ArticleThe Plant cell2026
SlSEC1- and SlSPY-mediated O-glycosylation stabilizes the transcription factor SlNOR to promote tomato fruit ripening.
Article in The Plant cell, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
O-glycosylation is a critical post-translational modification (PTM) that regulates protein function, yet its role in regulating plant transcription factors (TFs) remains poorly understood. Here, we report that O-glycosylation regulates NON-RIPENING (SlNOR), the master NAC TF controlling tomato (Solanum lycopersicum) fruit ripening. Using proteomic and interaction assays, we identified SlNOR as a substrate of 2 conserved nucleocytoplasmic O-glycosyltransferases: the O-GlcNAc transferase SlSEC1 and the O-fucosyltransferase SlSPY. We mapped 3 O-glycosylation sites (Thr93, Thr134, and Ser165) within the NAC domain of SlNOR. Biochemical assays suggested that O-glycosylation protects SlNOR from protein degradation. Accordingly, simultaneous mutagenesis of the 3 O-glycosylation sites reduced SlNOR protein stability and nuclear accumulation. Functionally, O-glycosylated SlNOR exhibited enhanced transcriptional activation of the ethylene biosynthesis genes (SlACS2 and SlACO1), which was corroborated by its increased DNA-binding affinity in electrophoretic mobility shift assays. Genetic evidence from CRISPR/Cas9-generated mutants revealed that loss of SlSEC1 or SlSPY reduces ethylene production and delays ripening, while the Slsec1-1 Slspy double mutant displayed a cooperative ripening delay and severe growth defects. Collectively, our findings uncover a key PTM-based regulatory mechanism in which SlSEC1/SlSPY-mediated O-glycosylation enhances SlNOR stability and transcriptional activity, thereby coupling a master transcriptional regulator to ethylene biosynthesis for the control of fruit ripening.
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