Comparative study of the different mechanisms for zinc ion stress sensing in two cyanobacterial strains, <i>Synechococcus</i> sp. PCC 7942 and <i>Synechocystis</i> sp. PCC 6803

  • Morita Eugene Hayato
    Department of Bioresources, Faculty of Agriculture, Ehime University Venture Business Laboratory, Ehime University
  • Kawamoto Satsuki
    Cell-Free Science and Technology Research Center, Ehime University
  • Abe Shunnosuke
    Department of Bioresources, Faculty of Agriculture, Ehime University
  • Nishiyama Yoshitaka
    Cell-Free Science and Technology Research Center, Ehime University Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University
  • Ikegami Takahisa
    Protein Research Institue, Osaka University
  • Hayashi Hidenori
    Venture Business Laboratory, Ehime University Cell-Free Science and Technology Research Center, Ehime University

Abstract

In response to an increased level of Zn2+, Synechococcus sp. PCC 7942 expresses SmtA, a metallothionein-like metal-chelating protein, while Synechocystis sp. PCC 6803 expresses ZiaA, a transporter of Zn2+. The gene expression of these proteins is regulated by repressor protein, SmtB and ZiaR, respectively. In spite of contributing to different response systems, both repressor proteins belong to the ArsR family and are highly homologous to each other. To understand the different systems responsible for dealing with excess Zn2+, we examined the cis-elements in the promoter regions of smtA and ziaA, as well as the binding affinities of recombinant SmtB and ZiaR proteins. The operator/promoter region of smtA included two palindromic sequences and that of ziaA included one. Electrophoretic mobility shift assay revealed that SmtB formed four different complexes with the operator/promoter region of smtA, whereas it formed only two different complexes with the corresponding region of ziaA. For ZiaR, the corresponding results were quite the same as those for SmtB. Furthermore, the complex formation between SmtB and operator/promoter regions is inhibited in the presence of Zn2+ at higher concentrations than 16 <symbol>m</symbol>M. On the other hand, the corresponding Zn2+ concentration is 128 <symbol>m</symbol>M. These results demonstrate that the degrees of protein-DNA complex formation between repressor proteins and the operator/promoter regions of regulated genes depend on the structures of the operator/promoter regions, and the effects of Zn2+ on the dissociation of these complexes are mainly associated with the structures of the repressors.<br>

Journal

  • BIOPHYSICS

    BIOPHYSICS 8 (0), 103-109, 2012

    The Biophysical Society of Japan

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