Bacteriophage MS2 genomic RNA encodes an assembly instruction manual for its capsid.

Peter G Stockley, Simon J White, Eric Dykeman, Iain Manfield, Ottar Rolfsson, Nikesh Patel, Richard Bingham, Amy Barker, Emma Wroblewski, Rebecca Chandler-Bostock, Eva U Weiß, Neil A Ranson, Roman Tuma, Reidun Twarock
{"title":"Bacteriophage MS2 genomic RNA encodes an assembly instruction manual for its capsid.","authors":"Peter G Stockley,&nbsp;Simon J White,&nbsp;Eric Dykeman,&nbsp;Iain Manfield,&nbsp;Ottar Rolfsson,&nbsp;Nikesh Patel,&nbsp;Richard Bingham,&nbsp;Amy Barker,&nbsp;Emma Wroblewski,&nbsp;Rebecca Chandler-Bostock,&nbsp;Eva U Weiß,&nbsp;Neil A Ranson,&nbsp;Roman Tuma,&nbsp;Reidun Twarock","doi":"10.1080/21597081.2016.1157666","DOIUrl":null,"url":null,"abstract":"<p><p>Using RNA-coat protein crosslinking we have shown that the principal RNA recognition surface on the interior of infectious MS2 virions overlaps with the known peptides that bind the high affinity translational operator, TR, within the phage genome. The data also reveal the sequences of genomic fragments in contact with the coat protein shell. These show remarkable overlap with previous predictions based on the hypothesis that virion assembly is mediated by multiple sequences-specific contacts at RNA sites termed Packaging Signals (PSs). These PSs are variations on the TR stem-loop sequence and secondary structure. They act co-operatively to regulate the dominant assembly pathway and ensure cognate RNA encapsidation. In MS2, they also trigger conformational change in the dimeric capsomere creating the A/B quasi-conformer, 60 of which are needed to complete the <i>T</i>=3 capsid. This is the most compelling demonstration to date that this ssRNA virus, and by implications potentially very many of them, assemble via a PS-mediated assembly mechanism.</p>","PeriodicalId":8686,"journal":{"name":"Bacteriophage","volume":"6 1","pages":"e1157666"},"PeriodicalIF":0.0000,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/21597081.2016.1157666","citationCount":"37","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bacteriophage","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1080/21597081.2016.1157666","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 37

Abstract

Using RNA-coat protein crosslinking we have shown that the principal RNA recognition surface on the interior of infectious MS2 virions overlaps with the known peptides that bind the high affinity translational operator, TR, within the phage genome. The data also reveal the sequences of genomic fragments in contact with the coat protein shell. These show remarkable overlap with previous predictions based on the hypothesis that virion assembly is mediated by multiple sequences-specific contacts at RNA sites termed Packaging Signals (PSs). These PSs are variations on the TR stem-loop sequence and secondary structure. They act co-operatively to regulate the dominant assembly pathway and ensure cognate RNA encapsidation. In MS2, they also trigger conformational change in the dimeric capsomere creating the A/B quasi-conformer, 60 of which are needed to complete the T=3 capsid. This is the most compelling demonstration to date that this ssRNA virus, and by implications potentially very many of them, assemble via a PS-mediated assembly mechanism.

Abstract Image

Abstract Image

Abstract Image

噬菌体MS2基因组RNA编码其衣壳的组装说明书。
利用RNA-外壳蛋白交联,我们发现传染性MS2病毒粒子内部的主要RNA识别表面与噬菌体基因组中结合高亲和力翻译操作符TR的已知肽重叠。这些数据还揭示了与外壳蛋白壳接触的基因组片段的序列。这些结果与先前基于病毒粒子组装是由称为包装信号(PSs)的RNA位点上的多个序列特异性接触介导的假设的预测有显著的重叠。这些ps是TR茎环序列和二级结构的变异。它们合作调节显性组装途径并确保同源RNA的封装。在MS2中,它们还触发二聚体衣壳的构象变化,产生A/B准构象,其中60个是完成T=3衣壳所需的。这是迄今为止最令人信服的证据,表明这种ssRNA病毒,以及潜在的许多病毒,通过ps介导的组装机制进行组装。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信