ArticleCommunications biology2025
Biochemical characterisation supports a central role for Oep80 from Arabidopsis thaliana in chloroplastic β-barrel protein assembly.
Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Assembly of two functionally-distinct protein import complexes in the outer membrane of plant chloroplasts.Nature communications · 2026Article
- Structural mass spectrometry techniques for characterisation of plant and algal proteins.The Plant journal : for cell and molecular biology · 2026Review
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3 authors.
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Abstract
The outer membranes of Gram-negative bacteria and endosymbiotic organelles mitochondria and chloroplasts contain β-barrel proteins essential for transporting metabolites, ions and proteins, as well as regulatory functions. While the assembly mechanisms of these proteins are well-studied in bacteria and mitochondria, they remain poorly understood in chloroplasts due to challenges in producing sufficient quantities of relevant plant proteins for structural and biochemical analyses. Here, we show that Oep80, the presumed core component of the chloroplastic β-barrel assembly machinery, can be overexpressed in bacteria and refolded in large quantities. While the soluble POTRA domain caused the heterologous protein to aggregate, we found that the isolated β-barrel membrane domain (Oep80
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