Inducer-Dependent Nuclear Localization of a Zn(II)2Cys6 Transcriptional Activator, AmyR, in Aspergillus nidulans

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  • MAKITA Tomohiro
    Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University
  • KATSUYAMA Yoko
    Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University
  • TANI Shuji
    Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University
  • SUZUKI Hayato
    Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University
  • KATO Naoki
    Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University
  • TODD Richard B.
    Department of Genetics, University of Melbourne
  • HYNES Michael J.
    Department of Genetics, University of Melbourne
  • TSUKAGOSHI Norihiro
    Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University
  • KATO Masashi
    Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University
  • KOBAYASHI Tetsuo
    Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University

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  • Inducer-dependent nuclear localization of a Zn(2)2Cys6 transcriptional activator, AmyR, in Aspergillus nidulans
  • Inducer-Dependent Nuclear Localization of a Zn(II)<sub>2</sub>Cys<sub>6</sub>Transcriptional Activator, AmyR, in<i>Aspergillus nidulans</i>

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Abstract

AmyR is a Zn(II)2Cys6 transcriptional activator that regulates expression of the amylolytic genes in Aspergillus species. Subcellular localization studies of GFP-fused AmyR in A. nidulans revealed that the fusion protein preferentially localized to the nucleus in response to isomaltose, the physiological inducer of the amylolytic genes. The C-terminal domains of AmyR, designated MH3 (residues 419–496) and MH4 (residues 516–542), were essential for sensing the inducing stimulus and regulating the subcellular localization. The MH2 domain (residues 234–375) located in the middle of AmyR was required for transcriptional activation of the target genes, and the nuclear localization signals were identified within the N-terminal Zn(II)2Cys6 DNA binding motif.

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