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Plant and Cell Physiology Advance Access originally published online on October 6, 2009
Plant and Cell Physiology 2009 50(11):1923-1932; doi:10.1093/pcp/pcp136
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© The Author 2009. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Arabidopsis OPT6 is an Oligopeptide Transporter with Exceptionally Broad Substrate Specificity

Sharon Pike1, Ami Patel1,3, Gary Stacey1,2 and Walter Gassmann1,*

1Division of Plant Sciences and Christopher S. Bond Life Sciences Center, 1201 E. Rollins Rd., University of Missouri, Columbia, MO 65211-7310, USA
2Department of Biochemistry, 117 Schweitzer Hall, University of Missouri, Columbia, MO 65211, USA

*Corresponding author: E-mail, gassmannw{at}missouri.edu; Fax: +1-573-884-9676.


  Abstract

Oligopeptide transporters (OPTs) are found in fungi, bacteria and plants. The nine Arabidopsis thaliana OPT genes are expressed mainly in the vasculature and are thought to transport tetra- and pentapeptides, and peptide-like substrates such as glutathione. Expression of AtOPT6 in Xenopus laevis oocytes demonstrated that AtOPT6 transports many tetra- and pentapeptides. In addition, AtOPT6 transported reduced glutathione (GSH), a tripeptide, but not oxidized glutathione (GSSG). Recent data showed that Candida albicans OPTs can transport peptides up to eight amino acids in length. AtOPT6 transported mammalian signaling peptides up to 10 amino acids in length and, in addition, known plant development- and nematode pathogenesis-associated peptides up to 13 amino acids long. AtOPT6 displayed high affinity for penta- and dodecapeptides, but low affinity for GSH. In comparison the Saccharomyces cerevisiae ScOPT1 was incapable of transporting any of the longer peptides tested. These data demonstrate the necessity of experimentally determining substrate specificity of individual OPTs, and lay a foundation for structure/function studies. Characterization of the AtOPT6 substrate range provides a basis for investigating the possible physiological function of AtOPT6 in peptide signaling and thiol transport in response to stress.

Keywords: Arabidopsis - CLE peptides - Membrane transporter - Oocytes - Two-electrode voltage clamp - Xenopus laevis

Abbreviations: ABC, ATP-binding cassette; CLE, CLAVATA3/ENDOSPERM SURROUNDING REGION; {gamma}EC, {gamma}-Glu-Cys; GNOS, S-nitrosoglutathione; GSH, reduced glutathione; GSSG, oxidized glutathione; GUS, β-glucuronidase; Imax, maximal current; K0.5, substrate concentration at half-maximal current; OPT, oligopeptide transporter; PC2, ({gamma}-Glu-Cys)2-Gly (phytochelatin); UTR, untranslated region.

3Present address: Department of Veterinary Pathobiology, 319 Connaway Hall, University of Missouri, Columbia, MO 65211, USA.

(Received July 17, 2009; Accepted September 27, 2009)
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