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Updated: Jul 21, 2025

Protein-protein Interactions Visualized by Bimolecular Fluorescence Complementation in Tobacco Protoplasts and Leaves
Published on: March 9, 2014
NdhS interacts with cytochrome b6 f to form a complex in Arabidopsis
Yixin Lan1, Qi Chen1, Hualing Mi1
1National Key Laboratory of Plant Molecular Genetics, CAS Center for Excellence in Molecular Plant Sciences / Institute of Plant Physiology and Ecology, 300 Fenglin Road, Shanghai, 200032, P.R. China.
Abstract:
Cyclic electron transport (CET) around photosystem I (PSI) is crucial for photosynthesis to perform photoprotection and sustain the balance of ATP and NADPH. However, the critical component of CET, cyt b6 f complex (cyt b6 f), functions in CET has yet to be understood entirely. In this study, we found that NdhS, a subunit of NADPH dehydrogenase-like (NDH) complex, interacted with cyt b6 f to form a complex in Arabidopsis. This interaction depended on the N-terminal extension of NdhS, which was conserved in eukaryotic plants but defective in prokaryotic algae. The migration of NdhS was much more in cyt b6 f than in PSI-NDH super-complex. Based on these results, we suggested that NdhS and NADP+ oxidoreductase provide a docking domain for the mobile electron carrier ferredoxin to transfer electrons to the plastoquinone pool via cyt b6 f in eukaryotic photosynthesis.
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