De-etiolation-induced protein 1 (DEIP1) mediates assembly of the cytochrome b6f complex in Arabidopsis

Omar Sandoval-Ibáñez, David Rolo, Rabea Ghandour, Alexander P. Hertle, Tegan Armarego-Marriott, Arun Sampathkumar, Reimo Zoschke and Ralph Bock ()
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Omar Sandoval-Ibáñez: Max Planck Institute of Molecular Plant Physiology
David Rolo: Max Planck Institute of Molecular Plant Physiology
Rabea Ghandour: Max Planck Institute of Molecular Plant Physiology
Alexander P. Hertle: Max Planck Institute of Molecular Plant Physiology
Tegan Armarego-Marriott: Max Planck Institute of Molecular Plant Physiology
Arun Sampathkumar: Max Planck Institute of Molecular Plant Physiology
Reimo Zoschke: Max Planck Institute of Molecular Plant Physiology
Ralph Bock: Max Planck Institute of Molecular Plant Physiology

Nature Communications, 2022, vol. 13, issue 1, 1-16

Abstract: Abstract The conversion of light energy to chemical energy by photosynthesis requires the concerted action of large protein complexes in the thylakoid membrane. Recent work has provided fundamental insights into the three-dimensional structure of these complexes, but how they are assembled from hundreds of parts remains poorly understood. Particularly little is known about the biogenesis of the cytochrome b6f complex (Cytb6f), the redox-coupling complex that interconnects the two photosystems. Here we report the identification of a factor that guides the assembly of Cytb6f in thylakoids of chloroplasts. The protein, DE-ETIOLATION-INDUCED PROTEIN 1 (DEIP1), resides in the thylakoid membrane and is essential for photoautotrophic growth. Knock-out mutants show a specific loss of Cytb6f, and are defective in complex assembly. We demonstrate that DEIP1 interacts with the two cytochrome subunits of the complex, PetA and PetB, and mediates the assembly of intermediates in Cytb6f biogenesis. The identification of DEIP1 provides an entry point into the study of the assembly pathway of a crucial complex in photosynthetic electron transfer.

Date: 2022
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DOI: 10.1038/s41467-022-31758-7

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