N-Terminal Structure of Maize Ferredoxin:NADP(+) Reductase Determines Recruitment into Different Thylakoid Membrane Complexes

Autor(en): Twachtmann, Manuel
Altmann, Bianca
Muraki, Norifumi
Voss, Ingo
Okutani, Satoshi
Kurisu, Genji
Hase, Toshiharu
Hanke, Guy T. 
Stichwörter: Biochemistry & Molecular Biology; BUNDLE-SHEATH; Cell Biology; CHLOROPHYLL-A FLUORESCENCE; CYCLIC ELECTRON FLOW; CYTOCHROME B(6)F COMPLEX; DEHYDROGENASE COMPLEX; FERREDOXIN-NADP(+) REDUCTASE; NADP+ OXIDOREDUCTASE; PHOTOSYSTEM-I; Plant Sciences; QUANTUM YIELD; REDOX POISE
Erscheinungsdatum: 2012
Herausgeber: AMER SOC PLANT BIOLOGISTS
Journal: PLANT CELL
Volumen: 24
Ausgabe: 7
Startseite: 2979
Seitenende: 2991
Zusammenfassung: 
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 in Arabidopsis thaliana of 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 in Arabidopsis, and analysis of chlorophyll fluorescence and photosystem I absorbance demonstrates the impact of FNR location on photosynthetic electron flow.
ISSN: 10404651
DOI: 10.1105/tpc.111.094532

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