Capping of tobacco mosaic virus RNA. Analysis of viral-coded guanylyltransferase-like activity

D. D. Dunigan, M. Zaitlin

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

The 5' end of tobacco mosaic virus (TMV) genomic RNA is capped with 7-methylguanosine. A virus-coded polypeptide with guanylyltransferase activity has been investigated. This enzyme is responsible for forming the 5'→5' linkage of guanosine 5'-monophosphate to the 5'-diphosphate of an acceptor RNA, thereby forming the cap. A critical step in the mechanism for cap formation in the eukaryotic nucleus is for guanylyltransferase to bind covalently to guanosine 5'-monophosphate with the hydrolysis of pyrophosphate when guanosine 5'-triphosphate is the substrate. The TMV 126-kilodalton protein, which is most probably a component of the TMV replicase, was found to have this activity. The mechanism of this reaction has been characterized biochemically.

Original languageEnglish (US)
Pages (from-to)779l7786
JournalJournal of Biological Chemistry
Volume265
Issue number14
StatePublished - Jun 1 1990

Fingerprint

Guanosine Monophosphate
Tobacco Mosaic Virus
Tobacco
Viruses
RNA
Diphosphates
Guanosine Triphosphate
Hydrolysis
Guanosine
Peptides
Enzymes
Proteins
Substrates
guanylyltransferase
7-methylguanosine
tobacco mosaic virus replicase
diphosphoric acid

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Capping of tobacco mosaic virus RNA. Analysis of viral-coded guanylyltransferase-like activity. / Dunigan, D. D.; Zaitlin, M.

In: Journal of Biological Chemistry, Vol. 265, No. 14, 01.06.1990, p. 779l7786.

Research output: Contribution to journalArticle

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