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De-etiolation-induced protein 1 (DEIP1) mediates assembly of the cytochrome b 6 f complex in Arabidopsis.

Omar Sandoval-IbañezDavid RoloRabea GhandourAlexander P HertleTegan Armarego-MarriottArun SampathkumarReimo ZoschkeRalph Bock
Published in: Nature communications (2022)
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 b 6 f complex (Cytb 6 f), the redox-coupling complex that interconnects the two photosystems. Here we report the identification of a factor that guides the assembly of Cytb 6 f 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 Cytb 6 f, 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 Cytb 6 f biogenesis. The identification of DEIP1 provides an entry point into the study of the assembly pathway of a crucial complex in photosynthetic electron transfer.
Keyphrases
  • electron transfer
  • binding protein
  • protein protein
  • amino acid
  • high glucose
  • diabetic rats
  • transcription factor
  • drug induced
  • stress induced