Tomato seeds Phosphorylation Label-free Quantitative Proteomic Analysis

Mitogen-activated protein kinases usually affect biological processes by phosphorylating proteins. To further investigate the consequences of MAPK11 interacting with SnRK1 in controlling tomato seed dormancy, we performed a phosphorylation label-free quantitative proteomic assay in vivo with dry seeds of TS-9and MAPK11-OE lines. Data analysis showed that a total of 8261 phosphosites and 6026 phosphopeptides derived from 2711 phosphoproteins were identified. The phosphopeptides with an average fold-change >2 or <0.5 and a P value <0.05 were selected as being significantly different. Among all identified phosphopeptides, 87 phosphopeptides were significantly up-regulated and 83 phosphopeptides were significantly down-regulated in seeds of MAPK11-OE line. In addition, we also found that 348 phosphopeptides were just abundant in MAPK11-OE-13 line, and 221 phosphopeptides merely in TS-9, respectively. To explore potential biological function of MAPK11, we conducted GO function annotation and enrichment, KEGG passway annotation and enrichment, and protein protein interaction network (PPI) analyses, and detected that MAPK11 might have effect on binding, catalytic activity, transporter activity, molecular function regulator and signal transducer; and involved in cellular process, metabolic process, biological regulation, regulation of biological process and response to stimulus