A putative ATPase mediates RNA transcription and capping in a dsRNA virus

mRNA transcription in dsRNA viruses is a highly regulated process but the mechanism of this regulation is not known. Here, by nucleoside triphosphatase (NTPase) assay and comparisons of six high-resolution (2.9–3.1 Å) cryo-electron microscopy structures of cytoplasmic polyhedrosis virus with bound l...

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Main Authors: Xuekui Yu, Jiansen Jiang, Jingchen Sun, Z Hong Zhou
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2015-08-01
Series:eLife
Subjects:
Online Access:https://elifesciences.org/articles/07901
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spelling doaj-0d0f8d0b5be34f09bf296d7672dad2d52021-05-04T23:56:55ZengeLife Sciences Publications LtdeLife2050-084X2015-08-01410.7554/eLife.07901A putative ATPase mediates RNA transcription and capping in a dsRNA virusXuekui Yu0Jiansen Jiang1Jingchen Sun2Z Hong Zhou3Department of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, Los Angeles, United States; California Nanosystems Institute, University of California, Los Angeles, Los Angeles, United StatesDepartment of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, Los Angeles, United States; California Nanosystems Institute, University of California, Los Angeles, Los Angeles, United StatesDepartment of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, Los Angeles, United States; Subtropical Sericulture and Mulberry Resources Protection and Safety Engineering Research Center, Guangdong Provincial Key Laboratory of Agro-animal Genomics and Molecular Breeding, College of Animal Science, South China Agricultural University, Guangzhou, ChinaDepartment of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, Los Angeles, United States; California Nanosystems Institute, University of California, Los Angeles, Los Angeles, United StatesmRNA transcription in dsRNA viruses is a highly regulated process but the mechanism of this regulation is not known. Here, by nucleoside triphosphatase (NTPase) assay and comparisons of six high-resolution (2.9–3.1 Å) cryo-electron microscopy structures of cytoplasmic polyhedrosis virus with bound ligands, we show that the large sub-domain of the guanylyltransferase (GTase) domain of the turret protein (TP) also has an ATP-binding site and is likely an ATPase. S-adenosyl-L-methionine (SAM) acts as a signal and binds the methylase-2 domain of TP to induce conformational change of the viral capsid, which in turn activates the putative ATPase. ATP binding/hydrolysis leads to an enlarged capsid for efficient mRNA synthesis, an open GTase domain for His217-mediated guanylyl transfer, and an open methylase-1 domain for SAM binding and methyl transfer. Taken together, our data support a role of the putative ATPase in mediating the activation of mRNA transcription and capping within the confines of the virus.https://elifesciences.org/articles/07901viral ATPasehistidine-mediated guanylyl transferallosteric regulationconformational change
collection DOAJ
language English
format Article
sources DOAJ
author Xuekui Yu
Jiansen Jiang
Jingchen Sun
Z Hong Zhou
spellingShingle Xuekui Yu
Jiansen Jiang
Jingchen Sun
Z Hong Zhou
A putative ATPase mediates RNA transcription and capping in a dsRNA virus
eLife
viral ATPase
histidine-mediated guanylyl transfer
allosteric regulation
conformational change
author_facet Xuekui Yu
Jiansen Jiang
Jingchen Sun
Z Hong Zhou
author_sort Xuekui Yu
title A putative ATPase mediates RNA transcription and capping in a dsRNA virus
title_short A putative ATPase mediates RNA transcription and capping in a dsRNA virus
title_full A putative ATPase mediates RNA transcription and capping in a dsRNA virus
title_fullStr A putative ATPase mediates RNA transcription and capping in a dsRNA virus
title_full_unstemmed A putative ATPase mediates RNA transcription and capping in a dsRNA virus
title_sort putative atpase mediates rna transcription and capping in a dsrna virus
publisher eLife Sciences Publications Ltd
series eLife
issn 2050-084X
publishDate 2015-08-01
description mRNA transcription in dsRNA viruses is a highly regulated process but the mechanism of this regulation is not known. Here, by nucleoside triphosphatase (NTPase) assay and comparisons of six high-resolution (2.9–3.1 Å) cryo-electron microscopy structures of cytoplasmic polyhedrosis virus with bound ligands, we show that the large sub-domain of the guanylyltransferase (GTase) domain of the turret protein (TP) also has an ATP-binding site and is likely an ATPase. S-adenosyl-L-methionine (SAM) acts as a signal and binds the methylase-2 domain of TP to induce conformational change of the viral capsid, which in turn activates the putative ATPase. ATP binding/hydrolysis leads to an enlarged capsid for efficient mRNA synthesis, an open GTase domain for His217-mediated guanylyl transfer, and an open methylase-1 domain for SAM binding and methyl transfer. Taken together, our data support a role of the putative ATPase in mediating the activation of mRNA transcription and capping within the confines of the virus.
topic viral ATPase
histidine-mediated guanylyl transfer
allosteric regulation
conformational change
url https://elifesciences.org/articles/07901
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