Characterization of a processive form of the vaccinia virus DNA polymerase.

Abstract:

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.

Polymerases:

Topics:

Historical Protein Properties (MW, pI, ...), Exonuclease Activity, Source / Purification, Nucleotide Incorporation, Kinetic Parameters

Status:

new topics/pols set partial results complete validated

Results:

Polymerase Reference Property Result Context
Vaccinia Virus Pol McDonald WF1997 Molecular Weight 1.16E+05 Dalton
Vaccinia Virus Pol McDonald WF1997 3-5' Exonuclease (proofreading) Yes
Vaccinia Virus Pol McDonald WF1997 Cloned or native Native organism
Vaccinia Virus Pol McDonald WF1997 5-3' Exonuclease Yes
Vaccinia Virus Pol McDonald WF1997 Full length or truncated Full length
Vaccinia Virus Pol McDonald WF1997 Processivity 7200bp
Vaccinia Virus Pol McDonald WF1997 Vmax 30 /second Reaction: Nucleotide incorporation; Substrate: dNTPs

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