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Expression and characterization of an RNA capping enzyme encoded by Chlorella virus PBCV-1

We report that the A103R protein of Chlorella virus PBCV-1 is an mRNA capping enzyme that catalyzes the transfer of GMP from GTP to the 5' diphosphate end of RNA. This is a two-step reaction in which the enzyme first condenses with GTP to form a covalent enzyme-GMP intermediate and then transfe...

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Published in:	Journal of Virology 1996-10, Vol.70 (10), p.6658-6664
Main Authors:	Ho, C.K. (University of Nebraska, Lincoln, NE.), Van Etten, J.L, Shuman, S
Format:	Article
Language:	English
Subjects:	ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE ARN CHLORELLA Chlorella - virology Chlorella virus Escherichia coli - genetics NUCLEOTIDE NUCLEOTIDOS Nucleotidyltransferases - genetics Plant Viruses - enzymology PURIFICACION PURIFICATION Recombinant Proteins - biosynthesis Recombinant Proteins - genetics Recombinant Proteins - metabolism RNA, Viral - metabolism Sequence Analysis TRANSFERASAS TRANSFERASE Viral Proteins - biosynthesis Viral Proteins - genetics Viral Proteins - metabolism VIRUS DE LAS PLANTAS VIRUS DES VEGETAUX
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container_issue	10
container_start_page	6658
container_title	Journal of Virology
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creator	Ho, C.K. (University of Nebraska, Lincoln, NE.) Van Etten, J.L Shuman, S
description	We report that the A103R protein of Chlorella virus PBCV-1 is an mRNA capping enzyme that catalyzes the transfer of GMP from GTP to the 5' diphosphate end of RNA. This is a two-step reaction in which the enzyme first condenses with GTP to form a covalent enzyme-GMP intermediate and then transfers the GMP to an RNA acceptor to form a GpppN cap. Purified recombinant A103R is a 38-kDa monomer that lacks RNA (guanine-7-) methyltransferase activity. With respect to its size, amino acid sequence, and biochemical properties, A103R is more closely related to the yeast RNA guanylyltransferases than it is to the multifunctional capping enzymes coded for by other large DNA viruses--the poxviruses and African swine fever virus. We surmise that in order to cap its transcripts, PBCV-1 must either encode additional 5' processing activities or else rely on the host alga to provide these functions
doi_str_mv	10.1128/jvi.70.10.6658-6664.1996
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(University of Nebraska, Lincoln, NE.)</creatorcontrib><creatorcontrib>Van Etten, J.L</creatorcontrib><creatorcontrib>Shuman, S</creatorcontrib><title>Expression and characterization of an RNA capping enzyme encoded by Chlorella virus PBCV-1</title><title>Journal of Virology</title><addtitle>J Virol</addtitle><description>We report that the A103R protein of Chlorella virus PBCV-1 is an mRNA capping enzyme that catalyzes the transfer of GMP from GTP to the 5' diphosphate end of RNA. This is a two-step reaction in which the enzyme first condenses with GTP to form a covalent enzyme-GMP intermediate and then transfers the GMP to an RNA acceptor to form a GpppN cap. Purified recombinant A103R is a 38-kDa monomer that lacks RNA (guanine-7-) methyltransferase activity. 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(University of Nebraska, Lincoln, NE.) ; Van Etten, J.L ; Shuman, S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c612t-f59eeb548285bd443b8087274719a4da1bedda784b49ba54ab73af902df12ff83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>ARN</topic><topic>CHLORELLA</topic><topic>Chlorella - virology</topic><topic>Chlorella virus</topic><topic>Escherichia coli - genetics</topic><topic>NUCLEOTIDE</topic><topic>NUCLEOTIDOS</topic><topic>Nucleotidyltransferases - genetics</topic><topic>Plant Viruses - enzymology</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>RNA, Viral - metabolism</topic><topic>Sequence Analysis</topic><topic>TRANSFERASAS</topic><topic>TRANSFERASE</topic><topic>Viral Proteins - biosynthesis</topic><topic>Viral Proteins - genetics</topic><topic>Viral Proteins - metabolism</topic><topic>VIRUS DE LAS PLANTAS</topic><topic>VIRUS DES VEGETAUX</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ho, C.K. 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With respect to its size, amino acid sequence, and biochemical properties, A103R is more closely related to the yeast RNA guanylyltransferases than it is to the multifunctional capping enzymes coded for by other large DNA viruses--the poxviruses and African swine fever virus. We surmise that in order to cap its transcripts, PBCV-1 must either encode additional 5' processing activities or else rely on the host alga to provide these functions</abstract><cop>United States</cop><pub>American Society for Microbiology</pub><pmid>8794301</pmid><doi>10.1128/jvi.70.10.6658-6664.1996</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record>
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subjects	ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE ARN CHLORELLA Chlorella - virology Chlorella virus Escherichia coli - genetics NUCLEOTIDE NUCLEOTIDOS Nucleotidyltransferases - genetics Plant Viruses - enzymology PURIFICACION PURIFICATION Recombinant Proteins - biosynthesis Recombinant Proteins - genetics Recombinant Proteins - metabolism RNA, Viral - metabolism Sequence Analysis TRANSFERASAS TRANSFERASE Viral Proteins - biosynthesis Viral Proteins - genetics Viral Proteins - metabolism VIRUS DE LAS PLANTAS VIRUS DES VEGETAUX
title	Expression and characterization of an RNA capping enzyme encoded by Chlorella virus PBCV-1
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