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Formation of guanosine(5')tetraphospho(5')adenosine cap structure by an unconventional mRNA capping enzyme of vesicular stomatitis virus.

Abstract
The RNA-dependent RNA polymerase L protein of vesicular stomatitis virus (VSV) elicits GTPase and RNA:GDP polyribonucleotidyltransferase (PRNTase) activities to produce a 5'-cap core structure, guanosine(5')triphospho(5')adenosine (GpppA), on viral mRNAs. Here, we report that the L protein produces an unusual cap structure, guanosine(5')tetraphospho(5')adenosine (GppppA), that is formed by the transfer of the 5'-monophosphorylated viral mRNA start sequence to GTP by the PRNTase activity before the removal of the gamma-phosphate from GTP by GTPase. Interestingly, GppppA-capped and polyadenylated full-length mRNAs were also found to be synthesized by an in vitro transcription system with the native VSV RNP.
AuthorsTomoaki Ogino, Amiya K Banerjee
JournalJournal of virology (J Virol) Vol. 82 Issue 15 Pg. 7729-34 (Aug 2008) ISSN: 1098-5514 [Electronic] United States
PMID18495767 (Publication Type: Journal Article, Research Support, N.I.H., Extramural)
Chemical References
  • Dinucleoside Phosphates
  • RNA Caps
  • RNA, Viral
  • Viral Proteins
  • guanosine 5'-triphosphate-5'-adenosine
  • Nucleotidyltransferases
  • L protein, vesicular stomatitis virus
  • RNA-Dependent RNA Polymerase
  • mRNA guanylyltransferase
Topics
  • Dinucleoside Phosphates (metabolism)
  • Nucleotidyltransferases (metabolism)
  • RNA Caps (chemistry, metabolism)
  • RNA, Viral (metabolism)
  • RNA-Dependent RNA Polymerase (metabolism)
  • Vesiculovirus (enzymology)
  • Viral Proteins (metabolism)

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