The goal of this study was to detect and quantify the presence of transgenic proteins in transformed A. thaliana plants and overall gene expression responses to presence of IPD3. Experimental plants were transformed with 3 versions of the gene Interacting Protein of DMI3 (IPD3), a transcription factor necessary for mycorrhizal symbiosis, derived from Medicago truncatula. Col-0 ecotype plants not transformed with any gene are labeled “WT.” Plants expressing the sequence of Medicago truncatula IPD3 with removal of introns but no coding sequence modifications are labeled “MtIPD3”. Plants expressing the coding sequence of IPD3 with an alteration causing a serine at position 50 to be replaced by aspartic acid, which results in consitutive activation via phosphomimicking, are labeled “S50DIPD3 .” Plants transformed with a truncated version of IPD3 consisting solely of the C-terminal DNA-binding domain found from aa 254-513, which has constitutively active DNA-binding activity, are labeled “IPD3-Min.” For shotgun proteomics, five biological replicates were included for each treatment. For targeted proteomics, one biological replicate was included for each treatment. Whole root or shoot tissue from plants grown for 5 weeks on ½ strength MS medium was harvested and immediately flash frozen with liquid nitrogen. This tissue was stored at -80ºC until it was ground to a fine powder under liquid nitrogen. The tissue was then weighed into 200 mg aliquots. Amino acid sequences of the respecitive transgenic proteins were used as a reference and “Wt” control plants were used as a negative control.