Phosphoproteome analysis of petunia corolla treated with ethylene and air

ABSTRACT: Senescence represents the last stage of flower development. Phosphorylation is one of the key post-translational modifications that regulate protein functions in diverse biological pathways and contexts. Generally, kinases may be more required than phosphatases during plant growth and development. However, little is known about global phosphorylation change during flower senescence. In this work, we quantitatively investigated the petunia phosphoproteome following ethylene or air treatment. In total, 2170 phosphosites in 1184 protein groups were identified, among which 2059 sites in 1124 proteins were quantified. Treatment with ethylene resulted in 711 down-regulated and only 117 up-regulated phosphosites using a 1.5-fold threshold (P<0.05), showing that ethylene negatively regulates global phosphorylation levels and that phosphorylation of lots of proteins was not necessary during flower senescence. Our results show that protein dephosphorylation may play an important role of in ethylene-induced corolla senescence in petunia and that phosphatases may be more required than kinases during flower senescence. In addition, our results show that ethylene regulates ethylene and ABA signaling transduction pathways via phosphorylation level, and plant mRNA splicing machinery was a major target of ethylene-induced dephosphorylation. Moreover, ethylene treatment increases the number of alternative splicing of precursor RNAs in petunia corollas.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Petunia Hybrida (petunia)

TISSUE(S): Corolla

SUBMITTER: Yixun Yu  

LAB HEAD: Yixun Yu

PROVIDER: PXD005599 | Pride | 2022-02-15

REPOSITORIES: Pride