Divalent metal transport in the green microalga Chlamydomonas reinhardtii is mediated by a protein similar to prokaryotic Nramp homologues.

Information about the molecular mechanisms of metal transport in algae is scarce, despite the significant status these organisms have in aquatic ecosystems. In the present study, we describe the cloning and functional characterization of a divalent metal transporter (named DMT1) in the green microalga Chlamydomonas reinhardtii Dangeard. The longest open reading frame of the cloned DMT1 cDNA encodes a protein of 513 amino acids with 11 putative transmembrane domains. The protein belongs to the Nramp family of divalent metal transporters and shows surprisingly higher similarity to some prokaryotic than to eukaryotic polypeptides. Especially the N-terminus, which is longer than of every other homologue considered in this study, displays--uniquely among selected eukaryotic Nramps--exclusively prokaryotic characteristics. Functional complementation experiments in yeast strains with impaired metal transport systems, revealed that C. reinhardtii DMT1 has a broad specificity, acting in the transport of several divalent metals (manganese, iron, cadmium, copper), but excluding zinc.