325
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Quantitative mapping of zinc fluxes in the mammalian egg reveals the origin of fertilization-induced zinc sparks

      research-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Fertilization of a mammalian egg induces a series of ‘zinc sparks’ that are necessary for inducing the egg-to-embryo transition. Despite the importance of these zinc efflux events little is known about their origin. To understand the molecular mechanism of the zinc spark we combined four physical approaches to resolve zinc distributions in single cells: a chemical probe for dynamic live-cell fluorescence imaging and a combination of scanning transmission electron microscopy with energy dispersive spectroscopy, X-ray fluorescence microscopy, and 3D elemental tomography for high resolution elemental mapping. We show that the zinc spark arises from a system of thousands of zinc-loaded vesicles, each of which contains, on average, 10 6 zinc atoms. These vesicles undergo dynamic movement during oocyte maturation and exocytosis at the time of fertilization. The discovery of these vesicles and the demonstration that zinc sparks originate from them provides a quantitative framework for understanding how zinc fluxes regulate cellular processes.

          Related collections

          Most cited references63

          • Record: found
          • Abstract: found
          • Article: not found

          Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis.

          Intracellular zinc is thought to be available in a cytosolic pool of free or loosely bound Zn(II) ions in the micromolar to picomolar range. To test this, we determined the mechanism of zinc sensors that control metal uptake or export in Escherichia coli and calibrated their response against the thermodynamically defined free zinc concentration. Whereas the cellular zinc quota is millimolar, free Zn(II) concentrations that trigger transcription of zinc uptake or efflux machinery are femtomolar, or six orders of magnitude less than one atom per cell. This is not consistent with a cytosolic pool of free Zn(II) and suggests an extraordinary intracellular zinc-binding capacity. Thus, cells exert tight control over cytosolic metal concentrations, even for relatively low-toxicity metals such as zinc.
            Bookmark
            • Record: found
            • Abstract: not found
            • Article: not found

            Metals in neurobiology: probing their chemistry and biology with molecular imaging.

              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Zinc biochemistry: from a single zinc enzyme to a key element of life.

              The nutritional essentiality of zinc for the growth of living organisms had been recognized long before zinc biochemistry began with the discovery of zinc in carbonic anhydrase in 1939. Painstaking analytical work then demonstrated the presence of zinc as a catalytic and structural cofactor in a few hundred enzymes. In the 1980s, the field again gained momentum with the new principle of "zinc finger" proteins, in which zinc has structural functions in domains that interact with other biomolecules. Advances in structural biology and a rapid increase in the availability of gene/protein databases now made it possible to predict zinc-binding sites from metal-binding motifs detected in sequences. This procedure resulted in the definition of zinc proteomes and the remarkable estimate that the human genome encodes ∼3000 zinc proteins. More recent developments focus on the regulatory functions of zinc(II) ions in intra- and intercellular information transfer and have tantalizing implications for yet additional functions of zinc in signal transduction and cellular control. At least three dozen proteins homeostatically control the vesicular storage and subcellular distribution of zinc and the concentrations of zinc(II) ions. Novel principles emerge from quantitative investigations on how strongly zinc interacts with proteins and how it is buffered to control the remarkably low cellular and subcellular concentrations of free zinc(II) ions. It is fair to conclude that the impact of zinc for health and disease will be at least as far-reaching as that of iron.
                Bookmark

                Author and article information

                Journal
                101499734
                35773
                Nat Chem
                Nat Chem
                Nature chemistry
                1755-4330
                1755-4349
                20 January 2015
                15 December 2014
                February 2015
                01 August 2015
                : 7
                : 2
                : 130-139
                Affiliations
                [1 ]The Chemistry of Life Processes Institute, Northwestern University, Evanston, IL 60208, USA
                [2 ]Northwestern University Atomic and Nanoscale Characterization Experimental Center, Evanston, IL 60208, USA
                [3 ]Department of Obstetrics and Gynecology, Northwestern University, Feinberg School of Medicine, Chicago, IL 60611, USA
                [4 ]X-ray Science Division, Argonne National Laboratory, Argonne, IL 60439, USA
                [5 ]Department of Chemistry, Northwestern University, Evanston, IL 60208, USA
                [6 ]Department of Materials Science and Engineering, Northwestern University; Evanston, IL 60208, USA
                [7 ]Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA
                Author notes
                Corresponding Authors: Thomas V. O’Halloran, Ph.D., Director, Chemistry of Life Processes Institute, Northwestern University, 2170 North Campus Drive, Silverman 4611, Evanston, IL 60208, Phone: 847-644-9410, Fax: 847-467-1566, t-ohalloran@ 123456northwestern.edu , and, Teresa K. Woodruff, Department of Obstetrics and Gynecology, Northwestern University Feinberg School of Medicine, 303 East Superior Street, Lurie 10-121, Chicago, IL 60611, Phone: 312-503-2503, Fax: 312-503-0219, tkw@ 123456northwestern.edu
                Article
                NIHMS642165
                10.1038/nchem.2133
                4315321
                25615666
                6cc132cc-3a2b-44ed-8377-b9fd445299f9
                History
                Categories
                Article

                Chemistry
                Chemistry

                Comments

                Comment on this article