Phosphorylation within a specific domain of the phosphoprotein of vesicular stomatitis virus regulates transcription in vitro.
We have investigated the functional significance of phosphoserine residues that lie in the L protein-binding domain between amino acids 213 and 247 of the phosphoprotein (NS) of vesicular stomatitis virus. A series of mutant NS proteins were made by cell-free translation of mRNAs transcribed from the cloned gene. Site-directed substitution of alanine for both serine 236 and serine 242 essentially abolished RNA synthesis catalyzed by the NS-L complex. Substitution of either of these serines reduced RNA synthesis by 75%. Serine 218 played no major role in RNA synthesis. Phosphorylation of NS by the L protein was abrogated by substitution of either serine 236 or serine 242. These results indicate that phosphorylation of serines 236 and 242 in the NS protein regulates its binding with the L protein and the N-RNA template and is essential for activation of viral RNA synthesis.
D000595:Amino Acid Sequence; D001483:Base Sequence; D005796:Genes; D005814:Genes, Viral; D009154:Mutation; D010750:Phosphoproteins / Q000502:physiology*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D014158:Transcription, Genetic; D014721:Vesicular stomatitis Indiana virus / Q000235:genetics*; D017361:Viral Nonstructural Proteins; D014764:Viral Proteins / Q000235:genetics* / Q000378:metabolism
D010750:Phosphoproteins; D017361:Viral Nonstructural Proteins; D014764:Viral Proteins; D011494:Protein Kinases