Characterisation of the unknown gene and the corresponding protein At3g29075 in <em>Arabidopsis thaliana</em>

Abstract

Phospholipases D (PLDs) are involved in different plant stress responses, exclusively to abiotic stresses like cold, salinity, and drought. The PLD enzymes catalyse the hydrolysis of membrane phospholipids into phosphatidic acid (PA) and a free head group. PA is a membranous second-messenger molecule that is involved in various stress-dependent signal transduction pathways. Earlier, an unknown protein PLDrp1 recognised as a putative target protein downstream of the PLD α1 signalling pathway. The substantial dependence of this protein from PLD α1 could be diminished under water stress conditions, raising the question about the mechanisms involved in this observation. Interestingly, the homolog of PLDrp1 with a 60% sequence similarity At3g29075 protein was identified in <em>A. thaliana</em>. To characterise unknown protein, At3g29075 was the main motive of this study.<br /> This study exhibits that the At3g29075 protein is a class V glycine-rich protein, with more than 21.1% lysine residues. The C-terminal end of the unknown protein At3g29075 has no similar protein or motif in the whole protein database. The protein localisation has confirmed to the cytosol and nucleus. Dehydration stress induces the expression of At3g29075. Wild Type and mutant plants were grown and phenotypically monitored upon standard growth conditions to define the protein’s function. The overexpression lines of AT3G29075 showed early flowering compared to the wild type, and at3g29075 knockdown mutant.