AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2015-12

AUTHORS

Malte Gersch, Kirsten Famulla, Maria Dahmen, Christoph Göbl, Imran Malik, Klaus Richter, Vadim S. Korotkov, Peter Sass, Helga Rübsamen-Schaeff, Tobias Madl, Heike Brötz-Oesterhelt, Stephan A. Sieber

ABSTRACT

The Clp protease complex degrades a multitude of substrates, which are engaged by a AAA+ chaperone such as ClpX and subsequently digested by the dynamic, barrel-shaped ClpP protease. Acyldepsipeptides (ADEPs) are natural product-derived antibiotics that activate ClpP for chaperone-independent protein digestion. Here we show that both protein and small-molecule activators of ClpP allosterically control the ClpP barrel conformation. We dissect the catalytic mechanism with chemical probes and show that ADEP in addition to opening the axial pore directly stimulates ClpP activity through cooperative binding. ClpP activation thus reaches beyond active site accessibility and also involves conformational control of the catalytic residues. Moreover, we demonstrate that substoichiometric amounts of ADEP potently prevent binding of ClpX to ClpP and, at the same time, partially inhibit ClpP through conformational perturbance. Collectively, our results establish the hydrophobic binding pocket as a major conformational regulatory site with implications for both ClpXP proteolysis and ADEP-based anti-bacterial activity. More... »

PAGES

6320

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncomms7320

DOI

http://dx.doi.org/10.1038/ncomms7320

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1037196231

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/25695750


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464 https://www.grid.ac/institutes/grid.6936.a schema:alternateName Technical University Munich
465 schema:name Department of Chemistry and Center for Integrated Protein Science Munich (CIPSM), Technische Universität München, Lichtenbergstraße 4, 85748 Garching, Germany
466 rdf:type schema:Organization
 




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