Characterization of a 7-kilodalton subunit of vaccinia virus DNA-dependent RNA polymerase with structural similarities to the smallest subunit of eukaryotic RNA polymerase II

B. Y. Amegadzie, Byung-Yoon Ahn, B. Moss

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

A previously unrecognized 7-kDa polypeptide copurified with the DNA- dependent RNA polymerase of vaccinia virus virions. Internal amino acid sequences of the small protein matched a viral genomic open reading frame of 63 codons. Antipeptide antiserum was used to confirm the specific and complete association of the 7-kDa protein with RNA polymerase. The amino acid sequence predicted from the viral gene, named rpo7, was 23% identical to that of the smallest subunit of Saccharomyces cerevisiae RNA polymerase II, and a metal-binding motif, Cys-X-X-Cys-Gly, was located at precisely the same location near the N terminus in the two proteins. RNA analyses demonstrated early transcriptional initiation and termination signals in the rpo7 gene sequence. The viral RNA polymerase subunit was synthesized during the early phase of infection and continued to accumulate during the late phase.

Original languageEnglish
Pages (from-to)3003-3010
Number of pages8
JournalJournal of Virology
Volume66
Issue number5
Publication statusPublished - 1992 Jan 1
Externally publishedYes

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RNA Polymerase II
Vaccinia virus
DNA-Directed RNA Polymerases
cysteinylglycine
Amino Acid Sequence
Proteins
Viral Genes
Viral RNA
Codon
Virion
Open Reading Frames
Saccharomyces cerevisiae
Immune Sera
Metals
RNA
Peptides
Infection
Genes

ASJC Scopus subject areas

  • Immunology

Cite this

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abstract = "A previously unrecognized 7-kDa polypeptide copurified with the DNA- dependent RNA polymerase of vaccinia virus virions. Internal amino acid sequences of the small protein matched a viral genomic open reading frame of 63 codons. Antipeptide antiserum was used to confirm the specific and complete association of the 7-kDa protein with RNA polymerase. The amino acid sequence predicted from the viral gene, named rpo7, was 23{\%} identical to that of the smallest subunit of Saccharomyces cerevisiae RNA polymerase II, and a metal-binding motif, Cys-X-X-Cys-Gly, was located at precisely the same location near the N terminus in the two proteins. RNA analyses demonstrated early transcriptional initiation and termination signals in the rpo7 gene sequence. The viral RNA polymerase subunit was synthesized during the early phase of infection and continued to accumulate during the late phase.",
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