A twin histidine motif is the core structure for high-affinity substrate selection in plant ammonium transporters.

ABSTRACT: Ammonium transporters (AMT), methylamine permeases (Mep), and the more distantly related rhesus factors (Rh) are trimeric membrane proteins present in all domains of life. AMT/Mep/Rhs are highly selective membrane proteins required for ammonium uptake or release, and they efficiently exclude the similarly sized K⁺ ion. Previously reported crystal structures have revealed that each transporter subunit contains a unique hydrophobic but occluded central pore, but it is unclear whether the base (NH₃) or NH₃ coupled with an H⁺ are transported. Here, using expression of two plant AMTs (AtAMT1;2 and AMT2) in budding yeast, we found that systematic replacements in the conserved twin-histidine motif, a hallmark of most AMT/Mep/Rh, alter substrate recognit

SUBMITTER: Ganz P 

PROVIDER: S-EPMC7062152 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature