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

التفاصيل البيبلوغرافية
العنوان: A putative ATPase mediates RNA transcription and capping in a dsRNA virus
المؤلفون: Xuekui Yu, Jiansen Jiang, Jingchen Sun, Z Hong Zhou
المصدر: eLife, Vol 4 (2015)
بيانات النشر: eLife Sciences Publications Ltd, 2015.
سنة النشر: 2015
المجموعة: LCC:Medicine
LCC:Science
LCC:Biology (General)
مصطلحات موضوعية: viral ATPase, histidine-mediated guanylyl transfer, allosteric regulation, conformational change, Medicine, Science, Biology (General), QH301-705.5
الوصف: 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.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2050-084X
Relation: https://elifesciences.org/articles/07901; https://doaj.org/toc/2050-084X
DOI: 10.7554/eLife.07901
URL الوصول: https://doaj.org/article/0d0f8d0b5be34f09bf296d7672dad2d5
رقم الأكسشن: edsdoj.0d0f8d0b5be34f09bf296d7672dad2d5
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:2050084X
DOI:10.7554/eLife.07901