A novel DNA-binding protein associated with DNA polymerase-alpha in pea stimulates polymerase activity on infrequently primed templates.
A 42 kDa DNA-binding protein is associated with DNA polymerase-alpha-primase in pea (Pisum sativum). In a previous publication it was shown that the protein has strong preference for ds-ss junctions in DNA, including the cohesive termini generated by restriction endonucleases. In this paper it is shown that when the DNA-binding protein is added back to polymerase-primase, the protein stimulates the activity of the polymerase. The stimulation is particularly marked when M13 DNA, primed with a single sequencing primer or primed with oligoribonucleotides by the polymerase's associated primase activity, is used as a template. The stimulation of polymerase activity is not caused by an increase in processivity. These data lead to the suggestion that the 42 kDa DNA-binding protein is a primer-recognition protein.
Bryant
J A
JA
School of Biological Sciences, University of Exeter, Exeter EX4 4QG, UK. Department of Biological Sciences, University of Illinois, Chicago, IL 60607-7060, USA. J.A.Bryant@exeter.ac.uk
Brice
D C
DC
Fitchett
P N
PN
Anderson
L E
LE
D000818:Animals; D002417:Cattle; D004256:DNA Polymerase I / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004789:Enzyme Activation; D010940:Plant Proteins / Q000378:metabolism*; D011485:Protein Binding; D013698:Templates, Genetic
D004268:DNA-Binding Proteins; D010940:Plant Proteins; D004256:DNA Polymerase I