Na2CO3-responsive phosphoproteins in chloroplasts from Puccinellia tenuiflora leaves

ABSTRACT: Alkali-salinity exerts severe osmotic, ionic, and high-pH stresses to plants. Photosynthetic machinery is especially sensitive to saline-alkali stress. In addition, reversible protein phosphorylation also play crucial roles in plant salt resistance. While our knowledge on protein phosphorylation events in salt stress response is very limited. Few studies have been published involving photosynthetic protein phosphorylation modulation to improve salt resistance. In the present study, we investigated the Na2CO3-responsive characteristics in Puccinellia tenuiflora chloroplasts using stable isotope dimethyl labeled phosphoproteomic approach. A total of 161 unique phosphopeptides were identified, and 137 phosphopeptides were quantified by dimethyl labeling. Among them, 50 proteins were quantified as Na2CO3-responsive proteins with 57 phosphosites, including 33 increased and 14 decreased. Importantly, 26 phosphosites were newly identified as Na2CO3-responsive phosphoproteins in plants, which were supposed to be crucial for regulating photosynthesis, membrane and transporting, signaling, stress response, and protein synthesis and turnover. Among them, seven light harvesting proteins, six PSII proteins, five PSI proteins, three electron transfer chain proteins, and two Calvin cycle-related proteins were increased, but five ATP synthase subunits and sucrose-phosphate synthase were decreased at phosphorylation level. Besides, Na+/H+ antiporter, villin-2, and two thylakoid organization related proteins were increased at phosphorylation level. Two signaling related proteins and most protein species in charge of gene expression and protein turnover were enhanced at phosphorylation level at 24h after Na2CO3 treatment.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Oryza Sativa (rice)

TISSUE(S): Plant Cell, Shoot

SUBMITTER: Shaojun Dai  

LAB HEAD: Shaojun Dai

PROVIDER: PXD005472 | Pride | 2021-08-30

REPOSITORIES: pride