear to be multiples of a modal length of 11-12 nucleotides. When DNA precursors are also present, the oligoribonucleotides are utilized by the accompanying DNA polymerase as primers for DNA synthesis. Copurification of these two enzymatic activities suggests their association in a physical complex which may function in the synthesis of Okazaki fragments at chromosomal replication forks.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Chromatography, DEAE-Cellulose
  • Chromatography, Gel
  • DNA Primase
  • DNA, Single-Stranded / metabolism
  • DNA-Directed DNA Polymerase / isolation & purification*
  • Electrophoresis, Polyacrylamide Gel
  • RNA Nucleotidyltransferases / isolation & purification*
  • Saccharomyces cerevisiae / enzymology*


  • DNA, Single-Stranded
  • DNA Primase
  • RNA Nucleotidyltransferases
  • DNA-Directed DNA Polymerase