Abstract
Synthetic modulators for plant 14-3-3s are promising chemical tools both for understanding the 14-3-3-related signaling pathways and controlling plant physiology. Here, we describe a novel small-molecule inhibitor for 14-3-3 proteins ofArabidopsisthaliana. The inhibitor was identified fromunexpected productsin DMSO stock solution of an in-house chemical library. Mass spectroscopy, mutant-based analyses,fluorescence polarization assays, and thermal shift assaysrevealed that the inhibitor covalently binds to an allosteric site of 14-3-3 with isoform selectivity. Moreover, infiltration of the inhibitor toArabidopsisleaves suppressed the stomatal aperture. The inhibitorshould provide a new insight into the design of potent and isoform-selective 14-3-3 modulators.
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