Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX SCIE SCOPUS
DC Field | Value | Language |
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dc.contributor.author | Kang, S.G. | - |
dc.contributor.author | Dimitrova, M.N. | - |
dc.contributor.author | Ortega, J. | - |
dc.contributor.author | Ginsburg, A. | - |
dc.contributor.author | Maurizi, M.R. | - |
dc.date.accessioned | 2020-04-20T13:55:24Z | - |
dc.date.available | 2020-04-20T13:55:24Z | - |
dc.date.created | 2020-01-28 | - |
dc.date.issued | 2005-10 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | https://sciwatch.kiost.ac.kr/handle/2020.kiost/5018 | - |
dc.description.abstract | The functional form of ClpP, the proteolytic component of ATP-dependent Clp proteases, is a hollow-cored particle composed of two heptameric rings joined face-to-face forming an aqueous chamber containing the proteolytic active sites. We have found that isolated human mitochondrial ClpP (hClpP) is stable as a heptamer and remains a monodisperse species (s20,w 7.0 S; M app 169, 200) at concentrations ≥3 mg/ml. Heptameric hClpP has no proteolytic activity and very low peptidase activity. In the presence of ATP, hClpX interacts with hClpP forming a complex, which by equilibrium sedimentation measurements has a Mapp of 1 × 106. Electron microscopy confirmed that the complex consisted of a double ring of hClpP with an hClpX ring axially aligned on each end. The hClpXP complex has protease activity and greatly increased peptidase activity, indicating that interaction with hClpX affects the conformation of the hClpP catalytic active site. A mutant of hClpP, in which a cysteine residue was introduced into the handle region at the interface between the two rings formed stable tetradecamers under oxidizing conditions but spontaneously dissociated into two heptamers upon reduction. Thus, hClpP rings interact transiently but very weakly in solution, and hClpX must exert an allosteric effect on hClpP to promote a conformation that stabilizes the tetradecamer. These data suggest that hClpX can regulate the appearance of hClpP peptidase activity in mitochondria and might affect the nature of the degradation products released during ATP-dependent proteolytic cycles. | - |
dc.description.uri | 1 | - |
dc.language | English | - |
dc.publisher | American Society for Biochemistry and Molecular Biology Inc. | - |
dc.title | Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX | - |
dc.type | Article | - |
dc.citation.endPage | 35432 | - |
dc.citation.startPage | 35424 | - |
dc.citation.title | Journal of Biological Chemistry | - |
dc.citation.volume | 280 | - |
dc.citation.number | 42 | - |
dc.contributor.alternativeName | 강성균 | - |
dc.identifier.bibliographicCitation | Journal of Biological Chemistry, v.280, no.42, pp.35424 - 35432 | - |
dc.identifier.doi | 10.1074/jbc.M507240200 | - |
dc.identifier.scopusid | 2-s2.0-27444440627 | - |
dc.identifier.wosid | 000232561200042 | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.subject.keywordPlus | Cytology | - |
dc.subject.keywordPlus | Electron microscopes | - |
dc.subject.keywordPlus | Enzyme kinetics | - |
dc.subject.keywordPlus | Interfaces (materials) | - |
dc.subject.keywordPlus | Mutagenesis | - |
dc.subject.keywordPlus | Solutions | - |
dc.subject.keywordPlus | Heptameric rings | - |
dc.subject.keywordPlus | Proteolytic component | - |
dc.subject.keywordPlus | Tetradecamer | - |
dc.subject.keywordPlus | Cells | - |
dc.subject.keywordPlus | adenosine triphosphate | - |
dc.subject.keywordPlus | cysteine | - |
dc.subject.keywordPlus | Hydrogen-Ion Concentration | - |
dc.subject.keywordPlus | endopeptidase Clp | - |
dc.subject.keywordPlus | endopeptidase ClpX | - |
dc.subject.keywordPlus | peptidase | - |
dc.subject.keywordPlus | allosterism | - |
dc.subject.keywordPlus | article | - |
dc.subject.keywordPlus | catalysis | - |
dc.subject.keywordPlus | complex formation | - |
dc.subject.keywordPlus | dissociation | - |
dc.subject.keywordPlus | electron microscopy | - |
dc.subject.keywordPlus | enzyme active site | - |
dc.subject.keywordPlus | enzyme activity | - |
dc.subject.keywordPlus | enzyme analysis | - |
dc.subject.keywordPlus | enzyme conformation | - |
dc.subject.keywordPlus | enzyme regulation | - |
dc.subject.keywordPlus | human | - |
dc.subject.keywordPlus | oxidation | - |
dc.subject.keywordPlus | priority journal | - |
dc.subject.keywordPlus | protein assembly | - |
dc.subject.keywordPlus | protein degradation | - |
dc.subject.keywordPlus | protein protein interaction | - |
dc.subject.keywordPlus | reduction | - |
dc.subject.keywordPlus | sedimentation | - |
dc.subject.keywordPlus | Adenosine Triphosphate | - |
dc.subject.keywordPlus | Allosteric Site | - |
dc.subject.keywordPlus | Animals | - |
dc.subject.keywordPlus | Binding Sites | - |
dc.subject.keywordPlus | Chromatin Immunoprecipitation | - |
dc.subject.keywordPlus | Chromatography, Gel | - |
dc.subject.keywordPlus | Cross-Linking Reagents | - |
dc.subject.keywordPlus | Cysteine | - |
dc.subject.keywordPlus | Dimerization | - |
dc.subject.keywordPlus | Disulfides | - |
dc.subject.keywordPlus | Endopeptidase Clp | - |
dc.subject.keywordPlus | Glutaral | - |
dc.subject.keywordPlus | Green Fluorescent Proteins | - |
dc.subject.keywordPlus | Histidine | - |
dc.subject.keywordPlus | Humans | - |
dc.subject.keywordPlus | Hydrolysis | - |
dc.subject.keywordPlus | Liver | - |
dc.subject.keywordPlus | Microscopy, Electron | - |
dc.subject.keywordPlus | Mitochondria | - |
dc.subject.keywordPlus | Mutagenesis | - |
dc.subject.keywordPlus | Mutation | - |
dc.subject.keywordPlus | Peptide Hydrolases | - |
dc.subject.keywordPlus | Protein Binding | - |
dc.subject.keywordPlus | Protein Conformation | - |
dc.subject.keywordPlus | Protein Structure, Tertiary | - |
dc.subject.keywordPlus | Rats | - |
dc.subject.keywordPlus | Recombinant Proteins | - |
dc.subject.keywordPlus | Time Factors | - |
dc.subject.keywordPlus | Trypsin | - |
dc.subject.keywordPlus | Ultracentrifugation | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |