Zn deficiency disrupts Cu and S homeostasis in Chlamydomonas resulting in over accumulation of Cu and Cysteine

Author:

Strenkert Daniela12ORCID,Schmollinger Stefan12,Hu Yuntao3,Hofmann Christian4,Holbrook Kristen2,Liu Helen W15,Purvine Samuel O6,Nicora Carrie D7,Chen Si8ORCID,Lipton Mary S6,Northen Trent R39,Clemens Stephan4ORCID,Merchant Sabeeha S123510

Affiliation:

1. California Institute for Quantitative Biosciences, University of California , Berkeley, CA , 94720, USA

2. Department of Chemistry and Biochemistry, University of California , Los Angeles, CA 90095, USA

3. Environmental Genomics and Systems Biology, Lawrence Berkeley National Laboratory Berkeley CA USA

4. Department of Plant Physiology, University of Bayreuth , Germany

5. Department of Plant and Microbial Biology, University of California , Berkeley, CA , 94720, USA

6. Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, US Department of Energy , Richland, WA 99352, USA

7. Biological Sciences Division, Pacific Northwest National Laboratory, US Department of Energy , Richland, WA 99352, USA

8. Advanced Photon Source, Argonne National Laboratory , Lemont, IL 60439, USA

9. Joint Genome Institute, Lawrence Berkeley National Laboratory , Berkeley CA USA

10. Department of Molecular & Cell Biology, University of California , Berkeley, CA , 94720, USA

Abstract

AbstractGrowth of Chlamydomonas reinhardtii in zinc (Zn) limited medium leads to disruption of copper (Cu) homeostasis, resulting in up to 40-fold Cu over-accumulation relative to its typical Cu quota. We show that Chlamydomonas controls its Cu quota by balancing Cu import and export, which is disrupted in a Zn deficient cell, thus establishing a mechanistic connection between Cu and Zn homeostasis. Transcriptomics, proteomics and elemental profiling revealed that Zn-limited Chlamydomonas cells up-regulate a subset of genes encoding “first responder” proteins involved in sulfur (S) assimilation and consequently accumulate more intracellular S, which is incorporated into L-cysteine, γ-glutamylcysteine, and homocysteine. Most prominently, in the absence of Zn, free L-cysteine is increased ∼80-fold, corresponding to ∼2.8 × 109 molecules/cell. Interestingly, classic S-containing metal binding ligands like glutathione and phytochelatins do not increase. X-ray fluorescence microscopy showed foci of S accumulation in Zn-limited cells that co-localize with Cu, phosphorus and calcium, consistent with Cu-thiol complexes in the acidocalcisome, the site of Cu(I) accumulation. Notably, cells that have been previously starved for Cu do not accumulate S or Cys, causally connecting cysteine synthesis with Cu accumulation. We suggest that cysteine is an in vivo Cu(I) ligand, perhaps ancestral, that buffers cytosolic Cu.

Funder

National Institutes of Health

Publisher

Oxford University Press (OUP)

Subject

Metals and Alloys,Biochemistry,Biomaterials,Biophysics,Chemistry (miscellaneous)

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