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

Manuel Twachtmann, Bianca Altmann, Norifumi Muraki, Ingo Voss, Satoshi Okutani, Genji Kurisu, Toshiharu Hase, Guy T. Hanke

Research output: Contribution to journalArticlepeer-review

26 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)2979-2991
Number of pages13
JournalPlant Cell
Volume24
Issue number7
DOIs
Publication statusPublished - 2012 Jul
Externally publishedYes

ASJC Scopus subject areas

  • Plant Science
  • Cell Biology

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