D-serine- and p-fluorophenylalanine-resistant mutants of Physcomitrium patens are defective in amino acid uptake
Abstract
Two amino acid analogue-resistant lines of Physcomitrium (formerly Physcomitrella) patens, DSR8 and PFR4, are resistant to a range of D-amino acids and an inhibitory concentration of L-lysine. Both are defective in the uptake of [35S]-L-methionine. Uptake by the wild-type line is pH-dependent (decreasing with raised external proton concentrations) and is depressed by dinitrophenol and by ammonium ions. We discuss the possible involvement of an active proton-general amino acid antiport pump in the plasma membrane.
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