Characterization of a processive form of the vaccinia virus DNA polymerase. Virology 1997 Jul 21;234(1):168-75
Date
07/21/1997Pubmed ID
9234958DOI
10.1006/viro.1997.8639Scopus ID
2-s2.0-0031582627 (requires institutional sign-in at Scopus site) 37 CitationsAbstract
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.
Author List
McDonald WF, Klemperer N, Traktman PMESH terms used to index this publication - Major topics in bold
Bacteriophage M13Catalysis
Cell Extracts
Cell Line
DNA, Single-Stranded
DNA, Viral
DNA-Directed DNA Polymerase
Genetic Complementation Test
Molecular Weight
Templates, Genetic
Vaccinia virus
Viral Proteins
