TpIRT1 from Polish wheat (Triticum polonicum L.) enhances the accumulation of Fe, Mn, Co, and Cd in Arabidopsis

• TpIRT1A and TpIRTTB have different expression level in different tissues. • Both TpIRT1A and TpIRTTB locate at plasma memenbrane and internal organelle. • The expression of TpIRT1A and TpIRTTB increase the sensitivity of yeast mutants under Co and Cd stresses. • The over-expression of TpIRT1B in A. thaliana increased Fe, Mn, Co, and Cd concentration. • Four distinct amino acid residues in TdiIRT1B ( T. dicoccum ) and TtuIRT1B ( T. turgidum ) potentially bind to Zn or Co. Uptake and internal transport of micronutrients are essential for plant growth, development, and yield. In this regard, Iron Regulated Transporters (IRTs) from the Zinc Regulated Transporter (ZRT)/IRT-related protein (ZIP) family play an important role in transition metal uptake. Most studies have been focused on IRT1-like proteins in diploid species. Information on IRT1-like proteins in polyploids is limited. Here, we studied the function of TpIRT1A and TpIRT1B homoeologs in a tetraploid crop, Polish wheat ( Triticum polonicum L.). Our results highlighted the importance of TpIRT1 in mediating the uptake and translocation of Fe, Mn, Co, and Cd with direct implications for wheat yield potential. Both TpIRT1A and TpIRT1B were located at the plasma membrane and internal vesicle-like organelle in protoplasts of Arabidopsis thaliana L. and increased Cd and Co sensitivity in yeast. The over-expression of TpIRT1B in A. thaliana increased Fe, Mn, Co, and Cd concentration in its tissues and improved plant growth under Fe, Mn, and Co deficiencies, while increased the sensitivity to Cd compared to wild type. Functional analysis of IRT1 homoeologs from tetraploid and diploid ancestral wheat species in yeast disclosed four distinct amino acid residues in TdiIRT1B ( T. dicoccum L. (Schrank)) and TtuIRT1B ( T. turgidum L.). Together, our results increase the knowledge of IRT1 function in a globally important crop, wheat.