1998
DOI: 10.1128/jvi.72.12.10011-10019.1998
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The LEF-4 Subunit of Baculovirus RNA Polymerase Has RNA 5′-Triphosphatase and ATPase Activities

Abstract: The baculovirus Autographa californica nuclear polyhedrosis virus encodes a DNA-dependent RNA polymerase that is required for transcription of viral late genes. This polymerase is composed of four equimolar subunits, LEF-8, LEF-4, LEF-9, and p47. The LEF-4 subunit has guanylyltransferase activity, suggesting that baculoviruses may encode a full complement of capping enzymes. Here we show that LEF-4 is a bifunctional enzyme that hydrolyzes the gamma phosphates of triphosphate-terminated RNA and also hydrolyzes … Show more

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Cited by 85 publications
(34 citation statements)
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“…After transfer of GMP to the RNA substrate, RNA methyltransferase catalyzes the transfer of a methyl group from Sadenosylmethionine to the guanosine cap. In the accompany- ing report (13), we present data showing that LEF-4 is a bifunctional protein and that RNA triphosphatase activity is localized in the N-terminal half of the protein. We have not yet identified a candidate for a virus-encoded methyltransferase.…”
Section: Discussionmentioning
confidence: 95%
“…After transfer of GMP to the RNA substrate, RNA methyltransferase catalyzes the transfer of a methyl group from Sadenosylmethionine to the guanosine cap. In the accompany- ing report (13), we present data showing that LEF-4 is a bifunctional protein and that RNA triphosphatase activity is localized in the N-terminal half of the protein. We have not yet identified a candidate for a virus-encoded methyltransferase.…”
Section: Discussionmentioning
confidence: 95%
“…The efficient translation of uncapped baculovirus p10 mRNA in vitro (Scheper et al, 1997), raises the question why late baculovirus mRNAs are capped by the baculovirus-encoded capping enzyme LEF4 (Jin et al, 1998). This might be explained, at least in part, by the fact that the cap structure might be necessary for other steps in the life cycle of baculovirus mRNAs, such as polyA addition, stabilization and nucleocytoplasmic transport.…”
Section: Discussionmentioning
confidence: 99%
“…Like most eukaryotic mRNAs, baculovirus mRNAs contain a methylated cap structure (m 7 G) at their 5 ′ end (Qin & Weaver, 1982). The late essential factor LEF4, which is a component of the baculovirus-encoded RNA polymerase, is responsible for capping baculovirus late and very late mRNAs (Jin et al , 1998). In all eukaryotes studied thus far, this methylated cap structure is recognized by the capbinding protein eIF4E, which has a size of approximately 25 kDa.…”
Section: Introductionmentioning
confidence: 99%
“…Similarly, substitution of E305 or E496 by alanine results in inactive Cet1. Moreover, these glutamates are also essential for the activities of other RNA triphosphatases, including the vaccinia virus, chlorella virus and baculovirus RNA triphosphatases (Yu et al, 1997;Jin et al, 1998;Gong and Shuman, 2002), mimivirus mRNA capping enzyme (Benarroch et al, 2008) and yeast Cth1p (CTL1; Rodriguez et al, 1999;Pei et al, 1999). Residues E305 and D471 of Cet1 coordinate a water molecule.…”
Section: Enzymatic Propertiesmentioning
confidence: 99%