Journal of Plant Biotechnology

  • 제33권1호
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  • Pages.1-9
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  • 2006
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  • 1229-2818(pISSN)
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  • 2384-1397(eISSN)
한국식물생명공학회 (The Korean Society of Plant Biotechnology)
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산화 스트레스에 의존한 식물 및 진핵세포 2-시스테인 퍼록시레독신의 기능 조절

Oxidative Stress-dependent Structural and Functional Regulation of 2-cysteine Peroxiredoxins In Eukaryotes Including Plant Cells

  • 장호희 (환경생명과학 국가핵심연구센터) ;
  • 김선영 (경상대학교 응용생명과학부) ;
  • 이상열 (경상대학교 응용생명과학부)
  • Jang, Ho-Hee (Environmental Biotechnology, National Core Research Center) ;
  • Kim, Sun-Young (Division of Applied Life Sciences (BK21 Program), Gyeongsang National University) ;
  • Lee, Sang-Yeol (Division of Applied Life Sciences (BK21 Program), Gyeongsang National University)
  • 발행 : 2006.03.01
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⟨ 이전 논문 다음 논문 ⟩

초록

도처에 분포하는 peroxiredoxins (Prxs)은 세포 내 방어신호전달 과정에서 다양한 기능을 하는 것으로 나타났다. Prxs는 크게 typical 2-Cys Prx, atypical 2-Cys Prx와 1-Cys Prx의 세 부류로 분류되는데, 이것들은 cysteine 잔기의 수와 촉매기전에 따라 구분된다. 세 종류의 단백질 중, N-말단에 peroxidatic cysteine 잔기를 포함하는 typical 2-Cys Prx는 $H_2O_2$ 분해과정 동안 과산화물-의존적인 sulfenic acid로의 산화와 thiol-의존적 환원과정이 순환되어 일어난다. Sulfenic acid는 고농도의 $H_2O_2$와 Trx, Trx reductase와 NADPH를 포함하는 촉매 요소의 존재하에 cysteine sulfenic acid로 과산화 될 수 있다 과산화된 2-Cys Prx는 ATP 의존성 효소인 sulfiredoxin의 작용에 의해 천천히 환원된다. 세포가 강력한 산화나 열 충격 스트레스에 노출되면, 2-Cys Prx는 LMW 단백질에서 HMW complex로 구조를 변화시켜 peroxidase에서 chaperone으로 기능의 전환을 일으킨다. 2-Cys Prx의 C-말단 부분 역시 이러한 구조적 전환에 중요한 역할을 한다. 따라서, C-말단이 잘려진 단백질은 과산화가 되지 않고 단백질의 구조와 기능이 조절될 수 없다. 이러한 반응들은 활성 자리인 peroxidatic cysteine 잔기에 의해 일차적으로 유도되며, 그것은 세포에서 '$H_2O_2$ sensor' 로서 작용하다. 2-Cys Prx의 가역적인 구조와 기능 변화는 세포가 외부자극에 적응하는 수단으로 작용하며, 아마도 세포내 방어신호체계를 활성화 시키는 것으로 생각된다. 특히, chloroplast에 존재하는 식물 2-Cys Prx는 촉매반응 동안 주된 구조적인 변화를 나타내는 역동적인 단백질 구조를 가지고 있어서, 산화-환원 의존적으로 super-complex를 형성하고 가역적으로 thylakoid membrane에 부착한다.

Peroxiredoxins (Prxs) are ubiquitously distributed and play important functions in diverse cellular signaling systems. The proteins are largely classified into three groups, such as typical 2-Cys Prx, atypical 2-Cys Prx, and 1-Cys Prx, that are distinguished by their catalytic mechanisms and number of Cys residues. From the three classes of Prxs, the typical 2-Cys Prx containing the two-conserved Cys residues at its N-terminus and C-terminus catalyzes $H_2O_2$ with the use of thioredoxin (Trx) as an electron donor. During the catalytic cycle, the N-terminal Cys residue undergoes a peroxide-dependent oxidation to sulfenic acid, which can be further oxidized to sulfinic acid at the presence of high concentrations of $H_2O_2$ and a Trx system containing Trx, Trx reductase, and NADPH. The sulfinic acid form of 2-Cys Prx is reduced by the action of sulfiredoxin which requires ATP as an energy source. Under the strong oxidative or heat shock stress conditions, 2-Cys Prx in eukaryotes rapidly switches its protein structure from low-molecular-weight species to high-molecular-weight protein structures. In accordance with its structural changes, the protein concomitantly triggers functional switching from a peroxidase to a molecular chaperone, which can protect its substrate denaturation from external stress. In addition to its N-terminal active site, the C-terminal domain including 'YF-motif' of 2-Cys Prx plays a critical role in the structural changes. Therefore, the C-terminal truncated 2-Cys Prxs are not able to regulate their protein structures and highly resistant to $H_2O_2$-dependent hyperoxidation, suggesting that the reaction is guided by the peroxidatic Cys residue. Based on the results, it may be concluded that the peroxidatic Cys of 2-Cys Prx acts as an '$H_2O_2$-sensor' in the cells. The oxidative stress-dependent regulation of 2-Cys Prx provides a means of defense systems in cells to adapt stress conditions by activating intracellular defense signaling pathways. Particularly, 2-Cys Prxs in plants are localized in chloroplasts with a dynamic protein structure. The protein undergoes conformational changes again oxidative stress. Depending on a redox-potential of the chloroplasts, the plant 2-Cys Prx forms super-molecular weight protein structures, which attach to the thylakoid membranes in a reversible manner.

키워드

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피인용 문헌

  1. Site-directed mutagenesis substituting cysteine for serine in 2-Cys peroxiredoxin (2-Cys Prx A) ofArabidopsis thalianaeffectively improves its peroxidase and chaperone functions vol.116, pp.4, 2015, https://doi.org/10.1093/aob/mcv094
  2. Overexpression of 2-cysteine peroxiredoxin enhances tolerance to methyl viologen-mediated oxidative stress and high temperature in potato plants vol.49, pp.8, 2011, https://doi.org/10.1016/j.plaphy.2011.04.001