{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kropat J"],"funding":["HHS | National Institutes of Health","NIGMS NIH HHS"],"pagination":["2644-51"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4352834"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["112(9)"],"pubmed_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."],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Copper economy in Chlamydomonas: prioritized allocation and reallocation of copper to respiration vs. photosynthesis."],"pmcid":["PMC4352834"],"funding_grant_id":["R01 GM042143","R37 GM042143","GM42143"],"pubmed_authors":["Gallaher SD","Kropat J","Tottey S","Urzica EI","Mason AZ","Merchant SS","Strenkert D","Nakamoto SS"],"additional_accession":[]},"is_claimable":false,"name":"Copper economy in Chlamydomonas: prioritized allocation and reallocation of copper to respiration vs. photosynthesis.","description":"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.","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Mar","modification":"2024-11-21T00:34:31.279Z","creation":"2019-03-27T01:47:47Z"},"accession":"S-EPMC4352834","cross_references":{"pubmed":["25646490"],"doi":["10.1073/pnas.1422492112"]}}