Characterization of the Nuclear- and Plastid-Encoded secA-Homologous Genes in the Unicellular Red Alga Cyanidioschyzon merolae

  • KOYAMA Yosuke
    Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University
  • TAKIMOTO Koji
    Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University
  • KOJIMA Asuka
    Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University
  • ASAI Kei
    Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University
  • MATSUOKA Satoshi
    Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University
  • MITSUI Toshiaki
    Graduate School of Science and Technology, Niigata University
  • MATSUMOTO Kouji
    Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University
  • HARA Hiroshi
    Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University
  • OHTA Niji
    Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University

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  • Characterization of the Nuclear- and Plastid-Encoded<i>secA</i>-Homologous Genes in the Unicellular Red Alga<i>Cyanidioschyzon merolae</i>

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Abstract

SecA is an ATP-driven motor for protein translocation in bacteria and plants. Mycobacteria and listeria were recently found to possess two functionally distinct secA genes. In this study, we found that Cyanidioschyzon merolae, a unicellular red alga, possessed two distinct secA-homologous genes; one encoded in the cell nucleus and the other in the plastid genome. We found that the plastid-encoded SecA homolog showed significant ATPase activity at low temperature, and that the ATPase activity of the nuclear-encoded SecA homolog showed significant activity at high temperature. We propose that the two SecA homologs play different roles in protein translocation.

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