Revisiting the substrate recognition of bacterial ribonuclease P: in the view of the recognition of the base N73 in the substrate.

Terumichi Tanaka, Tomoaki Ando, Yo Kikuchi
{"title":"Revisiting the substrate recognition of bacterial ribonuclease P: in the view of the recognition of the base N73 in the substrate.","authors":"Terumichi Tanaka,&nbsp;Tomoaki Ando,&nbsp;Yo Kikuchi","doi":"10.1093/nass/3.1.275","DOIUrl":null,"url":null,"abstract":"<p><p>The RNA subunit of bacterial ribonuclease P (RNase P) is a ribozyme which can cleave a canonical cloverleaf tRNA precursor and a hairpin RNA with a CCA-3' tag sequence as its substrate. At high concentration of Mg ion, the substrate shape preference of the ribozyme becomes broader to accept a hairpin shape RNA. In hairpin RNA cleavage reactions, we found that the base interaction between the base U294 of E. coli ribozyme and the base N73 of the substrate RNA did not obey the response according to the Watson-Crick type interaction which is usually observed in the interaction between the base U294 of ribozyme and the base N73 of tRNA precursor.</p>","PeriodicalId":86149,"journal":{"name":"Nucleic acids research. Supplement (2001)","volume":" 3","pages":"275-6"},"PeriodicalIF":0.0000,"publicationDate":"2003-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1093/nass/3.1.275","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nucleic acids research. Supplement (2001)","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1093/nass/3.1.275","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

The RNA subunit of bacterial ribonuclease P (RNase P) is a ribozyme which can cleave a canonical cloverleaf tRNA precursor and a hairpin RNA with a CCA-3' tag sequence as its substrate. At high concentration of Mg ion, the substrate shape preference of the ribozyme becomes broader to accept a hairpin shape RNA. In hairpin RNA cleavage reactions, we found that the base interaction between the base U294 of E. coli ribozyme and the base N73 of the substrate RNA did not obey the response according to the Watson-Crick type interaction which is usually observed in the interaction between the base U294 of ribozyme and the base N73 of tRNA precursor.

重新审视细菌核糖核酸酶P的底物识别:从底物中碱基N73的识别来看。
细菌核糖核酸酶P (RNase P)的RNA亚基是一种核糖酶,可以切割典型的三叶草tRNA前体和以CCA-3'标记序列为底物的发夹RNA。在高浓度Mg离子下,核酶对底物形状的偏好变得更广,可以接受发夹形状的RNA。在发夹RNA裂解反应中,我们发现大肠杆菌核酶的碱基U294与底物RNA的碱基N73之间的碱基相互作用不服从通常在核酶的碱基U294与tRNA前体的碱基N73相互作用中观察到的沃森-克里克型相互作用的响应。
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