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.
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Authors | Tomoaki Ogino, Amiya K Banerjee |
Journal | Journal of virology
(J Virol)
Vol. 82
Issue 15
Pg. 7729-34
(Aug 2008)
ISSN: 1098-5514 [Electronic] United States |
PMID | 18495767
(Publication Type: Journal Article, Research Support, N.I.H., Extramural)
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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
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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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