Crystal structure of Streptomyces coelicolor RraAS2, an unusual member of the RNase E inhibitor RraA protein family
DC Field | Value | Language |
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dc.contributor.author | Park, Nohra | - |
dc.contributor.author | Heo, Jihune | - |
dc.contributor.author | Song, Saemee | - |
dc.contributor.author | Jo, Inseong | - |
dc.contributor.author | Lee, Kangseok | - |
dc.contributor.author | Ha, Nam-Chul | - |
dc.date.available | 2019-03-08T08:56:42Z | - |
dc.date.issued | 2017-05 | - |
dc.identifier.issn | 1225-8873 | - |
dc.identifier.issn | 1976-3794 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/4497 | - |
dc.description.abstract | Bacterial ribonuclease E (RNase E) plays a crucial role in the processing and decay of RNAs. A small protein named RraA negatively regulates the activity of RNase E via protein-protein interaction in various bacteria. Recently, RraAS1 and RraAS2, which are functional homologs of RraA from Escherichia coli, were identified in the Gram-positive species Streptomyces coelicolor. RraAS1 and RraAS2 inhibit RNase ES ribonuclease activity in S. coelicolor. RraAS1 and RraAS2 have a C-terminal extension region unlike typical bacterial RraA proteins. In this study, we present the crystal structure of RraAS2, exhibiting a hexamer arranged in a dimer of trimers, consistent with size exclusion chromatographic results. Importantly, the C-terminal extension region formed a long alpha-helix at the junction of the neighboring subunit, which is similar to the trimeric RraA orthologs from Saccharomyces cerevisiae. Truncation of the C-terminal extension region resulted in loss of RNase ES inhibition, demonstrating its crucial role. Our findings present the first bacterial RraA that has a hexameric assembly with a C-terminal extension alpha-helical region, which plays an essential role in the regulation of RNase ES activity in S. coelicolor. | - |
dc.format.extent | 8 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | MICROBIOLOGICAL SOCIETY KOREA | - |
dc.title | Crystal structure of Streptomyces coelicolor RraAS2, an unusual member of the RNase E inhibitor RraA protein family | - |
dc.type | Article | - |
dc.identifier.doi | 10.1007/s12275-017-7053-8 | - |
dc.identifier.bibliographicCitation | JOURNAL OF MICROBIOLOGY, v.55, no.5, pp 388 - 395 | - |
dc.identifier.kciid | ART002220835 | - |
dc.description.isOpenAccess | Y | - |
dc.identifier.wosid | 000400268500010 | - |
dc.identifier.scopusid | 2-s2.0-85019050800 | - |
dc.citation.endPage | 395 | - |
dc.citation.number | 5 | - |
dc.citation.startPage | 388 | - |
dc.citation.title | JOURNAL OF MICROBIOLOGY | - |
dc.citation.volume | 55 | - |
dc.type.docType | Article | - |
dc.publisher.location | 대한민국 | - |
dc.subject.keywordAuthor | Rnase ES inhibitor | - |
dc.subject.keywordAuthor | crystal structure | - |
dc.subject.keywordAuthor | Streptomyces coelicolor | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI RRAA | - |
dc.subject.keywordPlus | RIBONUCLEOLYTIC ACTIVITY | - |
dc.subject.keywordPlus | VIBRIO-VULNIFICUS | - |
dc.subject.keywordPlus | DEGRADOSOME | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | ORTHOLOGS | - |
dc.subject.keywordPlus | ABUNDANCE | - |
dc.subject.keywordPlus | DOMAINS | - |
dc.relation.journalResearchArea | Microbiology | - |
dc.relation.journalWebOfScienceCategory | Microbiology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
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