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Molecular insights into the m-AAA protease-mediated dislocation of transmembrane helices in the mitochondrial inner membrane

DC Field Value Language
dc.contributor.authorLee, Seoeun-
dc.contributor.authorLee, Hunsang-
dc.contributor.authorYoo, Suji-
dc.contributor.authorKim, Hyun Ah-
dc.creatorHyun Ah Kim-
dc.date.accessioned2019-04-24T23:00:55Z-
dc.date.available2020-04-05T23:00:55Z-
dc.date.created2018-07-25-
dc.date.created2018-07-25-
dc.date.created2018-07-25-
dc.date.issued2017-12-
dc.identifier.citationJournal of Biological Chemistry, Vol.292 No.49, pp.20058-20066-
dc.identifier.issn0021-9258-
dc.identifier.urihttps://hdl.handle.net/10371/148612-
dc.description.abstractProtein complexes involved in respiration, ATP synthesis, and protein import reside in the mitochondrial inner membrane; thus, proper regulation of these proteins is essential for cell viability. The m-AAA protease, a conserved hetero-hexameric AAA (ATPase associated with diverse cellular activities) protease, composed of the Yta10 and Yta12 proteins, regulates mitochondrial proteostasis by mediating protein maturation and degradation. It also recognizes and mediates the dislocation of membrane-embedded substrates, including foreign transmembrane (TM) segments, but the molecular mechanism involved in these processes remains elusive. This study investigated the role of the TM domains in the m-AAA protease by systematic replacement of one TM domain at a time in yeast. Our data indicated that replacement of the Yta10 TM2 domain abolishes membrane dislocation for only a subset of substrates, whereas replacement of the Yta12 TM2 domain impairs membrane dislocation for all tested substrates, suggesting different roles of the TM domains in each m-AAA protease subunit. Furthermore, m-AAA protease-mediated membrane dislocation was impaired in the presence of a large downstream hydrophilic moiety in a membrane substrate. This finding suggested that the m-AAA protease cannot dislocate large hydrophilic domains across the membrane, indicating that the membrane dislocation probably occurs in a lipid environment. In summary, this study highlights previously underappreciated biological roles of TM domains of the m-AAA proteases in mediating the recognition and dislocation of membrane-embedded substrates.-
dc.language영어-
dc.language.isoenen
dc.publisherAmerican Society for Biochemistry and Molecular Biology Inc.-
dc.titleMolecular insights into the m-AAA protease-mediated dislocation of transmembrane helices in the mitochondrial inner membrane-
dc.typeArticle-
dc.identifier.doi10.1074/jbc.M117.796763-
dc.citation.journaltitleJournal of Biological Chemistry-
dc.identifier.wosid000417696400013-
dc.identifier.scopusid2-s2.0-85037540058-
dc.description.srndOAIID:RECH_ACHV_DSTSH_NO:T201718557-
dc.description.srndRECH_ACHV_FG:RR00200001-
dc.description.srndADJUST_YN:-
dc.description.srndEMP_ID:A078040-
dc.description.srndCITE_RATE:4.01-
dc.description.srndFILENAME:2017_Molecular insights into the m-AAA.pdf-
dc.description.srndDEPT_NM:생명과학부-
dc.description.srndEMAIL:joy@snu.ac.kr-
dc.description.srndSCOPUS_YN:Y-
dc.description.srndFILEURL:https://srnd.snu.ac.kr/eXrepEIR/fws/file/256da6b1-7445-4d8b-9207-f8e1fb4bd40a/link-
dc.citation.endpage20066-
dc.citation.number49-
dc.citation.startpage20058-
dc.citation.volume292-
dc.description.isOpenAccessY-
dc.contributor.affiliatedAuthorKim, Hyun Ah-
dc.identifier.srndT201718557-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.subject.keywordPlusCHAPERONE-LIKE ACTIVITY-
dc.subject.keywordPlusRHOMBOID PROTEASE-
dc.subject.keywordPlusSIGNAL SEQUENCE-
dc.subject.keywordPlusIN-VIVO-
dc.subject.keywordPlusPROTEINS-
dc.subject.keywordPlusYEAST-
dc.subject.keywordPlusATP-
dc.subject.keywordPlusDEGRADATION-
dc.subject.keywordPlusCOMPLEX-
dc.subject.keywordPlusMGM1-
dc.subject.keywordAuthorATPase associated with diverse cellular activities (AAA)-
dc.subject.keywordAuthormembrane-
dc.subject.keywordAuthormitochondria-
dc.subject.keywordAuthortransmembrane domain-
dc.subject.keywordAuthoryeast-
dc.subject.keywordAuthorYta10-
dc.subject.keywordAuthorYta12-
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