l-Galactono-1,4-lactone dehydrogenase (GLDH) Forms Part of Three Subcomplexes of Mitochondrial Complex I in Arabidopsis thaliana

Schertl, Peter; Sunderhaus, Stephanie; Klodmann, Jennifer; Grozeff, Gustavo Esteban Gergoff; Bártoli, Carlos Guillermo; Braun, Hans‐Peter

doi:10.1074/jbc.m111.305144

Cited by 89 publications

(81 citation statements)

References 53 publications

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“…7). Protein levels of nuclear-encoded GLDH, which regulates the assembly of Complex I (Schertl et al 2012), remained unchanged in the mitochondria of S-deficient A. thaliana relative to the control (Fig. 5b).…”

Section: Changes In Complex I Abundance and Capacitymentioning

confidence: 91%

“…GLDH is not associated with the holocomplex but with a smaller version of Complex I (Heazlewood et al 2003), and with three subcomplexes representing Complex I assembly intermediates (Schertl et al 2012); therefore, it cannot be considered a Complex I subunit (Meyer 2012). However, because the knockout mutant of GLDH does not synthesise Complex I, GLDH has been described as the potential assembly factor for Complex I in A. thaliana (Pineau et al 2008).…”

Section: Discussionmentioning

confidence: 99%

“…5b) and activities (OstaszewskaBugajska et al 2015) of GLDH in S-deficient A. thaliana and control plants suggest the maintenance of ascorbate biosynthesis and/or support of Complex I structure when tissue S content decreases. GLDH does not need to be active to function in Complex I assembly (Schertl et al 2012).…”

Section: Discussionmentioning

confidence: 99%

“…Three-dimensional gel electrophoresis with mass spectrometry provided a 3D gel map of Arabidopsis Complex I containing 55 types of proteins (Peters et al 2013). At least 40 of them are homologs of bovine Complex I, nine are unique to plants, and six are extra subunits: three gammatype carbonic anhydrases (CA1-3), two carbonic anhydrase-like proteins (CAL1-2) (Perales et al 2004(Perales et al , 2005, and L-galactone-1,4-lactone dehydrogenase (GLDH), which is the assembly factor of Complex I (Pineau et al 2008;Schertl et al 2012). The L-shaped Complex I is formed by two elongated domains consisting of a membrane arm with an extra spherical domain containing CA1-3 and a peripheral arm that protrudes into the mitochondrial matrix (Dudkina et al 2006).…”

Section: Introductionmentioning

confidence: 99%

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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.

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Section: Changes In Complex I Abundance and Capacitymentioning

confidence: 91%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

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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“…Consistent with the reduction of cytochrome c, GLDH is believed to be located in the intermembrane space (IMS), associated with the membrane arm of complex I (25). A recent study described two new low abundance GLDH containing protein complexes with molecular mass of 470 and 420 kDa in Arabidopsis mitochondria (43). These complexes represent parts of the membrane arm of complex I and assembly intermediates.…”

Section: Introductionmentioning

confidence: 99%

The Inter-Relationship of Ascorbate Transport, Metabolism and Mitochondrial, Plastidic Respiration

Szarka

Bánhegyi

Asard

2013

Antioxidants & Redox Signaling

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Significance: Ascorbate, this multifaceted small molecular weight carbohydrate derivative, plays important roles in a range of cellular processes in plant cells, from the regulation of cell cycle, through cell expansion and senescence. Beyond these physiological functions, ascorbate has a critical role in responses to abiotic stresses, such as high light, high salinity, or drought. The biosynthesis, recycling, and intracellular transport are important elements of the balancing of ascorbate level to the always-changing conditions and demands. Recent Advances: A bidirectional tight relationship was described between ascorbate biosynthesis and the mitochondrial electron transfer chain (mETC), since L-galactono-1,4-lactone dehydrogenase (GLDH), the enzyme catalyzing the ultimate step of ascorbate biosynthesis, uses oxidized cytochrome c as the only electron acceptor and has a role in the assembly of Complex I. A similar bidirectional relationship was revealed between the photosynthetic apparatus and ascorbate biosynthesis since the electron flux through the photosynthetic ETC affects the biosynthesis of ascorbate and the level of ascorbate could affect photosynthesis. Critical Issues: The details of this regulatory network of photosynthetic electron transfer, respiratory electron transfer, and ascorbate biosynthesis are still not clear, as are the potential regulatory role and the regulation of intracellular ascorbate transport and fluxes. Future Directions: The elucidation of the role of ascorbate as an important element of the network of photosynthetic, respiratory ETC and tricarboxylic acid cycle will contribute to understanding plant cell responses to different stress conditions.

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Direct Microbial Routes to VitaminCProduction

Pappenberger

Hohmann

2016

Industrial Biotechnology of Vitamins, Biopigments, and Antioxidants

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l-Galactono-1,4-lactone dehydrogenase (GLDH) Forms Part of Three Subcomplexes of Mitochondrial Complex I in Arabidopsis thaliana

Cited by 89 publications

References 53 publications

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

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

The Inter-Relationship of Ascorbate Transport, Metabolism and Mitochondrial, Plastidic Respiration

Direct Microbial Routes to VitaminCProduction

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