N-terminal structure of maize ferredoxin : NADP+ reductase determines recruitment into different thylakoid membrane complexes.

N-terminal structure of maize ferredoxin : NADP+ reductase determines recruitment into different thylakoid membrane complexes.
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玉米铁氧还蛋白的 N 端结构:NADP 还原酶决定招募到不同的类囊体膜复合物中。

DOI:
10.1105/tpc.111.094532
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发表时间:
2012
期刊:
影响因子:
11.6
通讯作者:
Hanke GT.
Hanke GT.
中科院分区:
生物学1区
文献类型:
--
作者:
Twachtmann M;Altmann B;Muraki N;Voss l;Okutani S;Kurisu G;Hase T;Hanke GT.

文献摘要

相似文献

为了适应不同的光强度,光合生物通过类囊体膜上的几条替代途径操纵电子流。酶铁氧还蛋白:NADP+还原酶(FNR)具有调节这种电子分配的潜力,因为它是大多数这些电子级联的组成部分,可以与几种不同的膜复合物。然而,控制FNR相对定位于不同膜复合物的因素尚未建立。玉米(Zea mays)含有三种叶绿体FNR蛋白与完全不同的膜协会,我们发现,这些蛋白质有可变的细胞之间的分布进行主要是循环电子传递(束鞘)和线性电子传递(叶肉)。在这里,所有三种酶的晶体结构得到解决,揭示了N-末端结构域和二聚体界面的主要结构差异。玉米FNR嵌合体和截短蛋白在拟南芥中的表达表明,N-末端决定FNR向不同膜复合物的募集。此外,不同的玉米FNR蛋白在拟南芥中的表达定位于不同的类囊体膜复合物上,叶绿素荧光和光系统I吸光度分析表明FNR蛋白定位对光合电子流的影响。
To adapt to different light intensities, photosynthetic organisms manipulate the flow of electrons through several alternative pathways at the thylakoid membrane. The enzyme ferredoxin:NADP+reductase (FNR) has the potential to regulate this electron partitioning because it is integral to most of these electron cascades and can associate with several different membrane complexes. However, the factors controlling relative localization of FNR to different membrane complexes have not yet been established. Maize (Zea mays) contains three chloroplast FNR proteins with totally different membrane association, and we found that these proteins have variable distribution between cells conducting predominantly cyclic electron transport (bundle sheath) and linear electron transport (mesophyll). Here, the crystal structures of all three enzymes were solved, revealing major structural differences at the N-terminal domain and dimer interface. Expression inArabidopsis thalianaof maize FNRs as chimeras and truncated proteins showed the N-terminal determines recruitment of FNR to different membrane complexes. In addition, the different maize FNR proteins localized to different thylakoid membrane complexes on expression inArabidopsis, and analysis of chlorophyll fluorescence and photosystem I absorbance demonstrates the impact of FNR location on photosynthetic electron flow.