Plant Molecular Biology

, Volume 40, Issue 1, pp 37-44

First online:

The IRT1 protein from Arabidopsis thaliana is a metal transporter with a broad substrate range

  • Yulia O. KorshunovaAffiliated withDepartment of Biology, Washington University
  • , David EideAffiliated withNutritional Science Program, University of Missouri
  • , W. Gregg ClarkAffiliated withDepartment of Biology, Washington University
  • , Mary Lou GuerinotAffiliated withDepartment of Biological Sciences, Dartmouth College
  • , Himadri B. PakrasiAffiliated withDepartment of Biology, Washington University

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The molecular basis for the transport of manganese across membranes in plant cells is poorly understood. We have found that IRT1, an Arabidopsis thaliana metal ion transporter, can complement a mutant Saccharomyces cerevisiae strain defective in high-affinity manganese uptake (smf1Δ). The IRT1 protein has previously been identified as an iron transporter. The current studies demonstrated that IRT1, when expressed in yeast, can transport manganese as well. This manganese uptake activity was inhibited by cadmium, iron(II) and zinc, suggesting that IRT1 can transport these metals. The IRT1 cDNA also complements a zinc uptake-deficient yeast mutant strain (zrt1zrt2), and IRT1-dependent zinc transport in yeast cells is inhibited by cadmium, copper, cobalt and iron(III). However, IRT1 did not complement a copper uptake-deficient yeast mutant (ctr1), implying that this transporter is not involved in the uptake of copper in plant cells. The expression of IRT1 is enhanced in A. thaliana plants grown under iron deficiency. Under these conditions, there were increased levels of root-associated manganese, zinc and cobalt, suggesting that, in addition to iron, IRT1 mediates uptake of these metals into plant cells. Taken together, these data indicate that the IRT1 protein is a broad-range metal ion transporter in plants.

copper iron manganese metal transport plant root zinc