RESUMO
Chlorophylls are the major pigments that harvest light energy during photosynthesis in plants. Although reactions in chlorophyll biogenesis have been largely known, little attention has been paid to the post-translational regulation mechanism of this process. In this study, we found that four lysine sites (K128/340/350/390) of NADPH:protochlorophyllide oxidoreductase A (PORA), which catalyzes the only light-triggered step in chlorophyll biosynthesis, were acetylated after dark-grown seedlings transferred to light via acetylomics analysis. Etiolated seedlings with K390 mutation of PORA had a lower greening rate and decreased PORA acetylation after illumination. Importantly, K390 of PORA was found extremely conserved in plants and cyanobacteria via bioinformatics analysis. We further demonstrated that the acetylation level of PORA was increased by exposing the dark-grown seedlings to the histone deacetylase (HDAC) inhibitor TSA. Thus, the HDACs probably regulate the acetylation of PORA, thereby controlling this non-histone substrate to catalyze the reduction of Pchlide to produce chlorophyllide, which provides a novel regulatory mechanism by which the plant actively tunes chlorophyll biosynthesis during the conversion from skotomorphogenesis to photomorphogenesis.
