Characterization of the phosphorylated small enzyme subunit, NS, of the vesicular stomatitis virus RNA polymerase.

NS protein of vesicular stomatitis virus was shown to migrate with a mobility consistent with the molecular weight predicted from the published cDNA sequence on polyacrylamide gels containing the detergent cetyltrimethylammonium bromide at low pH. Cyanogen bromide cleavage of NS protein produced a large acidic amino-terminal peptide, as predicted by the sequence, which contained the majority of the phosphate residues. However, analysis of tryptic peptides by high-performance liquid chromatography suggested that there may be inaccuracies in the sequence of the carboxyl terminus of the sequence.