Identification of amino acid residues in the catalytic domain of RNase E essential for survival of Escherichia coli: Functional analysis of DNase I subdomain
DC Field | Value | Language |
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dc.contributor.author | Shin, Eunkyoung | - |
dc.contributor.author | Go, Hayoung | - |
dc.contributor.author | Yeom, Ji-Hyun | - |
dc.contributor.author | Won, Miae | - |
dc.contributor.author | Bae, Jeehyeon | - |
dc.contributor.author | Han, Seung Hyun | - |
dc.contributor.author | Han, Kook | - |
dc.contributor.author | Lee, Younghoon | - |
dc.contributor.author | Ha, Nam-Chul | - |
dc.contributor.author | Moore ,Christopher J. | - |
dc.contributor.author | Sohlberg, Bjoern | - |
dc.contributor.author | Cohen, Stanley N. | - |
dc.contributor.author | Lee, Kangseok | - |
dc.date.available | 2019-05-30T04:40:51Z | - |
dc.date.issued | 2008-08 | - |
dc.identifier.issn | 0016-6731 | - |
dc.identifier.issn | 1943-2631 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/23675 | - |
dc.description.abstract | RNase E is all essential Escherichia coli endoribonuclease that plays a major endoribonuclease that plays a major role in the decay and processing of a large fraction of RNAs in the cell. To better understand the molecular mechanisms of RNase E action, we performed a genetic screen for amino acid substitution in the catalytic domain of the protein (N-Rne) that knock down the ability of RNase E to support survival of E. coli. Comparative phylogenetic analysis of RNase E homologs shows that wild-type residues at these mutated positions are nearly invariably conserved. Cells conditionally expressing these N-Rne mutants in the absence of wild-type RNase E show a decrease in copy number of plasmids regulated by the RNase E substrate RNA 1, and accumulation of 5S ribosomal RNA, M1 RNA, and tRNA(Asn) precursors, as has been found in Rne-depleted cells, suggesting that the inability of these mutants to support cellular growth results from loss of ribonucleolytic activity. Purified mutant proteins containing an amino acid substitution in the DNase 1 subdomain, which is spatially distant from the catalytic site posited from crystallographic studies, showed defecting binding to an RNase E substrate, p23 RNA, but still retained RNA cleavage activity-implicating a previously unidentified structural motif in the DNase 1 subdomain in the binding of RNase E to targeted RNA molecules, demonstrating the role of the DNase 1 domain in RNase E activity. subdoinain, which is spatially distant from the Catalytic site posited from ctystallographic studies, showed | - |
dc.format.extent | 9 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | GENETICS SOC AM | - |
dc.title | Identification of amino acid residues in the catalytic domain of RNase E essential for survival of Escherichia coli: Functional analysis of DNase I subdomain | - |
dc.type | Article | - |
dc.identifier.doi | 10.1534/genetics.108.088492 | - |
dc.identifier.bibliographicCitation | GENETICS, v.179, no.4, pp 1871 - 1879 | - |
dc.description.isOpenAccess | Y | - |
dc.identifier.wosid | 000258591200012 | - |
dc.identifier.scopusid | 2-s2.0-55749101368 | - |
dc.citation.endPage | 1879 | - |
dc.citation.number | 4 | - |
dc.citation.startPage | 1871 | - |
dc.citation.title | GENETICS | - |
dc.citation.volume | 179 | - |
dc.type.docType | Article | - |
dc.publisher.location | 미국 | - |
dc.subject.keywordPlus | 16S RIBOSOMAL-RNA | - |
dc.subject.keywordPlus | MESSENGER-RNA | - |
dc.subject.keywordPlus | RIBONUCLEASE-E | - |
dc.subject.keywordPlus | NUCLEOTIDE-SEQUENCE | - |
dc.subject.keywordPlus | M1 RNA | - |
dc.subject.keywordPlus | DEGRADOSOME | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | DEGRADATION | - |
dc.subject.keywordPlus | MATURATION | - |
dc.relation.journalResearchArea | Genetics & Heredity | - |
dc.relation.journalWebOfScienceCategory | Genetics & Heredity | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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