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Structural insights into ubiquitin chain cleavage by Legionella ovarian tumor deubiquitinases

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dc.contributor.authorKang, Sangwoo-
dc.contributor.authorKim, Gyuhee-
dc.contributor.authorChoi, Minhyeong-
dc.contributor.authorJeong, Minwoo-
dc.contributor.authorvan Noort, Gerbrand J. van der Heden-
dc.contributor.authorRoh, Soung-Hun-
dc.contributor.authorShin, Donghyuk-
dc.date.accessioned2024-05-16T01:49:46Z-
dc.date.available2024-05-16T01:49:46Z-
dc.date.created2023-05-23-
dc.date.created2023-05-23-
dc.date.issued2023-07-
dc.identifier.citationLife Science Alliance, Vol.6 No.7-
dc.identifier.issn2575-1077-
dc.identifier.urihttps://hdl.handle.net/10371/202895-
dc.description.abstractAlthough ubiquitin is found only in eukaryotes, several patho-genic bacteria and viruses possess proteins that hinder the host ubiquitin system. Legionella, a gram-negative intracellular bacterium, possesses an ovarian tumor (OTU) family of deubi-quitinases (Lot DUBs). Herein, we describe the molecular char-acteristics of Lot DUBs. We elucidated the structure of the LotA OTU1 domain and revealed that entire Lot DUBs possess a characteristic extended helical lobe that is not found in other OTU-DUBs. The structural topology of an extended helical lobe is the same throughout the Lot family, and it provides an S19 ubiquitin-binding site. Moreover, the catalytic triads of Lot DUBs resemble those of the A20-type OTU-DUBs. Furthermore, we revealed a unique mechanism by which LotA OTU domains co-operate together to distinguish the length of the chain and preferentially cleave longer K48-linked polyubiquitin chains. The LotA OTU1 domain itself cleaves K6-linked ubiquitin chains, whereas it is also essential for assisting the cleavage of longer K48-linked polyubiquitin chains by the OTU2 domain. Thus, this study provides novel insights into the structure and mechanism of action of Lot DUBs.-
dc.language영어-
dc.publisherLife Science Alliance LLC-
dc.titleStructural insights into ubiquitin chain cleavage by Legionella ovarian tumor deubiquitinases-
dc.typeArticle-
dc.identifier.doi10.26508/lsa.202201876-
dc.citation.journaltitleLife Science Alliance-
dc.identifier.wosid000984483500001-
dc.identifier.scopusid2-s2.0-85153921988-
dc.citation.number7-
dc.citation.volume6-
dc.description.isOpenAccessY-
dc.contributor.affiliatedAuthorRoh, Soung-Hun-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.subject.keywordPlusMOLECULAR-BASIS-
dc.subject.keywordPlusSPECIFICITY-
dc.subject.keywordPlusCYSTEINE-
dc.subject.keywordPlusDISTINCT-
dc.subject.keywordPlusFAMILY-
dc.subject.keywordPlusLIGASE-
dc.subject.keywordPlusPROBES-
dc.subject.keywordPlusDOMAIN-
dc.subject.keywordPlusEXPLOITATION-
dc.subject.keywordPlusDIUBIQUITIN-
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  • College of Natural Sciences
  • School of Biological Sciences
Research Area Cryogenic Electron Microscopy (Cryo-EM), Structural Biology, 분자생물학, 생물물리학, 생화학

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