The bacterial endoribonuclease RNase E can cleave RNA in the absence of the RNA chaperone Hfq
DC Field | Value | Language |
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dc.contributor.author | Baek, Yu Mi | - |
dc.contributor.author | Jang, Kyoung-Jin | - |
dc.contributor.author | Lee,Hyobeen | - |
dc.contributor.author | Yoon, Soojin | - |
dc.contributor.author | Baek, Ahruem | - |
dc.contributor.author | Lee, Kangseok | - |
dc.contributor.author | Kim, Dong-Eun | - |
dc.date.available | 2019-12-06T03:40:21Z | - |
dc.date.issued | 2019-11 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.issn | 1083-351X | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/37103 | - |
dc.description.abstract | RNase E is a component of the RNA degradosome complex and plays a key role in RNA degradation and maturation in Escherichia coli. RNase E-mediated target RNA degradation typically involves the RNA chaperone Hfq and requires small guide RNAs (sRNAs) acting as a seed by binding to short (7-12-bp) complementary regions in target RNA sequences. Here, using recombinantly expressed and purified proteins, site-directed mutagenesis, and RNA cleavage and protein cross-linking assays, we investigated Hfq-independent RNA decay by RNase E. Exploring its RNA substrate preferences in the absence of Hfq, we observed that RNase E preferentially cleaves AU-rich sites of single-stranded regions of RNA substrates that are annealed to an sRNA that contains a monophosphate at its 5-end. We further found that the quaternary structure of RNase E is also important for complete, Hfq-independent cleavage at sites both proximal and distal to the sRNA-binding site within target RNAs containing monophosphorylated 5-ends. Of note, genetic RNase E variants with unstable quaternary structure exhibited decreased catalytic activity. In summary, our results show that RNase E can degrade its target RNAs in the absence of the RNA chaperone Hfq. We conclude that RNase E-mediated, Hfq-independent RNA decay in E. coli requires a cognate sRNA sequence for annealing to the target RNA, a 5-monophosphate at the RNA 5-end, and a stable RNase E quaternary structure. © 2019 American Society for Biochemistry and Molecular Biology Inc.. All rights reserved. | - |
dc.format.extent | 14 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | American Society for Biochemistry and Molecular Biology Inc. | - |
dc.title | The bacterial endoribonuclease RNase E can cleave RNA in the absence of the RNA chaperone Hfq | - |
dc.type | Article | - |
dc.identifier.doi | 10.1074/jbc.RA119.010105 | - |
dc.identifier.bibliographicCitation | Journal of Biological Chemistry, v.294, no.44, pp 16465 - 16478 | - |
dc.description.isOpenAccess | Y | - |
dc.identifier.wosid | 000499478600047 | - |
dc.identifier.scopusid | 2-s2.0-85074446848 | - |
dc.citation.endPage | 16478 | - |
dc.citation.number | 44 | - |
dc.citation.startPage | 16465 | - |
dc.citation.title | Journal of Biological Chemistry | - |
dc.citation.volume | 294 | - |
dc.type.docType | Article | - |
dc.publisher.location | 미국 | - |
dc.subject.keywordAuthor | ribonuclease | - |
dc.subject.keywordAuthor | endoribonuclease | - |
dc.subject.keywordAuthor | RNA degradation | - |
dc.subject.keywordAuthor | mRNA decay | - |
dc.subject.keywordAuthor | RNA processing | - |
dc.subject.keywordAuthor | RNA turnover | - |
dc.subject.keywordAuthor | small guide RNA (sRNA) | - |
dc.subject.keywordAuthor | RNase E | - |
dc.subject.keywordAuthor | RNA chaperone Hfq | - |
dc.subject.keywordAuthor | protein expression | - |
dc.subject.keywordPlus | Binding sites | - |
dc.subject.keywordPlus | Catalyst activity | - |
dc.subject.keywordPlus | Escherichia coli | - |
dc.subject.keywordPlus | Proteins | - |
dc.subject.keywordPlus | Substrates | - |
dc.subject.keywordPlus | Endoribonuclease | - |
dc.subject.keywordPlus | Monophosphates | - |
dc.subject.keywordPlus | Protein crosslinking | - |
dc.subject.keywordPlus | Purified protein | - |
dc.subject.keywordPlus | Quaternary structure | - |
dc.subject.keywordPlus | RNA substrate | - |
dc.subject.keywordPlus | Single-stranded region | - |
dc.subject.keywordPlus | Site directed mutagenesis | - |
dc.subject.keywordPlus | RNA | - |
dc.subject.keywordPlus | bacterial RNA | - |
dc.subject.keywordPlus | chaperone | - |
dc.subject.keywordPlus | chaperone Hfq | - |
dc.subject.keywordPlus | recombinant protein | - |
dc.subject.keywordPlus | ribonuclease E | - |
dc.subject.keywordPlus | single stranded RNA | - |
dc.subject.keywordPlus | unclassified drug | - |
dc.subject.keywordPlus | Article | - |
dc.subject.keywordPlus | binding site | - |
dc.subject.keywordPlus | catalysis | - |
dc.subject.keywordPlus | controlled study | - |
dc.subject.keywordPlus | enzyme activity | - |
dc.subject.keywordPlus | Escherichia coli | - |
dc.subject.keywordPlus | gene targeting | - |
dc.subject.keywordPlus | genetic variability | - |
dc.subject.keywordPlus | nonhuman | - |
dc.subject.keywordPlus | phosphorylation | - |
dc.subject.keywordPlus | priority journal | - |
dc.subject.keywordPlus | protein cleavage | - |
dc.subject.keywordPlus | protein cross linking | - |
dc.subject.keywordPlus | protein quaternary structure | - |
dc.subject.keywordPlus | RNA cleavage | - |
dc.subject.keywordPlus | simulated annealing | - |
dc.subject.keywordPlus | site directed mutagenesis | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.description.journalRegisteredClass | sci | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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