Yeast Prx의 스트레스의존 구조적 변화의 기작
Mechanism of Stress-dependent Structural Change of Yeast Prx
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티올특이성 산화환원 단백질인 peroxiredoxin (thiol-specific peroxiredoxin, Prx) 은 거의 모든 생명체에 존재하며, reactive oxgen species(ROS)을 제거하는 역할을 수행한다. 전자현미경/image processing을 이용하여 세포의방어기작에 중요한 기능을 수행하는 Prx의 구조를 분석하였다. Yeast-Prx는 크게 세 가지의 다른 형태 즉, 구 형태, ring 형태의 구조와 비 규칙적인 적은 입자로 구성되어 있음을 확인하였다. 또한 산화/환원 상태에서의 구조적 변화를 관찰하기위해 DTT와 H2O2를 처리 후 전자현미경을 관찰 하였다. 환원상태의(DTT 처리 후) yeast-Prx는 많은 decamer 구조를 보여주는 반면, 산화상태에서는(H2O2 처리 후) dimer나 구 형태의 구조를 보여 주고 있다. 또한 dimeric subunit간의 ionic interaction이 yeast-Prx의 oligomerization에 중요한 인자임을 확인하였다.
Abstract
Peroxiredoxins (Prxs) are a superfamily of thiol-specific antioxidant proteins present in all organism andinvolved in the hydroperoxide detoxification of the cell. To determine the structural organization of yeast-Prx,-Prxs revealed three differentstructure, i.e. spherical-shaped structure, ring-shaped structure and irregularly-shaped small particles. Inorder to analyze the conformational change of yeast-Prx by reduction and oxidation, Prxs were subjected toDTT and H2O2 -Prx showed a high tendency to form a decamer. However, theychanged into dimeric or spherical structure in the oxidized state. Here we also show ionic interaction betweendimeric subunits is primarily responsible for yeast-Prx oligomerization.
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