RNA- temperature-sensitive mutants of vesicular stomatitis virus: L-protein thermosensitivity accounts for transcriptase restriction of group I mutants.
In vitro transcriptase activity of three group I temperature-sensitive (ts) mutants of vesicular stomatitis virus restricted at 39 C was restored by L-protein fractions derived from wild-type (wt) vesicular stomatitis virion nucleo-capsids. Soluble NS protein from wt nucleocapsids did not reconstitute restricted transcriptions of the group I RNA-ts mutants. NS protein activity, but not L protein activity, was purified from the group I ts mutants; this NS fraction always displayed the wt phenotype in reconstitution assays. Neither the L nor the NS protein was capable of restoring the defective transcriptive activity of the group IV vesicular stomatitis virus mutant ts W16B.
D002213:Capsid / Q000378:metabolism*; D012321:DNA-Directed RNA Polymerases / Q000096:biosynthesis* / Q000378:metabolism; D009154:Mutation; D011092:Polyethylene Glycols / Q000494:pharmacology; D012367:RNA, Viral / Q000096:biosynthesis; D012995:Solubility; D013696:Temperature; D014158:Transcription, Genetic; D014721:Vesicular stomatitis Indiana virus / Q000201:enzymology* / Q000378:metabolism; D014764:Viral Proteins / Q000378:metabolism*
D012367:RNA, Viral; D014764:Viral Proteins; D011092:Polyethylene Glycols; D012321:DNA-Directed RNA Polymerases