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The mitochondrial LYR protein SDHAF1 is required for succinate dehydrogenase activity in Arabidopsis

Li, Ying ; Belt, Katharina ; Alqahtani, Saad F. ; Saha, Saurabh ; Fenske, Ricarda ; Van Aken, Olivier LU ; Whelan, James ; Millar, A. Harvey ; Murcha, Monika W. and Huang, Shaobai (2022) In Plant Journal 110(2). p.499-512
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... (More)

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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author
; ; ; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
assembly factors, complex II, iron–sulfur cluster insertion, mitochondrial metabolism, succinate dehydrogenase
in
Plant Journal
volume
110
issue
2
pages
14 pages
publisher
Wiley-Blackwell
external identifiers
  • scopus:85125281540
  • pmid:35080330
ISSN
0960-7412
DOI
10.1111/tpj.15684
language
English
LU publication?
yes
additional info
Funding Information: KB was supported by a Scholarship for International Research Fees (SIRF) from the University of Western Australia. JW and MWM are funded by an Australian Research Council (ARC) grant (DP210103258). Publisher Copyright: © 2022 The Authors. The Plant Journal published by Society for Experimental Biology and John Wiley & Sons Ltd.
id
4b8c5a29-597e-407d-b585-2cf6c95809cd
date added to LUP
2022-12-30 12:48:22
date last changed
2024-06-10 05:40:55
@article{4b8c5a29-597e-407d-b585-2cf6c95809cd,
  abstract     = {{<p>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.</p>}},
  author       = {{Li, Ying and Belt, Katharina and Alqahtani, Saad F. and Saha, Saurabh and Fenske, Ricarda and Van Aken, Olivier and Whelan, James and Millar, A. Harvey and Murcha, Monika W. and Huang, Shaobai}},
  issn         = {{0960-7412}},
  keywords     = {{assembly factors; complex II; iron–sulfur cluster insertion; mitochondrial metabolism; succinate dehydrogenase}},
  language     = {{eng}},
  number       = {{2}},
  pages        = {{499--512}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{Plant Journal}},
  title        = {{The mitochondrial LYR protein SDHAF1 is required for succinate dehydrogenase activity in Arabidopsis}},
  url          = {{http://dx.doi.org/10.1111/tpj.15684}},
  doi          = {{10.1111/tpj.15684}},
  volume       = {{110}},
  year         = {{2022}},
}