Characterization of a processive form of the vaccinia virus DNA polymerase.
We have previously shown that the purified, 116-kDa DNA polymerase encoded by vaccinia virus is inherently distributive, synthesizing only a few nucleotides per template binding event under moderate reaction conditions (W. F. McDonald and P. Traktman, J. Biol. Chem. 269, 31190-31197). These properties would be incompatible with efficient DNA replication in vivo and suggest that the polymerase most probably interacts with accessory proteins that stabilize the template/polymerase interaction. Here we show that a highly processive form of the enzyme is indeed present with cytoplasmic lysates prepared from infected cells, and demonstrate that this form of the enzyme is likely to comprise the DNA polymerase in association with an early viral protein with a native molecular weight of approximately 48K.
McDonald
W F
WF
Department of Cell Biology, Cornell University Medical College, New York, New York 10021, USA.
Klemperer
N
N
Traktman
P
P
D017104:Bacteriophage M13 / Q000235:genetics; D002384:Catalysis; D002457:Cell Extracts; D002460:Cell Line; D004277:DNA, Single-Stranded / Q000378:metabolism; D004279:DNA, Viral / Q000096:biosynthesis / Q000378:metabolism; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism*; D005816:Genetic Complementation Test; D008970:Molecular Weight; D013698:Templates, Genetic; D014616:Vaccinia virus / Q000201:enzymology*; D014764:Viral Proteins / Q000378:metabolism
D002457:Cell Extracts; D004277:DNA, Single-Stranded; D004279:DNA, Viral; D014764:Viral Proteins; C090592:DNA polymerase, vaccinia virus; D004259:DNA-Directed DNA Polymerase