Identification of a Selective, Activity-Based Probe for Glyceraldehyde 3-Phosphate Dehydrogenases

Authors

  • Dr. Farnusch Kaschani,

    1. Zentrum für Medizinische Biotechnologie, Fakultät für Biologie, Universität Duisburg-Essen, Universitätsstrasse 2, 45117 Essen (Germany)
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    • These authors contributed equally to this work.

  • Dr. Jérôme Clerc,

    1. Institut für Organische und Biomolekulare Chemie, Universität Göttingen, Tammannstrasse 2, 37077 Göttingen (Germany)
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    • These authors contributed equally to this work.

  • Daniel Krahn,

    1. Zentrum für Medizinische Biotechnologie, Fakultät für Biologie, Universität Duisburg-Essen, Universitätsstrasse 2, 45117 Essen (Germany)
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  • David Bier,

    1. Chemical Genomics Centre der Max Planck Gesellschaft, Otto-Hahn-Strasse 15, 44227 Dortmund (Germany)
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  • Tram Ngoc Hong,

    1. Max-Planck-Institut für Pflanzenzüchtungsforschung, Carl-von-Linné-Weg 10, 50829 Köln (Germany)
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  • Dr. Christian Ottmann,

    1. Chemical Genomics Centre der Max Planck Gesellschaft, Otto-Hahn-Strasse 15, 44227 Dortmund (Germany)
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  • Sherry Niessen,

    1. The Center for Physiological Proteomics, The Scripps Research Institute, La Jolla (USA)
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  • Dr. Tom Colby,

    1. Max-Planck-Institut für Pflanzenzüchtungsforschung, Carl-von-Linné-Weg 10, 50829 Köln (Germany)
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  • Dr. Renier A. L. van der Hoorn,

    1. Max-Planck-Institut für Pflanzenzüchtungsforschung, Carl-von-Linné-Weg 10, 50829 Köln (Germany)
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  • Prof. Dr. Markus Kaiser

    Corresponding author
    1. Zentrum für Medizinische Biotechnologie, Fakultät für Biologie, Universität Duisburg-Essen, Universitätsstrasse 2, 45117 Essen (Germany)
    • Zentrum für Medizinische Biotechnologie, Fakultät für Biologie, Universität Duisburg-Essen, Universitätsstrasse 2, 45117 Essen (Germany)
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  • We thank the following people for their help: Diego F. Gomez-Casati for kindly providing the gapC-1 mutant line; Renate Scheibe for providing the GAPC-1 and GAPC-2 overexpression constructs; and Johanna Misas for technical assistance. This research was funded by an ERC starting grant (M.K., grant no. 258413).

Abstract

original image

Exceptionally specific: The natural-product-like structural complexity of a bicyclic hydantoin was exploited to generate the novel, highly specific activity-based profiling probe (ABPP) Mrl-Rh (Rh=rhodamine; see picture) for glyceraldehyde 3-phosphate dehydrogenases. This probe can be used to investigate activity changes of this enzyme class during plant–pathogen interactions.

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