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.
复制标题
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.
中科院分区:
文献类型:
--
作者:
Twachtmann M;Altmann B;Muraki N;Voss l;Okutani S;Kurisu G;Hase T;Hanke GT.
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.