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- Title
De-etiolation-induced protein 1 (DEIP1) mediates assembly of the cytochrome b<sub>6</sub>f complex in Arabidopsis.
- Authors
Sandoval-Ibáñez, Omar; Rolo, David; Ghandour, Rabea; Hertle, Alexander P.; Armarego-Marriott, Tegan; Sampathkumar, Arun; Zoschke, Reimo; Bock, Ralph
- 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. The Cytb6f complex is a multi-subunit enzyme that couples the two photosystems during the light reactions of photosynthesis. Here the authors show that the thylakoid-localized DEIP1 protein interacts with the PetA and PetB subunits, and is essential for Cytb6f complex assembly in Arabidopsis.
- Subjects
CHEMICAL energy conversion; CHLOROPLAST membranes; ARABIDOPSIS; CHEMICAL energy; CHARGE exchange; PROTEINS; CYTOCHROME oxidase
- Publication
Nature Communications, 2022, Vol 13, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-022-31758-7