Open AccessDNA primase activity found in an α‐like DNA polymerase obtained from Halobacterium halobium
Author(s) -
NAKAYAMA Masashi,
BENMAHREZ Kamel,
KOHIYAMA Masamichi
Publication year - 1988
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1988.tb14192.x
Subject(s) - primase , dna polymerase , aphidicolin , polymerase , biology , microbiology and biotechnology , dna clamp , dna polymerase ii , dna , biochemistry , polymerase chain reaction , gene , reverse transcriptase
An aphidicolin‐sensitive DNA polymerase was purified from extracts of Halobacterium halobium. The analysis of this a‐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 α isolated from eukaryotes, the α‐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 α‐like DNA polymerase of H. halobium. The primase activity was dependent on the presence of high salt concentrations.