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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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 |
work_keys_str_mv |
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