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    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. © 2022 The Authors. The Plant Journal published by Society for Experimental Biology and John Wiley & Sons Ltd.

    Citation

    Ying Li, Katharina Belt, Saad F Alqahtani, Saurabh Saha, Ricarda Fenske, Olivier Van Aken, James Whelan, A Harvey Millar, Monika W Murcha, Shaobai Huang. The mitochondrial LYR protein SDHAF1 is required for succinate dehydrogenase activity in Arabidopsis. The Plant journal : for cell and molecular biology. 2022 Apr;110(2):499-512

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    PMID: 35080330

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