Sendai Virus RNA-dependent RNA Polymerase L Protein Catalyzes Cap Methylation of Virus-specific mRNA*

@article{Ogino2005SendaiVR,
  title={Sendai Virus RNA-dependent RNA Polymerase L Protein Catalyzes Cap Methylation of Virus-specific mRNA*},
  author={Tomoaki Ogino and Masaki Kobayashi and Minako Iwama and Kiyohisa Mizumoto},
  journal={Journal of Biological Chemistry},
  year={2005},
  volume={280},
  pages={4429 - 4435}
}
The Sendai virus (SeV) RNA-dependent RNA polymerase complex, which consists of L and P proteins, participates in the synthesis of viral mRNAs that possess a methylated cap structure. To identify the SeV protein(s) involved in mRNA cap methylation, we developed an in vitro assay system to detect mRNA (guanine-7-)methyltransferase (G-7-MTase) activity. Viral ribonucleoprotein complexes and purified recombinant L protein but not P protein exhibited G-7-MTase activity. On the other hand, mRNA… 
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RNA triphosphatase and guanylyl transferase activities are associated with the RNA polymerase protein L of rinderpest virus.
TLDR
The biochemical characterization of the newly found RTPase/GT activity of L protein is described, demonstrating that the viral mRNAs synthesized in vitro by the recombinant L or purified RNP are capped and methylated at the N7 guanine position.
[The multifunctional RNA polymerase L protein of non-segmented negative strand RNA viruses catalyzes unique mRNA capping].
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Using vesicular stomatitis virus (VSV) as a prototypic model virus, it is shown that the L protein catalyzes the unconventional mRNA capping reaction, which is strikingly different from the eukaryotic reaction.
Histidine-mediated RNA transfer to GDP for unique mRNA capping by vesicular stomatitis virus RNA polymerase
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These findings suggest that an ancient NNS RNA viral polymerase has acquired the PRNTase domain independently of the eukaryotic mRNA capping enzyme during evolution andPRNTase becomes a rational target for designing antiviral agents.
Unconventional mechanism of mRNA capping by the RNA-dependent RNA polymerase of vesicular stomatitis virus.
TLDR
It is reported that the RNA-dependent RNA polymerase L protein of VSV catalyzes the capping reaction by an RNA:GDP polyribonucleotidyltransferase activity, in which a 5'-monophosphorylated viral mRNA-start sequence is transferred to GDP generated from GTP via a covalent enzyme-RNA intermediate.
Evidence for N7 guanine methyl transferase activity encoded within the modular domain of RNA-dependent RNA polymerase L of a Morbillivirus
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This work demonstrates the in vitro methylation of capped mRNA and shows that a recombinant C-terminal fragment of L protein is capable of methylating capped mRNA, suggesting that the various post-transcriptional activities of the L protein are located in independently folding domains.
Phosphoprotein, P of human parainfluenza virus type 3 prevents self-association of RNA-dependent RNA polymerase, L.
TLDR
It is demonstrated that a series of N-terminally deleted L proteins as well as several truncated proteins that span different regions of the L protein can also efficiently co-immunoprecipitate the full length L protein.
Genetic Interactions among the West Nile Virus Methyltransferase, the RNA-Dependent RNA Polymerase, and the 5′ Stem-Loop of Genomic RNA
TLDR
Biochemical analysis showed that a low level of N7 methylation of the D146S methyltransferase is essential for the recovery of adaptive viruses, and genetic interactions among flaviviral methyl transferase, RdRp, and the 5′ stem-loop of the genomic RNA are established.
Molecular architecture of the vesicular stomatitis virus RNA polymerase
TLDR
The structural map of L provides new insights into the interrelationship of its various domains, and their rearrangement on P binding that is likely important for RNA synthesis.
Recognition of Cap Structure by Influenza B Virus RNA Polymerase Is Less Dependent on the Methyl Residue than Recognition by Influenza A Virus Polymerase
TLDR
It is proposed that the cap recognition pocket of FluB PB2 does not have the specificity for m7G-cap structures and thus is more flexible to accept various cap structures than FluA PB2.
In vitro capping and transcription of rhabdoviruses.
TLDR
The methods for in vitro transcription and capping with the recombinant VSV L protein permit detailed characterization of its enzymatic reactions and mapping of active sites of its enzyme domains, which are expected to be adaptable to rhabdoviruses and, by extension, other NNS RNA viruses belonging to different families.
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