Release of RNA Polymerase from Vero Cell Mitochondria After Herpes Simplex Virus Type 1 Infection
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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.
HSV Replication: Triggering and Repressing STING Functionality.
Krawczyk E, Kangas C, He B Viruses. 2023; 15(1).
PMID: 36680267 PMC: 9864509. DOI: 10.3390/v15010226.
Hines J, Ray D Mol Cell Biol. 2010; 30(6):1319-28.
PMID: 20065037 PMC: 2832486. DOI: 10.1128/MCB.01231-09.
Tanaka M, Sata T, Kawaguchi Y Virol J. 2008; 5:125.
PMID: 18940012 PMC: 2577096. DOI: 10.1186/1743-422X-5-125.
Human mitochondrial RNA polymerase primes lagging-strand DNA synthesis in vitro.
Wanrooij S, Fuste J, Farge G, Shi Y, Gustafsson C, Falkenberg M Proc Natl Acad Sci U S A. 2008; 105(32):11122-7.
PMID: 18685103 PMC: 2516254. DOI: 10.1073/pnas.0805399105.
Herpes simplex virus 1 blocks caspase-3-independent and caspase-dependent pathways to cell death.
Galvan V, Brandimarti R, Roizman B J Virol. 1999; 73(4):3219-26.
PMID: 10074175 PMC: 104085. DOI: 10.1128/JVI.73.4.3219-3226.1999.