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Lee, Seong Gyu
단백질 커뮤니케이션 그룹
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ClpL is a functionally active tetradecameric AAA plus chaperone, distinct from hexameric/dodecameric ones

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dc.contributor.authorGyuhee Kim-
dc.contributor.authorSeong-Gyu Lee-
dc.contributor.authorSeungsu Han-
dc.contributor.authorJaeeun Jung-
dc.contributor.authorHyeong Seop Jeong-
dc.contributor.authorJae-kyung Hyun-
dc.contributor.authorDong-Kwon Rhee-
dc.contributor.authorHo Min Kim-
dc.contributor.authorSangho Lee-
dc.date.accessioned2020-12-22T02:30:41Z-
dc.date.accessioned2020-12-22T02:30:41Z-
dc.date.available2020-12-22T02:30:41Z-
dc.date.available2020-12-22T02:30:41Z-
dc.date.created2020-10-16-
dc.date.issued2020-11-
dc.identifier.issn0892-6638-
dc.identifier.urihttps://pr.ibs.re.kr/handle/8788114/7569-
dc.description.abstract© 2020 Federation of American Societies for Experimental Biology. AAA+ (ATPases associated with diverse cellular activities) chaperones are involved in a plethora of cellular activities to ensure protein homeostasis. The function of AAA+ chaperones is mostly modulated by their hexameric/dodecameric quaternary structures. Here we report the structural and biochemical characterizations of a tetradecameric AAA+ chaperone, ClpL fromStreptococcus pneumoniae. ClpL exists as a tetradecamer in solution in the presence of ATP. The cryo-EM structure of ClpL at 4.5 angstrom resolution reveals a striking tetradecameric arrangement. Solution structures of ClpL derived from small-angle X-ray scattering data suggest that the tetradecameric ClpL could assume a spiral conformation found in active hexameric/dodecameric AAA+ chaperone structures. Vertical positioning of the middle domain accounts for the head-to-head arrangement of two heptameric rings. Biochemical activity assays with site-directed mutagenesis confirmed the critical roles of residues both in the integrity of the tetradecameric arrangement and activities of ClpL. Non-conserved Q321 and R670 are crucial in the heptameric ring assembly of ClpL. These results establish that ClpL is a functionally active tetradecamer, clearly distinct from hexameric/dodecameric AAA+ chaperones-
dc.description.uri1-
dc.language영어-
dc.publisherFEDERATION AMER SOC EXP BIOL-
dc.subjectchaperone-
dc.subjectClpL-
dc.subjectHsp100-
dc.subjectS-
dc.subjectpneumoniae-
dc.subjecttetradecamer-
dc.titleClpL is a functionally active tetradecameric AAA plus chaperone, distinct from hexameric/dodecameric ones-
dc.typeArticle-
dc.type.rimsART-
dc.identifier.wosid000570574700001-
dc.identifier.scopusid2-s2.0-85090431615-
dc.identifier.rimsid73224-
dc.contributor.affiliatedAuthorSeong-Gyu Lee-
dc.contributor.affiliatedAuthorHo Min Kim-
dc.identifier.doi10.1096/fj.202000843R-
dc.identifier.bibliographicCitationFASEB JOURNAL, v.34, no.11, pp.14353 - 14370-
dc.citation.titleFASEB JOURNAL-
dc.citation.volume34-
dc.citation.number11-
dc.citation.startPage14353-
dc.citation.endPage14370-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.subject.keywordPlusCRYO-EM STRUCTURE-
dc.subject.keywordPlusESCHERICHIA-COLI-
dc.subject.keywordPlusMOLECULAR CHAPERONE-
dc.subject.keywordPlusATPASE CYCLE-
dc.subject.keywordPlusMIDDLE DOMAIN-
dc.subject.keywordPlusPROTEIN-
dc.subject.keywordPlusBINDING-
dc.subject.keywordPlusHSP104-
dc.subject.keywordPlusOLIGOMERIZATION-
dc.subject.keywordPlusDYNAMICS-
dc.subject.keywordAuthorchaperone-
dc.subject.keywordAuthorClpL-
dc.subject.keywordAuthorHsp100-
dc.subject.keywordAuthorS-
dc.subject.keywordAuthorpneumoniae-
dc.subject.keywordAuthortetradecamer-
Appears in Collections:
Pioneer Research Center for Biomolecular and Cellular Structure(바이오분자 및 세포구조 연구단) > Protein Communication Group(단백질 커뮤니케이션 그룹) > 1. Journal Papers (저널논문)
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