ClpL is a functionally active tetradecameric AAA plus chaperone, distinct from hexameric/dodecameric ones

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dc.contributor.authorKim, Gyuheeko
dc.contributor.authorLee, Seong-Gyuko
dc.contributor.authorHan, Seungsuko
dc.contributor.authorJung, Jaeeunko
dc.contributor.authorJeong, Hyeong Seopko
dc.contributor.authorHyun, Jae-kyungko
dc.contributor.authorRhee, Dong-Kwonko
dc.contributor.authorKim, Ho Minko
dc.contributor.authorLee, Sanghoko
dc.date.accessioned2021-01-28T05:56:50Z-
dc.date.available2021-01-28T05:56:50Z-
dc.date.created2020-10-05-
dc.date.issued2020-11-
dc.identifier.citationFASEB JOURNAL, v.34, no.11, pp.14353 - 14370-
dc.identifier.issn0892-6638-
dc.identifier.urihttp://hdl.handle.net/10203/280082-
dc.description.abstractAAA+ (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.languageEnglish-
dc.publisherWILEY-
dc.titleClpL is a functionally active tetradecameric AAA plus chaperone, distinct from hexameric/dodecameric ones-
dc.typeArticle-
dc.identifier.wosid000570574700001-
dc.identifier.scopusid2-s2.0-85090431615-
dc.type.rimsART-
dc.citation.volume34-
dc.citation.issue11-
dc.citation.beginningpage14353-
dc.citation.endingpage14370-
dc.citation.publicationnameFASEB JOURNAL-
dc.identifier.doi10.1096/fj.202000843R-
dc.contributor.localauthorKim, Ho Min-
dc.contributor.nonIdAuthorKim, Gyuhee-
dc.contributor.nonIdAuthorLee, Seong-Gyu-
dc.contributor.nonIdAuthorHan, Seungsu-
dc.contributor.nonIdAuthorJung, Jaeeun-
dc.contributor.nonIdAuthorJeong, Hyeong Seop-
dc.contributor.nonIdAuthorHyun, Jae-kyung-
dc.contributor.nonIdAuthorRhee, Dong-Kwon-
dc.contributor.nonIdAuthorLee, Sangho-
dc.description.isOpenAccessY-
dc.type.journalArticleArticle-
dc.subject.keywordAuthorchaperone-
dc.subject.keywordAuthorClpL-
dc.subject.keywordAuthorHsp100-
dc.subject.keywordAuthorS-
dc.subject.keywordAuthorpneumoniae-
dc.subject.keywordAuthortetradecamer-
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-
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