Release of RNA polymerase from vero cell mitochondria after herpes simplex virus type 1 infection.
Infection of Vero cells with herpes simplex virus type 1 results in the appearance in soluble extracts of a DNA primase activity. The partially purified enzyme, Mr, approximately 100,000, is identical in resistance to alpha-amanitin, pH profile, Mg2+ dependence, salt sensitivity, and KmATP to the catalytic core of Vero cell mitochondrial RNA polymerase. Moreover, the products synthesized are those expected of an RNA polymerase rather than a DNA primase. Inasmuch as the enzyme is not present in soluble extracts of uninfected Vero cells, we presume that the specific appearance of RNA polymerase in extracts of herpesvirus-infected cells results from infection-induced disruption of the mitochondrial membrane, followed by release of the enzyme into the cytosol.
Tsurumi
T
T
Department of Biochemistry, Beckman Center, Stanford University, California 94305-5307.
Lehman
I R
IR
D000818:Animals; D002472:Cell Transformation, Viral; D012321:DNA-Directed RNA Polymerases / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008928:Mitochondria / Q000201:enzymology*; D018139:Simplexvirus / Q000201:enzymology / Q000235:genetics*; D014709:Vero Cells
D012321:DNA-Directed RNA Polymerases