ArticleJournal of virology2003
Yeast-based genetic system for functional analysis of poxvirus mRNA cap methyltransferase.
Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Synthetic Platforms for Characterizing and Targeting of SARS-CoV-2 Genome Capping Enzymes.ACS synthetic biology · 2022Article
- Structure and Biochemical Characteristic of the Methyltransferase (MTase) Domain of RNA Capping Enzyme from African Swine Fever Virus.Journal of virology · 2021Article
- Molecular mechanisms of coronavirus RNA capping and methylation.Virologica Sinica · 2016Review
- Yeast-based assays for the high-throughput screening of inhibitors of coronavirus RNA cap guanine-N7-methyltransferase.Antiviral research · 2014Article
- Crystal structure of vaccinia virus mRNA capping enzyme provides insights into the mechanism and evolution of the capping apparatus.Structure (London, England : 1993) · 2014Article
- Structure-function analysis of severe acute respiratory syndrome coronavirus RNA cap guanine-N7-methyltransferase.Journal of virology · 2013Article
- Characterization of a mimivirus RNA cap guanine-N2 methyltransferase.RNA (New York, N.Y.) · 2009Article
- Functional screen reveals SARS coronavirus nonstructural protein nsp14 as a novel cap N7 methyltransferase.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Identification of sendai virus L protein amino acid residues affecting viral mRNA cap methylation.Journal of virology · 2009Article
- Mutational analysis of vaccinia virus mRNA cap (guanine-N7) methyltransferase reveals essential contributions of the N-terminal peptide that closes over the active site.RNA (New York, N.Y.) · 2008Article
- Phenotypic analysis of a temperature sensitive mutant in the large subunit of the vaccinia virus mRNA capping enzyme.Virology · 2008Article
- Structure-function analysis of vaccinia virus mRNA cap (guanine-N7) methyltransferase.RNA (New York, N.Y.) · 2008Article
- Structural insights into the mechanism and evolution of the vaccinia virus mRNA cap N7 methyl-transferase.The EMBO journal · 2007Article
- Characterization of a Trypanosoma brucei RNA cap (guanine N-7) methyltransferase.RNA (New York, N.Y.) · 2006Article
- A single amino acid change in the L-polymerase protein of vesicular stomatitis virus completely abolishes viral mRNA cap methylation.Journal of virology · 2005Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Structural differences between poxvirus and human mRNA capping enzymes recommend cap formation as a target for antipoxviral drug discovery. Genetic and pharmacologic analysis of the poxvirus capping enzymes requires in vivo assays in which the readout depends on the capacity of the viral enzyme to catalyze cap synthesis. Here we have used the budding yeast Saccharomyces cerevisiae as a genetic model for the study of poxvirus cap guanine-N7 methyltransferase. The S. cerevisiae capping system consists of separate triphosphatase (Cet1), guanylyltransferase (Ceg1), and methyltransferase (Abd1) components. All three activities are essential for cell growth. We report that the methyltransferase domain of vaccinia virus capping enzyme (composed of catalytic vD1-C and stimulatory vD12 subunits) can function in lieu of yeast Abd1. Coexpression of both vaccinia virus subunits is required for complementation of the growth of abd1Delta cells. Previously described mutations of vD1-C and vD12 that eliminate or reduce methyltransferase activity in vitro either abolish abd1Delta complementation or elicit conditional growth defects. We have used the yeast complementation assay as the primary screen in a new round of alanine scanning of the catalytic subunit. We thereby identified several new amino acids that are critical for cap methylation activity in vivo. Studies of recombinant proteins show that the lethal vD1-C mutations do not preclude heterodimerization with vD12 but either eliminate or reduce cap methyltransferase activity in vitro.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.