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TitleRegulatory coiled-coil domains promote head-to-head assemblies of AAA+ chaperones essential for tunable activity control.
Journal, issue, pagesElife, Vol. 6, Year 2017
Publish dateNov 22, 2017
AuthorsMarta Carroni / Kamila B Franke / Michael Maurer / Jasmin Jäger / Ingo Hantke / Felix Gloge / Daniela Linder / Sebastian Gremer / Kürşad Turgay / Bernd Bukau / Axel Mogk /
PubMed AbstractRing-forming AAA+ chaperones exert ATP-fueled substrate unfolding by threading through a central pore. This activity is potentially harmful requiring mechanisms for tight repression and substrate- ...Ring-forming AAA+ chaperones exert ATP-fueled substrate unfolding by threading through a central pore. This activity is potentially harmful requiring mechanisms for tight repression and substrate-specific activation. The AAA+ chaperone ClpC with the peptidase ClpP forms a bacterial protease essential to virulence and stress resistance. The adaptor MecA activates ClpC by targeting substrates and stimulating ClpC ATPase activity. We show how ClpC is repressed in its ground state by determining ClpC cryo-EM structures with and without MecA. ClpC forms large two-helical assemblies that associate via head-to-head contacts between coiled-coil middle domains (MDs). MecA converts this resting state to an active planar ring structure by binding to MD interaction sites. Loss of ClpC repression in MD mutants causes constitutive activation and severe cellular toxicity. These findings unravel an unexpected regulatory concept executed by coiled-coil MDs to tightly control AAA+ chaperone activity.
External linksElife / PubMed:29165246 / PubMed Central
MethodsEM (single particle)
Resolution8.4 - 11.0 Å
Structure data

3894

6em8

EMDB-3894, PDB-6em8:
S.aureus ClpC resting state, C2 symmetrised
Method: EM (single particle) / Resolution: 8.4 Å

3895

6em9

EMDB-3895, PDB-6em9:
S.aureus ClpC resting state, asymmetric map
Method: EM (single particle) / Resolution: 8.4 Å

3897

6emw

EMDB-3897, PDB-6emw:
Structure of S.aureus ClpC in complex with MecA
Method: EM (single particle) / Resolution: 11.0 Å

Source
  • staphylococcus aureus (bacteria)
  • staphylococcus aureus (strain bovine rf122 / et3-1) (bacteria)
KeywordsCHAPERONE / ClpC / AAA+ protease / oligomeric complex / AAA+ protein / unfoldase

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