Labeling and enrichment of Arabidopsis thaliana matrix metalloproteases using an active-site directed, marimastat-based photoreactive probe |
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| Authors: | Lenger Janina Kaschani Farnusch Lenz Thomas Dalhoff Christian Villamor Joji Grace Köster Hubert Sewald Norbert van der Hoorn Renier A L |
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| Affiliation: | 1. Bioorganic and Organic Chemistry, Department of Chemistry, Bielefeld University, Universitätsstr. 25, 33615 Bielefeld, Germany;2. Plant Chemetics Lab, Chemical Genomics Centre of the Max Planck Society, Max-Planck-Institute for Plant Breeding Research, Carl-von-Linné-Weg 10, 50829 Cologne, Germany;3. caprotec bioanalytics GmbH, Volmerstrasse 5, 12489 Berlin, Germany;1. Universiteit Leiden, Leiden Inst. of Chemistry, Postbus 9502, Leiden, 2300 RA, Netherlands |
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| Abstract: | Matrix metalloproteases (MMPs) are secreted or membrane-bound zinc-containing proteases that play diverse roles in development and immunity in plants and in tissue remodeling in animals. We developed a photoreactive probe based on the MMP inhibitor marimastat, conjugated to a 4-azidotetrafluorobenzoyl moiety as photoreactive group and biotin as detection or sorting function. The probe labels At2-MMP, At4-MMP, At5-MMP, and likely other plant MMPs in leaf extracts, as shown by transient At-MMP expression in Nicotiana benthamiana, protein blot, and LC-MS/MS analysis. This MMP probe is a valuable tool to study the post-translational status of MMPs during plant immunity and other MMP-regulated processes. |
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