ArticleJournal of virology1998
RNA 5'-triphosphatase, nucleoside triphosphatase, and guanylyltransferase activities of baculovirus LEF-4 protein.
Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 73 citations in OpenAlex.
- Vaccinia Virus Capping Enzyme Subunit D12 Is Differentially Required for Viral Replication in Different Cell Lines and Gastrointestinal Organoids.Journal of medical virology · 2026Article
- IE1 of Autographa californica Multiple Nucleopolyhedrovirus Activates Low Levels of Late Gene Expression in the Absence of Virus RNA Polymerase.Microbiology spectrum · 2023Article
- A Biochemical Perspective of the Nonstructural Proteins (NSPs) and the Spike Protein of SARS CoV-2.The protein journal · 2021Review
- Crystal structures of the RNA triphosphatase fromThe Journal of biological chemistry · 2020Article
- RNA Synthesis and Capping by Non-segmented Negative Strand RNA Viral Polymerases: Lessons From a Prototypic Virus.Frontiers in microbiology · 2019Review
- Article
- Crystal structure of vaccinia virus mRNA capping enzyme provides insights into the mechanism and evolution of the capping apparatus.Structure (London, England : 1993) · 2014Article
- Mutualistic polydnaviruses share essential replication gene functions with pathogenic ancestors.PLoS pathogens · 2013Article
- Baculovirus: molecular insights on their diversity and conservation.International journal of evolutionary biology · 2011Article
- Characterization of LEF4 ligand binding property and its role as part of baculoviral transcription machinery.Molecular and cellular biochemistry · 2010Article
- Roles of LEF-4 and PTP/BVP RNA triphosphatases in processing of baculovirus late mRNAs.Journal of virology · 2008Article
- 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
- Expression of baculovirus late and very late genes depends on LEF-4, a component of the viral RNA polymerase whose guanyltransferase function is essential.Journal of virology · 2006Article
- Autographa californica nucleopolyhedrovirus orf69 encodes an RNA cap (nucleoside-2'-O)-methyltransferase.Journal of virology · 2003Article
- Mapping the triphosphatase active site of baculovirus mRNA capping enzyme LEF4 and evidence for a two-metal mechanism.Nucleic acids research · 2003Article
- Functional characterization and structural modelling of late gene expression factor 4 from Bombyx mori nucleopolyhedrovirus.The Biochemical journal · 2002Article
- Analysis of an Autographa californica multicapsid nucleopolyhedrovirus lef-6-null virus: LEF-6 is not essential for viral replication but appears to accelerate late gene transcription.Journal of virology · 2002Article
- Virus-specific mRNA capping enzyme encoded by hepatitis E virus.Journal of virology · 2001Article
- A yeast-like mRNA capping apparatus in Plasmodium falciparum.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Autographa californica nuclear polyhedrosis virus late and very late mRNAs are transcribed by an RNA polymerase consisting of four virus-encoded polypeptides: LEF-8, LEF-9, LEF-4, and p47. The 464-amino-acid LEF-4 subunit contains the signature motifs of GTP:RNA guanylyltransferases (capping enzymes). Here, we show that the purified recombinant LEF-4 protein catalyzes two reactions involved in RNA cap formation. LEF-4 is an RNA 5'-triphosphatase that hydrolyzes the gamma phosphate of triphosphate-terminated RNA and a guanylyltransferase that reacts with GTP to form a covalent protein-guanylate adduct. The RNA triphosphatase activity depends absolutely on a divalent cation; the cofactor requirement is satisfied by either magnesium or manganese. LEF-4 also hydrolyzes ATP to ADP and Pi (Km = 43 microM ATP; Vmax = 30 s-1) and GTP to GDP and Pi. The LEF-4 nucleoside triphosphatase (NTPase) is activated by manganese or cobalt but not by magnesium. The RNA triphosphatase and NTPase activities of baculovirus LEF-4 resemble those of the vaccinia virus and Saccharomyces cerevisiae mRNA capping enzymes. We suggest that these proteins comprise a novel family of metal-dependent triphosphatases.
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