SUMO E3 Ligase SIZ1 stabilizes MYB75 to regulate anthocyanin accumulation under high light conditions in Arabidopsis

Sumoylation is one of post-translational modification (PTM) in which SUMO (small ubiquitin-like modifier) are covalently conjugated to protein substrates through a range of biochemical steps. This paper presents evidence that SUMO E3 ligase SIZ1 positively regulates anthocyanin accumulation. Loss-of-function siz1 mutant seedlings exhibit anthocyanin accumulation-reduced phenotype under high light conditions. Moreover, SIZ1 interacts and sumoylates MYB75/PAP1, a key transcription factor in anthocyanin accumulation. Loss-of-function siz1 or K246R substitution in MYB75 blocked SIZ1-mediated sumoylation in vitro and in vivo. Anthocyanin accumulation in mutant myb75-c can not be rescued by expressing MYB75^K246R, but expression of wild-type MYB75^WT complements the mutant phenotype. It suggested that sumoylation is important for MYB75 function. We further prove that sumoylation is essential for MYB75 protein stability. And SIZ1 is involved in the light-induced accumulation of anthocyanins. Our findings reveal an important role for sumoylation of MYB in regulation of anthocyanin accumulation in plants.