ArticleJournal of virology2001
RNA triphosphatase component of the mRNA capping apparatus of Paramecium bursaria Chlorella virus 1.
Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 30 citations in OpenAlex.
- Structural basis of the monkeypox virus mRNA cap N7 methyltransferase complex.Emerging microbes & infections · 2024Article
- Functional Genomic Analyses Reveal an Open Pan-genome for the Chloroviruses and a Potential for Genetic Innovation in New Isolates.Journal of virology · 2022Article
- Crystal structures of the RNA triphosphatase fromThe Journal of biological chemistry · 2020Article
- Chloroviruses.Viruses · 2019Review
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- Article
- Development and validation of a high-density fluorescence polarization-based assay for the trypanosoma RNA triphosphatase TbCet1.Combinatorial chemistry & high throughput screening · 2009Article
- Magnesium-binding studies reveal fundamental differences between closely related RNA triphosphatases.Nucleic acids research · 2008Article
- Inhibition of a metal-dependent viral RNA triphosphatase by decavanadate.The Biochemical journal · 2006Article
- Chlorella viruses.Advances in virus research · 2006Review
- Divergent subunit interactions among fungal mRNA 5'-capping machineries.Eukaryotic cell · 2002Article
- A yeast-like mRNA capping apparatus in Plasmodium falciparum.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- RNA triphosphatase is essential in Schizosaccharomyces pombe and Candida albicans.BMC microbiology · 2001Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Paramecium bursaria chlorella virus 1 (PBCV-1) elicits a lytic infection of its unicellular green alga host. The 330-kbp viral genome has been sequenced, yet little is known about how viral mRNAs are synthesized and processed. PBCV-1 encodes its own mRNA guanylyltransferase, which catalyzes the addition of GMP to the 5' diphosphate end of RNA to form a GpppN cap structure. Here we report that PBCV-1 encodes a separate RNA triphosphatase (RTP) that catalyzes the initial step in cap synthesis: hydrolysis of the gamma-phosphate of triphosphate-terminated RNA to generate an RNA diphosphate end. We exploit a yeast-based genetic system to show that Chlorella virus RTP can function as a cap-forming enzyme in vivo. The 193-amino-acid Chlorella virus RTP is the smallest member of a family of metal-dependent phosphohydrolases that includes the RNA triphosphatases of fungi and other large eukaryotic DNA viruses (poxviruses, African swine fever virus, and baculoviruses). Chlorella virus RTP is more similar in structure to the yeast RNA triphosphatases than to the enzymes of metazoan DNA viruses. Indeed, PBCV-1 is unique among DNA viruses in that the triphosphatase and guanylyltransferase steps of cap formation are catalyzed by separate viral enzymes instead of a single viral polypeptide with multiple catalytic domains.
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