RNA- temperature-sensitive mutants of vesicular stomatitis virus: L-protein thermosensitivity accounts for transcriptase restriction of group I mutants

J Virol. 1976 May;18(2):596-603. doi: 10.1128/JVI.18.2.596-603.1976.


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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Capsid / metabolism*
  • DNA-Directed RNA Polymerases / biosynthesis*
  • DNA-Directed RNA Polymerases / metabolism
  • Mutation*
  • Polyethylene Glycols / pharmacology
  • RNA, Viral / biosynthesis
  • Solubility
  • Temperature
  • Transcription, Genetic
  • Vesicular stomatitis Indiana virus / enzymology*
  • Vesicular stomatitis Indiana virus / metabolism
  • Viral Proteins / metabolism*


  • RNA, Viral
  • Viral Proteins
  • Polyethylene Glycols
  • DNA-Directed RNA Polymerases