Regulatory coiled-coil domains promote head-to-head assemblies of AAA+ chaperones essential for tunable activity control

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 essentia...

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Detalles Bibliográficos
Autores principales: Carroni, Marta, Franke, Kamila B, Maurer, Michael, Jäger, Jasmin, Hantke, Ingo, Gloge, Felix, Linder, Daniela, Gremer, Sebastian, Turgay, Kürşad, Bukau, Bernd, Mogk, Axel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2017
Materias:
Biochemistry and Chemical Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5699869/
https://www.ncbi.nlm.nih.gov/pubmed/29165246
http://dx.doi.org/10.7554/eLife.30120

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5699869/
https://www.ncbi.nlm.nih.gov/pubmed/29165246
http://dx.doi.org/10.7554/eLife.30120

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