Temperature-sensitive mutations in the vaccinia virus H4 gene encoding a component of the virion RNA polymerase

Eileen M. Kane, Stewart Shuman

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

Four previously isolated temperature-sensitive (ts) mutants of vaccinia virus WR (ts1, ts31, ts55, and ts58) comprising a single complementation group (R. C. Condit, A. Motyczka, and G. Spizz, Virology 128:429-443, 1983) have been mapped by marker rescue to the H4L open reading frame located within the genomic HindIII-H DNA fragment. The H4 gene is predicted to encode a 93.6-kDa polypeptide expressed at late times during infection. Nucleotide sequence alterntions responsible for thermolabile growth lead to amino acid substitutions in the H4 gene product. All four ts alleles display "normal" patterns of early and late viral protein synthesis at the nonpermissive temperature (40°C). Mature virion particles, microscopically indistinguishable from wild-type virions, are produced in the cytoplasm of cell infected with ts1 at 40°C. Western immunoblot analysis localizes the H4 protein to the virion core. After solubilization from cores, the H4 protein is associated during purification with trascriptioally active vaccinia virus DNA-depedent RNA polymerase.

Original languageEnglish (US)
Pages (from-to)5752-5762
Number of pages11
JournalJournal of Virology
Volume66
Issue number10
StatePublished - Oct 1992

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Vaccinia virus
DNA-Directed RNA Polymerases
DNA-directed RNA polymerase
virion
Virion
mutation
Mutation
Temperature
Genes
virology
temperature
Virology
genes
viral proteins
amino acid substitution
Viral Proteins
DNA
Amino Acid Substitution
solubilization
Open Reading Frames

All Science Journal Classification (ASJC) codes

  • Immunology

Cite this

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Temperature-sensitive mutations in the vaccinia virus H4 gene encoding a component of the virion RNA polymerase. / Kane, Eileen M.; Shuman, Stewart.

In: Journal of Virology, Vol. 66, No. 10, 10.1992, p. 5752-5762.

Research output: Contribution to journalArticle

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