ArticleThe Plant journal : for cell and molecular biology2022
The mitochondrial LYR protein SDHAF1 is required for succinate dehydrogenase activity in Arabidopsis.
Article in The Plant journal : for cell and molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 15 citations in OpenAlex.
- Functional Relationships of Two NFU Proteins in Maintaining the Abundances of Mitochondrial Iron-Sulfur Proteins.Plant direct · 2025Article
- Assembly and comparative analysis of the complete mitochondrial of Spodiopogon sagittifolius, an endemic and protective species from Yunnan, China.BMC plant biology · 2025Article
- The complex I subunit B22 contains a LYR domain that is crucial for an interaction with the mitochondrial acyl carrier protein SDAP1.The Plant journal : for cell and molecular biology · 2025Article
- The biogenesis and regulation of the plant oxidative phosphorylation system.Plant physiology · 2023Review
- Structural and Functional Perspectives on Mitochondrial LYR-Domain Proteins in Plants.Physiologia plantarumArticle
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Authors and funding
10 authors at 2 institutions in 3 countries.
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Abstract
Succinate dehydrogenase (SDH, complex II), which plays an essential role in mitochondrial respiration and tricarboxylic acid metabolism, requires the assembly of eight nuclear-encoded subunits and the insertion of various cofactors. Here, we report on the characterization of an Arabidopsis thaliana leucine-tyrosine-arginine (LYR) protein family member SDHAF1, (At2g39725) is a factor required for SDH activity. SDHAF1 is located in mitochondria and can fully complement the yeast SDHAF1 deletion strain. Knockdown of SDHAF1 using RNA interference resulted in a decrease in seedling hypocotyl elongation and reduced SDH activity. Proteomic analyses revealed a decreased abundance of various SDH subunits and assembly factors. Protein interaction assays revealed that SDHAF1 can interact exclusively with the Fe-S cluster-containing subunit SDH2 and HSCB, a cochaperone involved in Fe-S cluster complex recruitment. Therefore, we propose that in Arabidopsis, SDHAF1 plays a role in the biogenesis of SDH2 to form the functional complex II, which is essential for mitochondrial respiration and metabolism.
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