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THE PLANT CELL, Vol 6, Issue 9 1289-1299, Copyright © 1994 by American Society of Plant Biologists
An Arabidopsis Peptide Transporter Is a Member of a New Class of Membrane Transport Proteins
H. Y. Steiner, W. Song, L. Zhang, F. Naider, J. M. Becker and G. Stacey
Department of Microbiology, University of Tennessee, Knoxville, Tennessee 37996-0845
An Arabidopsis peptide transport gene was cloned from an Arabidopsis cDNA
library by functionally complementing a yeast peptide transport mutant. The
Arabidopsis plant peptide transporter (AtPTR2) allowed growth of yeast
cells on dipeptides and tripeptides but not peptides four residues and
higher. The plant peptide transporter also conferred sensitivity to a
number of ethionine-containing, toxic peptides of chain length three or
less and restored the ability to take up radiolabeled dileucine at levels
similar to that of the wild type. Dileucine uptake was reduced by the
addition of a variety of growth-promoting peptides. The sequence of a cDNA
insert of 2.8 kb indicated an open reading frame encoding a 610-amino acid
polypeptide (67.5 kD). Hydropathy analysis predicted a highly hydrophobic
protein with a number of potential transmembrane segments. At the amino
acid level, the Arabidopsis plant peptide transporter shows 24.6, 28.5, and
45.2% identity to the Arabidopsis nitrate-inducible nitrate transporter
(CHL1), the rabbit small intestine oligopeptide transporter (PepT1), and
the yeast peptide transporter (Ptr2p), respectively, but little identity to
other proteins known to be involved in peptide transport. Root growth of
Arabidopsis seedlings exposed to ethionine-containing toxic peptides was
inhibited, and growth was restored by the addition of certain peptides
shown to compete with dileucine uptake in yeast expressing the Arabidopsis
transport gene. Consistent with the observed inhibition of root growth by
toxic peptides, the peptide transporter is expressed in the roots of
Arabidopsis seedlings. This study represents the characterization of a
plant peptide transporter that is a member of a new class of related
membrane transport proteins.
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