Increased phosphate transport of Arabidopsis thaliana Pht1;1 by site‐directed mutagenesis of tyrosine 312 may be attributed to the disruption of homomeric interactions

• DOI: 10.1111/pce.12522
• Publication Date: 2015-03-06T00:48:56Z
• Authors: Elena B. Fontenot; Sandra Feuer Ditusa; Naohiro Kato; Danielle M. Olivier; Renee Dale; Wei‐Yi Lin; Tzyy‐Jen Chiou; Megan A. Macnaughtan; Aaron P. Smith
• Keywords: Homomeric; Heterologous expression

Members of the Pht1 family plant phosphate (Pi) transporters play vital roles in Pi acquisition from soil and planta translocation to maintain optimal growth development. The study specificities biochemical properties will contribute improving current understanding phosphorus homeostasis use-efficiency. In this study, we show through split vivo interaction methods vitro analysis microsomal root tissues that Arabidopsis thaliana Pht1;1 Pht1;4 form homomeric heteromeric complexes. Transient heterologous expression variants, Pht1;1(Y312D), Pht1;1(Y312A) Pht1;1(Y312F), was used analyse role a putative binding residue (Tyr 312) transporter oligomerization function. among proteins disrupted by mutation Tyr 312 Asp, but not Ala or Phe. addition, Pht1;1(Y312D) variant conferred enhanced transport when expressed yeast cells. contrast, Phe did affect kinetics. Our demonstrates modifications higher-order structure affects transport, suggesting may serve as regulatory mechanism for modulating uptake.