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PLANT PHYSIOLOGY , Vol 110, Issue 1 171-178, Copyright © 1996 by American Society of Plant Biologists

BIOCHEMISTRY AND ENZYMOLOGY

Cloning of a Second Arabidopsis Peptide Transport Gene

W. Song, H. Y. Steiner, L. Zhang, F. Naider, G. Stacey and J. M. Becker
Department of Microbiology (W.S., H.-Y.S., G.S., J.M.B.) and Center for Legume Research (W.S., G.S.), University of Tennessee, Knoxville, Tennessee 37996-0845

Previously, we reported the isolation of a peptide transport gene designated AtPTR2 from Arabidopsis thaliana by functional complementation of a yeast peptide transport mutant. We now report the isolation of a second peptide transport gene (AtPTR2-B) from Arabidopsis using the same approach. Similar to the effects of transferring AtPTR2-A (previously called AtPTR2), transfer of AtPTR2-B to yeast peptide transport mutants restored the ability to grow on di- and tripeptides but not peptides four residues or longer. However, unlike yeast mutants complemented with either the yeast PTR2 gene or the AtPTR2-A gene, transformants expressing AtPTR2-B were only partially sensitive to toxic peptides. Northern analysis showed that AtPTR2-B was constitutively expressed in all plant organs. Studies of the kinetics indicated that AtPTR2-A and AtPTR2-B have Km values of 47 and 14 [mu]M, respectively, with Vmax values of 0.061 and 0.013 nmol mg-1 cell dry weight s-1, respectively, when dileucine was used as a substrate. AtPTR2-B is encoded on a 2.0-kb cDNA corresponding to a 585-amino acid protein (64.4 kD). Hydropathy analysis indicates that the protein is highly hydrophobic and suggests that there are 12 putative transmembrane segments. AtPTR2-B, like AtPTR2-A, shares significant similarity to a number of other proteins involved in transport of peptides into cells.


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