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… 
View on ASBMB
jbc.org
101 Citations
Highly Influential Citations
2
Background Citations
45
Methods Citations
7
Results Citations
5

101 Citations

Citation Type

Citation Type

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].
TLDR
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
TLDR
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.
Evidence for N7 guanine methyl transferase activity encoded within the modular domain of RNA-dependent RNA polymerase L of a Morbillivirus
TLDR
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.
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.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 40 REFERENCES
Protein factors required for in vitro transcription of Sendai virus genome.
TLDR
The results suggest that, in addition to the general factors which are present ubiquitously in eukaryotic cells, a factor(s) specific to Sendai virus-infection is required forSendai virus transcription.
Recombinant Human mRNA Cap Methyltransferase Binds Capping Enzyme/RNA Polymerase IIo Complexes*
TLDR
Recombinant human methyltransferase transferred a methyl group fromS-adenosylmethionine to GpppG 5′ends, which are formed on RNA polymerase II transcripts by the sequential action of RNA 5′-triphosphatase and guanylyltransferase activities in the bifunctional mammalian capping enzyme.
Transcriptional activity and mutational analysis of recombinant vesicular stomatitis virus RNA polymerase
TLDR
Experimental evidence is provided that the GDN of negative-strand, nonsegmented RNA viruses is a variant of the GDD motif of plus-stranded RNA viruses and of the XDD motif in DNA viruses and reverse transcriptases.
In vitro mRNA synthesis by Sendai virus: isolation and characterization of the transcription initiation complex.
TLDR
Data suggest that cellular tubulin, one of the host factors essential for Sendai virus transcription, interacts with the viral ribonucleoprotein to form an active complex at the initiation step.
Reaction in alphavirus mRNA capping: formation of a covalent complex of nonstructural protein nsP1 with 7-methyl-GMP.
TLDR
It is suggested that in the capping of alphavirus mRNAs the guanine is methylated before linkage to the mRNA molecule.
An acidic activation-like domain of the Sendai virus P protein is required for RNA synthesis and encapsidation.
TLDR
Deletion analysis of the P gene found that residues 1-77 in the N-terminal half were in fact essential for RNA encapsidation, and either residues 1 -77 or 78-144 also provided a function that was essential forRNA synthesis per se.
Complexes of Sendai virus NP-P and P-L proteins are required for defective interfering particle genome replication in vitro
TLDR
The replication data suggest that two protein complexes, NP-P and P-L, are required for nucleocapsid RNA replication and that these complexes must form during or soon after synthesis of the proteins.
An amino-proximal domain of the L protein binds to the P protein in the measles virus RNA polymerase complex.
TLDR
Data show that the N-terminal 408 amino acids of the L protein contain the P binding domain and suggest that domain I within this region of theL proteins of (-) strand RNA viruses may be important for RNA polymerase complex formation.
Messenger RNA capping enzymes from eukaryotic cells.
  • K. Mizumoto, Y. Kaziro
  • Biology, Chemistry
    Progress in nucleic acid research and molecular biology
  • 1987
Interaction of cellular tubulin with Sendai virus M protein regulates transcription of viral genome.
...
1
2
3
4
...