Phosphorylation sites on phosphoprotein NS of vesicular stomatitis virus

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NS phosphoprotein of vesicular stomatitis virus: subspecies separated by electrophoresis and isoelectric focusing.

The NS protein of vesicular stomatitis virus is the only phosphorylated nucleocapsid protein. The amount of NS phosphorylation appears to regulate the activity of the protein in the transcription of the virus genome. Several methods have been used to separate NS subspecies containing different amounts of phosphate, but the relationships among the subspecies separated by different workers have b...

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Effects of phosphorylation and pH on the association of NS protein with vesicular stomatitis virus cores.

The proteins of vesicular stomatitis virus (VSV) were analyzed on the basis of charge as well as size in polyacrylamide gels containing urea and acetic acid. The phosphorprotein NS was resolved into two major species. The less phosphorylated NS1 species contained about 10% fewer phosphate residues than the second species, NS2. These two phosphorylated forms were compartmentalized both in the vi...

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Phosphorylation of vesicular stomatitis virus phosphoprotein P is indispensable for virus growth.

The phosphoprotein (P) of vesicular stomatitis virus (VSV) is an essential subunit of the viral RNA-dependent RNA polymerase (RdRp) complex. It is phosphorylated at two different domains. Using defective interfering (DI) RNA or minigenomic RNA templates, we previously demonstrated that phosphorylation within the amino-terminal domain I is essential for transcription, whereas phosphorylation wit...

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Vesicular Stomatitis Virus

Defective particles were the major product after undiluted passage of certain temperature-sensitive (ts) mutants of the Indiana C strain of vesicular stomatitis virus in BHK-21 cells at the permissive temperature (31 C). Essentially homogeneous preparations of defective particles were obtained with the wild-type and individual ts mutants. The defective particles associated with some of the ts m...

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Phosphorylation by cellular casein kinase II is essential for transcriptional activity of vesicular stomatitis virus phosphoprotein P.

We have previously shown that phosphorylation of vesicular stomatitis virus (VSV) phosphoprotein P by cellular protein kinase activity is an essential prerequisite for its transcriptional function. We have now purified this protein kinase by monitoring its ability to phosphorylate bacterially expressed, unphosphorylated P protein. Biochemical studies showed that the kinase is indistinguishable ...

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ژورنال

عنوان ژورنال: Journal of Virology

سال: 1985

ISSN: 0022-538X,1098-5514

DOI: 10.1128/jvi.54.3.697-702.1985