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Plant Physiol, December 2002, Vol. 130, pp. 2039-2048
The Involvement of a Multicopper Oxidase in Iron Uptake by
the Green Algae Chlamydomonas
reinhardtii1
Alexandra
Herbik,
Christian
Bölling, and
Thomas J.
Buckhout*
Applied Botany, Humboldt University Berlin, Invalidenstrasse 42, 10115 Berlin, Germany
In the unicellular green algae Chlamydomonas
reinhardtii, high-affinity uptake of iron (Fe) requires an
Fe3+-chelate reductase and an Fe transporter. Neither of
these proteins nor their corresponding genes have been isolated. We
previously identified, by analysis of differentially expressed plasma
membrane proteins, an approximately 150-kD protein whose synthesis was induced under conditions of Fe-deficient growth. Based on homology of
internal peptide sequences to the multicopper oxidase hephaestin, this
protein was proposed to be a ferroxidase. A nucleotide sequence to the
full-length cDNA clone for this ferroxidase-like protein has been
obtained. Analysis of the primary amino acid sequence revealed a
putative transmembrane domain near the amino terminus of the protein
and signature sequences for two multicopper oxidase I motifs and one
multicopper oxidase II motif. The ferroxidase-like gene was transcribed
under conditions of Fe deficiency. Consistent with the role of a copper
(Cu)-containing protein in Fe homeostasis, growth of cells in
Cu-depleted media eliminated high-affinity Fe uptake, and Cu-deficient
cells that were grown in optimal Fe showed greatly reduced Fe
accumulation compared with control, Cu-sufficient cells. Reapplication
of Cu resulted in the recovery of Fe transport activity. Together,
these results were consistent with the participation of a ferroxidase
in high-affinity Fe uptake in C. reinhardtii.
1
This work was supported by the Deutsche
Forschungsgemeinschaft (grant to T.J.B.).
*
Corresponding author; e-mail h1131dqy{at}rz.hu-berlin.de, fax
49-30-20938725.
© 2002 American Society of Plant Biologists
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