Relaxed Cleavage Specificity of Hyperactive Variants of Escherichia coli RNase E on RNA I
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Bae, Dayeong | - |
dc.contributor.author | Hyeon, Hana | - |
dc.contributor.author | Shin, Eunkyoung | - |
dc.contributor.author | Yeom, Ji-Hyun | - |
dc.contributor.author | Lee, Kangseok | - |
dc.date.accessioned | 2023-04-10T01:41:20Z | - |
dc.date.available | 2023-04-10T01:41:20Z | - |
dc.date.issued | 2023-02 | - |
dc.identifier.issn | 1225-8873 | - |
dc.identifier.issn | 1976-3794 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/66372 | - |
dc.description.abstract | RNase E is an essential enzyme in Escherichia coli. The cleavage site of this single-stranded specific endoribonuclease is well-characterized in many RNA substrates. Here, we report that the upregulation of RNase E cleavage activity by a mutation that affects either RNA binding (Q36R) or enzyme multimerization (E429G) was accompanied by relaxed cleavage specificity. Both mutations led to enhanced RNase E cleavage in RNA I, an antisense RNA of ColE1-type plasmid replication, at a major site and other cryptic sites. Expression of a truncated RNA I with a major RNase E cleavage site deletion at the 5′-end (RNA I-5) resulted in an approximately twofold increase in the steady-state levels of RNA I-5 and the copy number of ColE1-type plasmid in E. coli cells expressing wild-type or variant RNase E compared to those expressing RNA I. These results indicate that RNA I-5 does not efficiently function as an antisense RNA despite having a triphosphate group at the 5′-end, which protects the RNA from ribonuclease attack. Our study suggests that increased cleavage rates of RNase E lead to relaxed cleavage specificity on RNA I and the inability of the cleavage product of RNA I as an antisense regulator in vivo does not stem from its instability by having 5′-monophosphorylated end. © 2023, The Author(s), under exclusive licence to Microbiological Society of Korea. | - |
dc.format.extent | 10 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | The Korean Society for Mocrobiology / The Korean Society of Virology | - |
dc.title | Relaxed Cleavage Specificity of Hyperactive Variants of Escherichia coli RNase E on RNA I | - |
dc.type | Article | - |
dc.identifier.doi | 10.1007/s12275-023-00013-z | - |
dc.identifier.bibliographicCitation | Journal of Microbiology, v.61, no.2, pp 211 - 220 | - |
dc.identifier.kciid | ART002938910 | - |
dc.description.isOpenAccess | Y | - |
dc.identifier.wosid | 000936376900001 | - |
dc.identifier.scopusid | 2-s2.0-85148519494 | - |
dc.citation.endPage | 220 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 211 | - |
dc.citation.title | Journal of Microbiology | - |
dc.citation.volume | 61 | - |
dc.type.docType | Article | - |
dc.publisher.location | 대한민국 | - |
dc.subject.keywordAuthor | Cleavage specificity | - |
dc.subject.keywordAuthor | Endoribonuclease | - |
dc.subject.keywordAuthor | Plasmid copy number | - |
dc.subject.keywordAuthor | RNA I | - |
dc.subject.keywordAuthor | RNase E | - |
dc.subject.keywordPlus | RIBONUCLEASE-E | - |
dc.subject.keywordPlus | MESSENGER-RNA | - |
dc.subject.keywordPlus | CATALYTIC DOMAIN | - |
dc.subject.keywordPlus | ANTISENSE RNAI | - |
dc.subject.keywordPlus | DEGRADATION | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | MATURATION | - |
dc.subject.keywordPlus | ABUNDANCE | - |
dc.subject.keywordPlus | MUTATION | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.relation.journalResearchArea | Microbiology | - |
dc.relation.journalWebOfScienceCategory | Microbiology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
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