publication . Article . 2014

Subcellular metal imaging identifies dynamic sites of Cu accumulation in Chlamydomonas.

Anne Hong-Hermesdorf; Marcus Miethke; Sean D. Gallaher; Janette Kropat; Sheel C. Dodani; Jefferson Y. Chan; Dulmini Barupala; Dylan W. Domaille; Dyna I. Shirasaki; Joseph A. Loo; ...
Open Access
  • Published: 26 Oct 2014
  • Publisher: eScholarship, University of California
  • Country: United States
We identified a Cu-accumulating structure with a dynamic role in intracellular Cu homeostasis. During Zn limitation, Chlamydomonas reinhardtii hyperaccumulates Cu, a process dependent on the nutritional Cu sensor CRR1, but it is functionally Cu deficient. Visualization of intracellular Cu revealed major Cu accumulation sites coincident with electron-dense structures that stained positive for low pH and polyphosphate, suggesting that they are lysosome-related organelles. Nano-secondary ion MS showed colocalization of Ca and Cu, and X-ray absorption spectroscopy was consistent with Cu(+) accumulation in an ordered structure. Zn resupply restored Cu homeostasis con...
Persistent Identifiers
free text keywords: Lysosomes, Chlamydomonas reinhardtii, Polyphosphates, Cations, Divalent, Copper, Zinc, Isotopes, Plastocyanin, Transcription Factors, Gene Expression Profiling, Isotope Labeling, Homeostasis, Hydrogen-Ion Concentration, Molecular Imaging, Transcriptome, Biochemistry & Molecular Biology, Medicinal and Biomolecular Chemistry, Biochemistry and Cell Biology, Cell Biology, Molecular Biology, Article, Bioinorganic chemistry, Chemistry, Plastocyanin, Intracellular, Divalent, chemistry.chemical_classification, Zinc, chemistry.chemical_element, Chlamydomonas, biology.organism_classification, biology, Polyphosphate, chemistry.chemical_compound, Biophysics, Inorganic chemistry, Chlamydomonas reinhardtii
Funded by
NIH| Detroit Cardiovascular Training Program
  • Funder: National Institutes of Health (NIH)
  • Project Code: 5T32HL120822-02
56 references, page 1 of 4

Andreini, C, Bertini, I, Cavallaro, G, Holliday, GL, Thornton, JM. Metal ions in biological catalysis: from enzyme databases to general principles. J Biol Inorg Chem. 2008; 13: 1205-18 [OpenAIRE] [PubMed]

Irving, H, Williams, RJP. The stability of transition-metal complexes. J Chem Soc. 1953; 637: 3192-3210

Dudev, T, Lim, C. Metal binding affinity and selectivity in metalloproteins: insights from computational studies. Annu Rev Biophys. 2008; 37: 97-116 [PubMed]

Waldron, KJ, Rutherford, JC, Ford, D, Robinson, NJ. Metalloproteins and metal sensing. Nature. 2009; 460: 823-30 [PubMed]

Rae, TD, Schmidt, PJ, Pufahl, RA, Culotta, VC, O’Halloran, TV. Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science. 1999; 284: 805-8 [OpenAIRE] [PubMed]

Valentine, JS, Gralla, EB. Delivering Copper Inside Yeast and Human Cells. Science (80-). 1997; 278: 817-818

Tottey, S. Protein-folding location can regulate manganese-binding versus copper- or zinc-binding. Nature. 2008; 455: 1138-42 [PubMed]

Waldron, KJ, Robinson, NJ. How do bacterial cells ensure that metalloproteins get the correct metal?. Nat Rev Microbiol. 2009; 7: 25-35 [PubMed]

Boal, AK, Rosenzweig, AC. Structural biology of copper trafficking. Chem Rev. 2009; 109: 4760-79 [OpenAIRE] [PubMed]

Foster, AW, Robinson, NJ. Promiscuity and preferences of metallothioneins: the cell rules. BMC Biol. 2011; 9: 25 [OpenAIRE] [PubMed]

Merchant, SS. Between a rock and a hard place: trace element nutrition in Chlamydomonas. Biochim Biophys Acta. 2006; 1763: 578-94 [PubMed]

Page, MD, Kropat, J, Hamel, PP, Merchant, SS. Two Chlamydomonas CTR copper transporters with a novel cys-met motif are localized to the plasma membrane and function in copper assimilation. Plant Cell. 2009; 21: 928-43 [OpenAIRE] [PubMed]

Merchant, S, Bogorad, L. Metal ion regulated gene expression: use of a plastocyanin-less mutant of Chlamydomonas reinhardtii to study the Cu(II)-dependent expression of cytochrome c-552. EMBO J. 1987; 6: 2531-5 [OpenAIRE] [PubMed]

Merchant, S, Hill, K, Howe, G. Dynamic interplay between two copper-titrating components in the transcriptional regulation of cyt c6. EMBO J. 1991; 10: 1383-9 [OpenAIRE] [PubMed]

Kropat, J. A regulator of nutritional copper signaling in Chlamydomonas is an SBP domain protein that recognizes the GTAC core of copper response element. Proc Natl Acad Sci U S A. 2005; 102: 18730-18735 [OpenAIRE] [PubMed]

56 references, page 1 of 4
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