PHOTOMORPHOGENESIS REGULATION BY PROTEIN PHOSPHORYLATION

ARICO DENISE; LUCIANA CASTRO; WENGIER DIEGO; FOX ANA ROMINA, FRANCESCO SPINELLI , MUSCHIETTI JORGE, MATTEI BENEDETTA, MAZZELLA MARIA AGUSTINA

CABA

Congreso; Reunión conjunta de sociedades de biociencias; 2017

Light environment provides signals for plants to develop and accomplish their life cycle successfully. Those signals are perceived and transduced by photoreceptors. Phosphorylation is one of the biochemical mechanisms initiating light signalling cascade and is a challenging question in the photobiology field today. Here, we study early light-induced phosphoproteome in Arabidopsis thaliana through a Label free LC-MS/MS proteomic approach to identify proteins which significantly change their phosphorylation status in a light-responsive way. Total proteins were extracted from three treatments: 5-d-old etiolated WT seedlings (WTD); 5-d-old etiolated WT (WTL) and phyA phyB cry1 cry2 quadruple mutant (TETL) seedlings exposed for 20 min to white light pulse (100 µmol.m-2.s-1) just before harvest. Lyophilized samples were sent to Department of Proteomiqué, University of Laval, Québec, Canada; where phosphopeptide enrichment was performed. Two comparisons were studied: (1) WTD vs WTL, and (2) WTL vs TETL. The first one (1) identifies peptides which change their phosphorylation status in response to the light treatment. Over these phosphopeptides it was done the second comparison (2) that reveals phosphorylation dependency.