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Plant Sci ; 338: 111897, 2024 Jan.
Article En | MEDLINE | ID: mdl-37852415

Due to anthropogenic global warming, droughts are expected to increase and water availability to decrease in the coming decades. For this reason, research is increasingly focused on developing plant varieties and crop cultivars with reduced water consumption. Transpiration occurs through stomatal pores, resulting in water loss. Potassium plays a significant role in stomatal regulation. KAT1 is an inward-rectifying potassium channel that contributes to stomatal opening. Using a yeast high-throughput screening of an Arabidopsis cDNA library, MEE31 was found to physically interact with KAT1. MEE31 was initially identified in a screen for mutants with delayed embryonic development. The gene encodes a conserved phosphomannose isomerase (PMI). We report here that MEE31 interacts with and increases KAT1 activity in yeast and this interaction was also confirmed in plants. In addition, MEE31 complements the function of the yeast homologue, whereas the truncated version recovered in the screening does not, thus uncoupling the enzymatic activity from KAT1 regulation. We show that MEE31 overexpression leads to increased stomatal opening in Arabidopsis transgenic lines. Our data suggest that MEE31 is a moonlighting protein involved in both GDP-D-mannose biosynthesis and KAT1 regulation.


Arabidopsis Proteins , Arabidopsis , Mannose-6-Phosphate Isomerase , Potassium Channels, Inwardly Rectifying , Arabidopsis/metabolism , Arabidopsis Proteins/genetics , Arabidopsis Proteins/metabolism , Mannose/metabolism , Plant Proteins/metabolism , Potassium Channels, Inwardly Rectifying/genetics , Potassium Channels, Inwardly Rectifying/metabolism , Saccharomyces cerevisiae/genetics , Saccharomyces cerevisiae/metabolism , Water/metabolism , Mannose-6-Phosphate Isomerase/metabolism
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