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Transcript
Secretome profiling of chickpea identifies a leaderless Bet v1-like protein that participates in stress response Vijay Wardhan, Subhra Chakraborty and Niranjan Chakraborty* National Institute of Plant Genome Research, Aruna Asaf Ali Marg, New Delhi 110067, India Secreted proteins maintain cell structure and biogenesis, besides acting in signaling events crucial for cellular homeostasis during stress adaptation. To better understand the underlying mechanism of stress-responsive secretion, the suspension-cultured cells of chickpea were subjected to water-deficit conditions. Cell viability of the suspension culture remained unaltered until 96 h, which gradually declined at later stages of dehydration. Proteomic analysis led to the identification of 215 differentially regulated proteins, involved in multivariate cellular processes that include metabolism, cell defence and signal transduction suggesting their concerted role in stress adaptation. One-third of the secreted proteins displayed no N-terminal secretion signals suggesting a nonclassical secretion route. Screening of the secretome identified a leaderless Bet v 1-like protein, designated CaRRP1, the export of which was inhibited by brefeldin A. We investigated the gene structure and genomic organization, and demonstrated that CaRRP1 may be involved in stress response. The transcript abundance of CaRRP1 was significantly and positively correlated to stresses caused by both abiotic and biotic factors. Functional complementation of CaRRP1 could rescue the growth defects in yeast mutant, deficient in vesicular transport indicating a partial overlap of protein secretion and stress response. Our study provides the most comprehensive analysis of dehydration-responsive plant secretome and the complex metabolic network operating in plant extracellular space.