Subcomplexes of Ancestral Respiratory Complex I Subunits Rapidly Turn Over in Vivo as Productive Assembly Intermediates in Arabidopsis*

Li, Lie; Nelson, Clark J.; Carrie, Chris; Gawryluk, Ryan M.R.; Solheim, Cory; Gray, Michael W.; Whelan, James; Millar, A. Harvey

doi:10.1074/jbc.m112.432070

Cited by 46 publications

(59 citation statements)

References 52 publications

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“…Complex I levels in the B10 line reached 100% only at growth stage 3.90, or mature rosettes, which is 2 weeks after growth stage 1.04 when INDH expression reached >100% of wild-type levels. The dynamics of complex I assembly in Arabidopsis was recently described for the first time (Li et al, 2013). Reassembly of complex I was apparent 20 min after reintroduction of the CA2 subunit in isolated mitochondria of a ca2 mutant.…”

Section: Reassembly Of Complex I Is Significantly Delayed Upon Expresmentioning

confidence: 97%

“…The complex is assembled in a modular way with the help of at least 10 assembly factors Hoefs et al, 2012;Mimaki et al, 2012). Complex I in plants follows a similar assembly pattern, except that it builds on the assembly of the plant-specific carbonic anhydrase module as an early step Li et al, 2013). It is not yet known whether any of the mammalian assembly factors are conserved in plants.…”

Section: Introductionmentioning

confidence: 99%

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The Evolutionarily Conserved Iron-Sulfur Protein INDH Is Required for Complex I Assembly and Mitochondrial Translation in Arabidopsis

et al. 2013

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The assembly of respiratory complexes is a multistep process, requiring coordinate expression of mitochondrial and nuclear genes and cofactor biosynthesis. We functionally characterized the iron-sulfur protein required for NADH dehydrogenase (INDH) in the model plant Arabidopsis thaliana. An indh knockout mutant lacked complex I but had low levels of a 650-kD assembly intermediate, similar to mutations in the homologous NUBPL (nucleotide binding protein-like) in Homo sapiens. However, heterozygous indh/+ mutants displayed unusual phenotypes during gametogenesis and resembled mutants in mitochondrial translation more than mutants in complex I. Gradually increased expression of INDH in indh knockout plants revealed a significant delay in reassembly of complex I, suggesting an indirect role for INDH in the assembly process. Depletion of INDH protein was associated with decreased 35 S-Met labeling of translation products in isolated mitochondria, whereas the steady state levels of several mitochondrial transcripts were increased. Mitochondrially encoded proteins were differentially affected, with near normal levels of cytochrome c oxidase subunit2 and Nad7 but little Nad6 protein in the indh mutant. These data suggest that INDH has a primary role in mitochondrial translation that underlies its role in complex I assembly.

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Section: Reassembly Of Complex I Is Significantly Delayed Upon Expresmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

The Evolutionarily Conserved Iron-Sulfur Protein INDH Is Required for Complex I Assembly and Mitochondrial Translation in Arabidopsis

et al. 2013

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“…A lower amount of assembled complex I in slp1 (approximately 50%; Fig. 3C) subsequently leads to lower abundance of supercomplexes containing complex I because of equilibrium between them (Li et al, 2013). Alternatively, the near complete loss of supercomplex I 2 III 4 could be a consequence of destabilizing effects that occur within the inner membrane in the absence of SLP1.…”

Section: How Does Slp1 Affect Complex I Abundance?mentioning

confidence: 99%

An Arabidopsis Stomatin-Like Protein Affects Mitochondrial Respiratory Supercomplex Organization

et al. 2014

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Stomatins belong to the band-7 protein family, a diverse group of conserved eukaryotic and prokaryotic membrane proteins involved in the formation of large protein complexes as protein-lipid scaffolds. The Arabidopsis (Arabidopsis thaliana) genome contains two paralogous genes encoding stomatin-like proteins (SLPs; AtSLP1 and AtSLP2) that are phylogenetically related to human SLP2, a protein involved in mitochondrial fusion and protein complex formation in the mitochondrial inner membrane. We used reverse genetics in combination with biochemical methods to investigate the function of AtSLPs. We demonstrate that both SLPs localize to mitochondrial membranes. SLP1 migrates as a large (approximately 3 MDa) complex in blue-native gel electrophoresis. Remarkably, slp1 knockout mutants have reduced protein and activity levels of complex I and supercomplexes, indicating that SLP affects the assembly and/or stability of these complexes. These findings point to a role for SLP1 in the organization of respiratory supercomplexes in Arabidopsis.

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“…The number of subunits that join to form structural modules and establish a functional Complex I is a major factor determining assembly of this protein in fungi and mammals (Mimaki et al 2012). A similar modular assembly pathway was proposed for the Complex I membrane arm in A. thaliana (Meyer et al 2011;Li et al 2013). A lower level of the Fe-S-containing NAD9 mitochondrial-encoded subunit of Complex I was found in S-deficient A. thaliana (Fig.…”

Section: Discussionmentioning

confidence: 98%

Changes in the OXPHOS system in leaf and root mitochondria of Arabidopsis thaliana subjected to long-term sulphur deficiency

Ostaszewska-Bugajska

Juszczuk

2016

Acta Physiol Plant

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Long-term sulphur (S) deficiency in Arabidopsis thaliana affects the functioning of the mitochondrial oxidative phosphorylation system (OXPHOS) via alteration of the multisubunit NADH-ubiquinone oxidoreductase (Complex I; EC 1.6.5.3), which contains several iron-sulphur clusters. Densitometric analysis of bands of respiratory chain complexes after one-dimensional blue-native polyacrylamide gel electrophoresis (BN-PAGE) showed that levels and in-gel capacities of Complex I in leaf and root mitochondria were lower than those of the control. Twodimensional BN/SDS-PAGE showed lower abundance of all Complex I subunits, but the qualitative structural composition (subunit expression and mobility) did not change. In mitochondria of S-deficient A. thaliana, impairment of Complex I could be compensated to some extent by additional type II NADH dehydrogenases that do not contain iron-sulphur clusters. The level and capacity of external NADH dehydrogenases in leaf and root mitochondria was higher under S deficiency, but that of internal NADH dehydrogenases did not differ from the control. The amount of COXII (mitochondrial-encoded subunit of cytochrome c oxidase in Complex IV; EC 1.9.3.1) and the capacity of Complex IV were lower under S deficiency, but levels of alternative oxidase, a bypass to Complex IV, did not change. We discuss S deficiency in A. thaliana in relation to the assembly and stability of Complex I and to a bypass of Complex I by external type II NADH dehydrogenases.

show abstract

Subcomplexes of Ancestral Respiratory Complex I Subunits Rapidly Turn Over in Vivo as Productive Assembly Intermediates in Arabidopsis*

Cited by 46 publications

References 52 publications

The Evolutionarily Conserved Iron-Sulfur Protein INDH Is Required for Complex I Assembly and Mitochondrial Translation in Arabidopsis

The Evolutionarily Conserved Iron-Sulfur Protein INDH Is Required for Complex I Assembly and Mitochondrial Translation in Arabidopsis

An Arabidopsis Stomatin-Like Protein Affects Mitochondrial Respiratory Supercomplex Organization

Changes in the OXPHOS system in leaf and root mitochondria of Arabidopsis thaliana subjected to long-term sulphur deficiency

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