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.

[1]  I. Lehman,et al.  Herpes simplex virus 1 helicase-primase: a complex of three herpes-encoded gene products. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[2]  A. M. Holmes,et al.  Identification and characterization of a DNA primase activity present in herpes simplex virus type 1-infected HeLa cells , 1988, Journal of virology.

[3]  I. Lehman,et al.  A DNA binding protein specific for an origin of replication of herpes simplex virus type 1. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[4]  I. Lehman,et al.  Yeast mitochondrial RNA polymerase. Purification and properties of the catalytic subunit. , 1986, The Journal of biological chemistry.

[5]  T. Wong,et al.  DNA primase of human mitochondria is associated with structural RNA that is essential for enzymatic activity , 1986, Cell.

[6]  T. Wong,et al.  Isolation and characterization of a DNA primase from human mitochondria. , 1985, The Journal of biological chemistry.

[7]  T. S. Wang,et al.  DNA primase from KB cells. Characterization of a primase activity tightly associated with immunoaffinity-purified DNA polymerase-alpha. , 1984, The Journal of biological chemistry.

[8]  M. Walberg,et al.  In vitro transcription of human mitochondrial DNA. Identification of specific light strand transcripts from the displacement loop region. , 1983, The Journal of biological chemistry.

[9]  S. Weller,et al.  Genetic analysis of temperature-sensitive mutants which define the gene for the major herpes simplex virus type 1 DNA-binding protein , 1983, Journal of virology.

[10]  R. Conaway,et al.  A DNA primase activity associated with DNA polymerase alpha from Drosophila melanogaster embryos. , 1982, Proceedings of the National Academy of Sciences of the United States of America.

[11]  M. Gefter,et al.  DNA Replication , 2019, Advances in Experimental Medicine and Biology.

[12]  P. Chambon.  9. Eucaryotic RNA Polymerases , 1974 .

[13]  B. Roizman,et al.  The Replication of Herpesviruses , 1974 .

[14]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.