Vibralactone as a Tool to Study the Activity and Structure of the ClpP1P2 Complex from Listeria monocytogenes

Authors

  • Evelyn Zeiler,

    1. Department Chemie, Center for Integrated Protein Science CIPSM, Institute of Advanced Studies IAS, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching (Germany)
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  • Dr. Nathalie Braun,

    1. Center for Integrated Protein Science Munich CIPSM, Department of Chemistry, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching (Germany)
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  • Dr. Thomas Böttcher,

    1. AVIRU, EXIST Transfer of Research, OC II, Lichtenbergstrasse 4, 85747 Garching (Germany)
    2. Current address: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA (USA)
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  • Andreas Kastenmüller,

    1. Center for Integrated Protein Science Munich CIPSM, Department of Chemistry, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching (Germany)
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  • Prof. Dr. Sevil Weinkauf,

    1. Center for Integrated Protein Science Munich CIPSM, Department of Chemistry, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching (Germany)
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  • Prof. Dr. Stephan A. Sieber

    Corresponding author
    1. Department Chemie, Center for Integrated Protein Science CIPSM, Institute of Advanced Studies IAS, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching (Germany)
    • Department Chemie, Center for Integrated Protein Science CIPSM, Institute of Advanced Studies IAS, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching (Germany)
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  • We thank Mona Wolff for excellent scientific support and Wolfgang Steglich for helpful discussions. E.Z. was supported by the SFB749 and by the TUM-GS. E.Z. thanks Quan Zhou for helpful discussions. T.B. was supported by the German National Academic Foundation and by an EXIST technology transfer grant of the Federal Ministry of Economics and Technology (BMWi); S.A.S. was supported by the Deutsche Forschungsgemeinschaft (Emmy Noether), SFB749, FOR1406, an ERC starting grant, and the Center for Integrated Protein Science Munich CIPSM. S.W. and N.B. were funded by the DFG (SFB594) and CIPSM.

Abstract

original image

The Clp proteolytic machinery has important functions in many bacteria such as L. monocytogenes. Some organisms encode for two uncharacterized ClpP isoforms. Vibralactone was used to study the activity and assembly of ClpP1 and ClpP2 subunits in a hetero-oligomeric complex. Electron microscopic images reveal that the tetradecameric assembly is made up of two stacked homoheptameric ClpP1 and ClpP2 rings.

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