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Bacterial Cell Stress Protein ClpP: A Novel Antibiotic Target

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Moonlighting Cell Stress Proteins in Microbial Infections

Part of the book series: Heat Shock Proteins ((HESP,volume 7))

Abstract

Clp proteases play important roles in maintaining the protein homeostasis in bacterial cells, particularly under stress conditions. On the one hand they perform central functions in general protein quality control by degrading mis-translated, denatured or otherwise malfunctioning proteins. On the other hand, they direct cellular differentiation and development programs by temporally and spatially precise degradation of key regulatory proteins. On top of their already diverse functions in the physiological context, an additional role was discovered over the last years for this class of protein, namely to serve as a target for antibiotic action. Especially the conserved proteolytic core component of the protease machinery, designated ClpP, is important here. ClpP is capable of killing bacteria via uncontrolled proteolysis after deregulation by a potent class of novel antibiotics.

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Authors and Affiliations

  1. Institute for Pharmaceutical Biology and Biotechnology, University of Duesseldorf, Building 26.32.U1.82, Universitaetsstrasse 1, Duesseldorf, D-40225, Germany

    Heike Brötz-Oesterhelt & Peter Sass

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  1. Heike Brötz-Oesterhelt
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  2. Peter Sass
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Correspondence to Heike Brötz-Oesterhelt .

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Editors and Affiliations

  1. Eastman Dental Institute, Div. Microbial Diseases, University College, London, Gray's Inn Road 256, London, WC1X 8LD, United Kingdom

    Brian Henderson

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Brötz-Oesterhelt, H., Sass, P. (2013). Bacterial Cell Stress Protein ClpP: A Novel Antibiotic Target. In: Henderson, B. (eds) Moonlighting Cell Stress Proteins in Microbial Infections. Heat Shock Proteins, vol 7. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-6787-4_24

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