Journal of Life Science (생명과학회지)

Korean Society of Life Science (한국생명과학회)
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Working Mechanism of Peroxiredoxins (Prxs) and Sulphiredoxin1 (Srx1) in Arabidopsis thaliana

애기장대 peroxiredoxins (Prxs)과 sulphiredoxin1 (Srx1)의 작용기작

  • Kim, Min-Gab (Bio-Crops Development Division, Department of Agricultural Biotechnology, National Academyof Agricultural Science, RDA) ;
  • Su'udi, Mukhamad (Bio-Crops Development Division, Department of Agricultural Biotechnology, National Academyof Agricultural Science, RDA) ;
  • Park, Sang-Ryeol (Bio-Crops Development Division, Department of Agricultural Biotechnology, National Academyof Agricultural Science, RDA) ;
  • Hwang, Duk-Ju (Bio-Crops Development Division, Department of Agricultural Biotechnology, National Academyof Agricultural Science, RDA) ;
  • Bae, Shin-Chul (Bio-Crops Development Division, Department of Agricultural Biotechnology, National Academyof Agricultural Science, RDA)
  • 김민갑 (농촌진흥청 국립농업과학원 신작물개발과) ;
  • 수디 무하마드 (농촌진흥청 국립농업과학원 신작물개발과) ;
  • 박상렬 (농촌진흥청 국립농업과학원 신작물개발과) ;
  • 황덕주 (농촌진흥청 국립농업과학원 신작물개발과) ;
  • 배신철 (농촌진흥청 국립농업과학원 신작물개발과)
  • Received : 2010.11.04
  • Accepted : 2010.12.14
  • Published : 2010.12.30
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Abstract

Plants generate reactive oxygen species (ROS) as a by-product of normal aerobic metabolism or when exposed to a variety of stress conditions, which can cause widespread damage to biological macromolecules. To protect themselves from oxidative stress, plant cells are equipped with a wide range of antioxidant proteins. However, the detailed reaction mechanisms of these are still unknown. Peroxiredoxins (Prxs) are ubiquitous thiol-containing antioxidants that reduce hydrogen peroxide with an N-terminal cysteine. The active-site cysteine of peroxiredoxins is selectively oxidized to cysteine sulfinic acid during catalysis, which leads to inactivation of peroxidase activity. This oxidation was thought to be irreversible. Recently identified small protein sulphiredoxin (Srx1), which is conserved in higher eukaryotes, reduces cysteine.sulphinic acid in yeast peroxiredoxin. Srx1 is highly induced by $H_2O_2$-treatment and the deletion of its gene causes decreased yeast tolerance to $H_2O_2$, which suggest its involvement in the metabolism of oxidants. Moreover, Srx1 is required for heat shock and oxidative stress induced functional, as well as conformational switch of yeast cytosolic peroxiredoxins. This change enhances protein stability and peroxidase activity, indicating that Srx1 plays a crucial role in peroxiredoxin stability and its regulation mechanism. Thus, the understanding of the molecular basis of Srx1 and its regulation is critical for revealing the mechanism of peroxiredoxin action. We postulate here that Srx1 is involved in dealing with oxidative stress via controlling peroxiredoxin recycling in Arabidopsis. This review article thus will be describing the functions of Prxs and Srx in Arabidopsis thaliana. There will be a special focus on the possible role of Srx1 in interacting with and reducing hyperoxidized Cys-sulphenic acid of Prxs.

식물체는 대사과정의 부산물로서 또는 생물학적으로 피해를 줄 수 있는 다양한 종류의 외부 스트레스에 직면했을 활성산소(Reactive Oxygen Species, ROS)를 생산한다. 이러한 oxidative 스트레스로부터 자신들을 보호하기 위하여 식물세포들은 다양한 종류의 항산화 단백질들을 보유하고 있다. 하지만 이들의 작용기작은 여전히 자세히 밝혀지지 않았다. Peroxiredoxins (Prxs)은 식물체에 광범위하게 존재하는 thiol-을 함유한 항산화 단백질로 N-말단에 존재하는 cysteine 잔기를 이용하여 hydrogen peroxide를 환원한다. 이러한 과정에서 peroxiredoxins의 활성부위인 cysteine 잔기는 선택적으로 cysteine sulfinic acid로 산화됨으로써 peroxidase activity의 불활성화를 일으킨다. 이러한 산화과정은 비가역적으로 일어난다. 최근 발견된 진핵생물들에 잘 보존된 sulphiredoxin (Srx1)이라 불리는 단백질은 cysteine-sulphinic acid를 환원시키는 기능을 지닌다. 본 논문에서는 애기장대에 존재하는 Prxs와 Srx의 기능에 대하여 서술할 예정이다.

Keywords

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