Sequential phosphorylation of the phosphoprotein of vesicular stomatitis virus by cellular and viral protein kinases is essential for transcription activation.

Abstract

The phosphoprotein (P) and the large protein (L) constitute the RNA-dependent RNA polymerase of vesicular stomatitis virus (VSV). We show that phosphate-free P protein expressed in bacteria is transcriptionally inactive when reconstituted with L protein and viral N-RNA template free of cellular protein kinase. Phosphorylation of P protein by a cellular kinase(s) was essential for transcription as well as for further phosphorylation by an L-associated kinase, the two kinases acting in a sequential (cascade) manner. Phosphate groups introduced by cell kinase were stable, whereas those due to L kinase underwent a turnover which was coupled to ongoing transcription. We present a model for the phosphorylation pathway of P protein and propose that continued phosphorylation and dephosphorylation of P protein may represent a transcriptional regulatory (on-off) switch of nonsegmented negative-strand RNA viruses.

• Authors: S Barik, A K Banerjee
• Journal: Journal of virology (J Virol) Vol. 66 Issue 2 Pg. 1109-18 (Feb 1992) ISSN: 0022-538X [Print] United States
• PMID: 1309893 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Phosphoproteins
• Recombinant Proteins
• Protein Kinases
• RNA-Dependent RNA Polymerase

Topics

• Animals
• Cell Line
• Cloning, Molecular
• Escherichia coli (genetics)
• Kinetics
• Models, Biological
• Phosphoproteins (genetics, isolation & purification, metabolism)
• Phosphorylation
• Protein Kinases (metabolism)
• RNA-Dependent RNA Polymerase (genetics, isolation & purification, metabolism)
• Recombinant Proteins (isolation & purification, metabolism)
• Transcription, Genetic
• Transcriptional Activation
• Vesicular stomatitis Indiana virus (enzymology, genetics, metabolism)