title: Copper economy in Chlamydomonas: prioritized allocation and reallocation of copper to respiration vs. photosynthesis.
abstract: Inorganic elements, although required only in trace amounts, permit life and primary productivity because of their functions in catalysis. Every organism has a minimal requirement of each metal based on the intracellular abundance of proteins that use inorganic cofactors, but elemental sparing mechanisms can reduce this quota. A well-studied copper-sparing mechanism that operates in microalgae faced with copper deficiency is the replacement of the abundant copper protein plastocyanin with a heme-containing substitute, cytochrome (Cyt) c6. This switch, which is dependent on a copper-sensing transcription factor, copper response regulator 1 (CRR1), dramatically reduces the copper quota. We show here that in a situation of marginal copper availability, copper is preferentially allocated from plastocyanin, whose function is dispensable, to other more critical copper-dependent enzymes like Cyt oxidase and a ferroxidase. In the absence of an extracellular source, copper allocation to Cyt oxidase includes CRR1-dependent proteolysis of plastocyanin and quantitative recycling of the copper cofactor from plastocyanin to Cyt oxidase. Transcriptome profiling identifies a gene encoding a Zn-metalloprotease, as a candidate effecting copper recycling. One reason for the retention of genes encoding both plastocyanin and Cyt c6 in algal and cyanobacterial genomes might be because plastocyanin provides a competitive advantage in copper-depleted environments as a ready source of copper.
authors: Department of Chemistry and Biochemistry, and.
authors: Janette
authors: J
authors: Kropat
authors: Department of Chemistry and Biochemistry, and.
authors: Sean D
authors: SD
authors: Gallaher
authors: Department of Chemistry and Biochemistry, and.
authors: Eugen I
authors: EI
authors: Urzica
authors: Department of Chemistry and Biochemistry, and.
authors: Stacie S
authors: SS
authors: Nakamoto
authors: Department of Chemistry and Biochemistry, and.
authors: Daniela
authors: D
authors: Strenkert
authors: Department of Chemistry and Biochemistry, and.
authors: Stephen
authors: S
authors: Tottey
authors: Institute for Integrated Research in Materials, Environments, and Societies, California State University, Long Beach, CA 90840.
authors: Andrew Z
authors: AZ
authors: Mason
authors: Department of Chemistry and Biochemistry, and Institute for Genomics and Proteomics, University of California, Los Angeles, CA 90095; and sabeeha@chem.ucla.edu.
authors: Sabeeha S
authors: SS
authors: Merchant
mesh_terms: D002570:Ceruloplasmin / Q000235:genetics / Q000378:metabolism; D002696:Chlamydomonas / Q000235:genetics / Q000378:metabolism*; D003300:Copper / Q000378:metabolism*; D045365:Cytochromes c6 / Q000235:genetics / Q000378:metabolism; D003576:Electron Transport Complex IV / Q000235:genetics / Q000378:metabolism; D008666:Metalloendopeptidases / Q000235:genetics / Q000378:metabolism; D010101:Oxygen Consumption / Q000502:physiology*; D010788:Photosynthesis / Q000502:physiology*; D010970:Plastocyanin / Q000235:genetics / Q000378:metabolism
chemical_list: D045365:Cytochromes c6; D003300:Copper; D010970:Plastocyanin; D002570:Ceruloplasmin; D003576:Electron Transport Complex IV; D008666:Metalloendopeptidases
keywords: RNA-seq; acclimation; copper homeostasis; copper store; metal
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