DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Gyuhee | ko |
dc.contributor.author | Lee, Seong-Gyu | ko |
dc.contributor.author | Han, Seungsu | ko |
dc.contributor.author | Jung, Jaeeun | ko |
dc.contributor.author | Jeong, Hyeong Seop | ko |
dc.contributor.author | Hyun, Jae-kyung | ko |
dc.contributor.author | Rhee, Dong-Kwon | ko |
dc.contributor.author | Kim, Ho Min | ko |
dc.contributor.author | Lee, Sangho | ko |
dc.date.accessioned | 2021-01-28T05:56:50Z | - |
dc.date.available | 2021-01-28T05:56:50Z | - |
dc.date.created | 2020-10-05 | - |
dc.date.issued | 2020-11 | - |
dc.identifier.citation | FASEB JOURNAL, v.34, no.11, pp.14353 - 14370 | - |
dc.identifier.issn | 0892-6638 | - |
dc.identifier.uri | http://hdl.handle.net/10203/280082 | - |
dc.description.abstract | 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.language | English | - |
dc.publisher | WILEY | - |
dc.title | ClpL is a functionally active tetradecameric AAA plus chaperone, distinct from hexameric/dodecameric ones | - |
dc.type | Article | - |
dc.identifier.wosid | 000570574700001 | - |
dc.identifier.scopusid | 2-s2.0-85090431615 | - |
dc.type.rims | ART | - |
dc.citation.volume | 34 | - |
dc.citation.issue | 11 | - |
dc.citation.beginningpage | 14353 | - |
dc.citation.endingpage | 14370 | - |
dc.citation.publicationname | FASEB JOURNAL | - |
dc.identifier.doi | 10.1096/fj.202000843R | - |
dc.contributor.localauthor | Kim, Ho Min | - |
dc.contributor.nonIdAuthor | Kim, Gyuhee | - |
dc.contributor.nonIdAuthor | Lee, Seong-Gyu | - |
dc.contributor.nonIdAuthor | Han, Seungsu | - |
dc.contributor.nonIdAuthor | Jung, Jaeeun | - |
dc.contributor.nonIdAuthor | Jeong, Hyeong Seop | - |
dc.contributor.nonIdAuthor | Hyun, Jae-kyung | - |
dc.contributor.nonIdAuthor | Rhee, Dong-Kwon | - |
dc.contributor.nonIdAuthor | Lee, Sangho | - |
dc.description.isOpenAccess | Y | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | chaperone | - |
dc.subject.keywordAuthor | ClpL | - |
dc.subject.keywordAuthor | Hsp100 | - |
dc.subject.keywordAuthor | S | - |
dc.subject.keywordAuthor | pneumoniae | - |
dc.subject.keywordAuthor | tetradecamer | - |
dc.subject.keywordPlus | CRYO-EM STRUCTURE | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | MOLECULAR CHAPERONE | - |
dc.subject.keywordPlus | ATPASE CYCLE | - |
dc.subject.keywordPlus | MIDDLE DOMAIN | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | HSP104 | - |
dc.subject.keywordPlus | OLIGOMERIZATION | - |
dc.subject.keywordPlus | DYNAMICS | - |
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