CYO1/ABC2 protein, a cotyledon-specific chloroplast development factor of Arabidopsis, had thiol-disulfide reduction activity

DOI
  • Shimada Hiroshi
    Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
  • Ogura Kan
    Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
  • Mochizuki Mariko
    Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
  • Mori Kazuaki
    Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
  • Shirano Yumiko
    Boyce Thompson Institute for Plant Research
  • Shibata Daisuke
    Kazusa DNA Research Institute
  • Takamiya Ken-ichiro
    Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology

Bibliographic Information

Other Title
  • 子葉葉緑体形成因子CYO1/ABC2は茎頂分裂組織形成に必須な分子シャペロンである。

Abstract

Chloroplast development in cotyledons differs in a number of ways from that in true leaves, but the cotyledon-specific program of chloroplast biogenesis has not been clarified. The cyo1/abc2 mutant in Arabidopsis thaliana has albino cotyledons but normal green true leaves. Chloroplasts develop abnormally in cyo1/abc2 mutant plants grown in the light, but etioplasts are normal in mutants grown in the dark. CYO1/ABC2 protein localizes to the thylakoid membrane in chloroplasts, and CYO1/ABC2 protein copurified with the PSI/LHCI and PSII/LHCII complexes. CYO1/ABC2 has a C4-type zinc finger domain similar to that of Escherichia coli DnaJ. Recombinant CYO1 accelerates disulfide bond reduction in the model substrate insulin and renatures RNase A, indicating that CYO1/ABC2 has protein disulfide isomerase activity. These results suggest that CYO1/ABC2 has a chaperone-like activity required for thylakoid biogenesis in cotyledons.

Journal

Details 詳細情報について

  • CRID
    1390282680609017344
  • NII Article ID
    130006993933
  • DOI
    10.14841/jspp.2008.0.0172.0
  • Data Source
    • JaLC
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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