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Chaperone-Proteases of Mycobacteria

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The Molecular Chaperones Interaction Networks in Protein Folding and Degradation

Part of the book series: Interactomics and Systems Biology ((INTERACTOM,volume 1))

Abstract

Energy-dependent protein degradation ensures protein homeostasis in all organisms. It requires the concerted action of unfoldase and protease components to achieve the processive cleavage of substrate proteins into small peptides. Rapid changes in nutritional sources and oxygen levels are constant challenges of the mycobacterial habitat, and survival under these conditions requires a multitude of adaptive response mechanisms including—as one important cornerstone—protein degradation. Three energy-dependent protease systems invariantly exist in all mycobacteria: the membrane-associated FtsH, the Clp protease complexes, and a bacterial proteasome assembly that is unique to the actinobacterial phylum. In this chapter, structural features, substrate recruitment principles, and cellular roles of all three systems are discussed.

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Acknowledgments

We thank members of the Weber-Ban group for critically reading the manuscript. This work was supported by the Swiss National Science Foundation (SNSF), the National Centre of Excellence in Research (NCCR) Structural Biology program of the SNSF and an ETH research grant.

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Authors and Affiliations

  1. Institute of Molecular Biology & Biophysics, ETH Zurich, Zurich, Switzerland

    Juerg Laederach BSc, MSc, Julia Leodolter MSc, Jannis Warweg Dipl. Biolgie & Eilika Weber-Ban PhD

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  1. Juerg Laederach BSc, MSc
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  2. Julia Leodolter MSc
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  3. Jannis Warweg Dipl. Biolgie
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  4. Eilika Weber-Ban PhD
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Correspondence to Eilika Weber-Ban PhD .

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  1. Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada

    Walid A. Houry

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Laederach, J., Leodolter, J., Warweg, J., Weber-Ban, E. (2014). Chaperone-Proteases of Mycobacteria. In: Houry, W. (eds) The Molecular Chaperones Interaction Networks in Protein Folding and Degradation. Interactomics and Systems Biology, vol 1. Springer, New York, NY. https://doi.org/10.1007/978-1-4939-1130-1_16

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