Posphoproteomics profiling reveals the regulatory role of a phosphorylated protein PvFBA1 in cadmium tolerance in seashore paspalum.

Seashore paspalum (Paspalum vaginatum) is a warm-season and perennial turfgrass and is known for its cadmium (Cd)-stress tolerance. Here, a Phosphoproteomics analysis was performed to examine the key proteins relating to Cd tolerance in seashore paspalum. Fructose 1,6-biphosphate aldolase, PvFBA1, was identified for its phosphorylated state after exposure to Cd stress. Specifically, the phosphorylation of PvFBA1 was enhanced in several metabolic pathways, including pentose phosphate pathway (PPP), carbon fixation and biosynthesis of amino acids under Cd stress. By transforming PvFBA1 into Arabidopsis, the PvFBA1-OE plants exhibited longer roots, greater FBA activity and higher soluble sugar content than WT under 100 µM CdCl ₂ treatment. By expressing the PvFBA1 in yeast, a serine 50 phosphorylation site was identified as functional site. By microscale thermophoresis experiment, we indicted that PvFBA1can bind Cd directly enhancing its phosphorylation level to alleviate the damage of Cd. This finding may provide new insights into the molecular mechanisms of plants Cd tolerance.
Competing Interests: Declaration of Competing Interest The authors declare that they have no conflict of interest.
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