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PMID: 3015929 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Proofreading function associated with the RNA-dependent RNA polymerase from influenza virus.

The Journal of biological chemistry ·Vol. 261 ·No. 22 ·1986-08-05 ·Pages 10417-21

Ishihama A, Mizumoto K, Kawakami K, Kato A, Honda A

Abstract

The influenza virus-associated RNA polymerase cleaves capped RNA in an endonucleolytic manner and the transcription is initiated by the addition of GMP, the first substrate to be polymerized under the direction of viral RNA template, onto 3'-termini of resulting capped RNA fragments. In the presence of high concentrations of GTP as a sole substrate, multiple GMP residues were polymerized onto the primers. By the addition of the second substrate CTP, excess GMP residues, other than the 1st residue, were removed prior to elongation. The result may suggest that the RNA-dependent RNA polymerase carries a proofreading function.

MeSH Terms
Cytidine Monophosphate/metabolism Cytidine Triphosphate/pharmacology Guanosine Monophosphate/metabolism,pharmacology Guanosine Triphosphate/pharmacology Influenza A virus/enzymology Poly A/metabolism Poly U/metabolism RNA Caps/metabolism RNA Nucleotidyltransferases/metabolism RNA-Dependent RNA Polymerase/metabolism Transcription, Genetic/drug effects
Chemicals
RNA Caps Poly A Poly U Cytidine Triphosphate Guanosine Monophosphate Guanosine Triphosphate RNA Nucleotidyltransferases RNA-Dependent RNA Polymerase Cytidine Monophosphate
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Ishihama A
Mizumoto K
Kawakami K
Kato A
Honda A
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1986-08-05
Pages
10417-21
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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