Sequence diversity and conservation in factors influencing succinate dehydrogenase flavinylation

Huang, Shaobai; Millar, A. Harvey

doi:10.4161/psb.22815

Cited by 7 publications

(3 citation statements)

References 11 publications

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“…Therefore, Glu19 is a critical residue required for SDH function but not for the interaction with SdhA. Interestingly, despite Glu19 being completely conserved across all SdhE homologues, ,,, a conservative substitution to aspartate did not affect the activation of SDH in growth assays. Glutamate and aspartate are structurally similar residues (i.e., negatively charged and hydrophilic), suggesting that either the change in charge or hydrophobicity associated with E19A is the likely reason for the loss of function.…”

Section: Discussionmentioning

confidence: 93%

The Conserved RGxxE Motif of the Bacterial FAD Assembly Factor SdhE Is Required for Succinate Dehydrogenase Flavinylation and Activity

McNeil

Fineran

2013

Biochemistry

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Succinate dehydrogenase (SDH) is an important respiratory enzyme that plays a critical role in the generation of energy in the majority of eukaryotes, bacteria, and archaea. The activity of SDH is dependent on the covalent attachment of the redox cofactor FAD to the flavoprotein subunit SdhA. In the Gram-negative bacteria Escherichia coli and Serratia sp. ATCC 39006, the covalent attachment of FAD to SdhA is dependent on the FAD assembly factor SdhE (YgfY). Although mechanisms have been proposed, experimental evidence that elucidates the molecular details of SdhE-mediated flavinylation are scarce. In this study, truncation and alanine swap mutagenesis of SdhE identified a highly conserved RGxxE motif that was important for SdhE function. Interestingly, RGxxE site-directed variants were not impaired in terms of protein folding or interactions with SdhA. Purification and analysis of SdhA from different mutant backgrounds demonstrated that SdhE interacts with and flavinylates folded SdhA without a requirement for the assembly of the entire SDH complex. SdhA was also partially active in the absence of SdhE, suggesting that SdhA is able to attach FAD through an inefficient autocatalytic mechanism. The results presented are of widespread relevance because SdhE and SDH are required for bacterial pathogenesis and mutations in the eukaryotic homologues of SdhE and SDH are associated with cancer in humans.

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Section: Discussionmentioning

confidence: 93%

The Conserved RGxxE Motif of the Bacterial FAD Assembly Factor SdhE Is Required for Succinate Dehydrogenase Flavinylation and Activity

McNeil

Fineran

2013

Biochemistry

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“…In the present study, the activity of MDH and the levels of MDH1 were significantly decreased and carbonylated in aged seeds compared with the control (Figs 4A and 5A), indicating that the TCA cycle was inhibited at the CN after seed imbibition. In addition, SDH is a key member of the electron transport chain complex II, which catalyzes the oxidation of succinate to fumarate with the reduction of ubiquinone to ubiquinol and participates in succinate dependent O 2 consumption in the electron transport chain32. SDH1 knockout Arabidopsis mutants had a decreased activity of the electron transport chain, but an increased amount of ROS under environmental stress33.…”

Section: Discussionmentioning

confidence: 99%

Proteomic and Carbonylation Profile Analysis at the Critical Node of Seed Ageing in Oryza sativa

Yin

Xia

et al. 2017

Sci Rep

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The critical node (CN), which is the transition from the plateau phase to the rapid decreasing phase of seed ageing, is extremely important for seed conservation. Although numerous studies have investigated the oxidative stress during seed ageing, information on the changes in protein abundance at the CN is limited. In this study, we aimed to investigate the abundance and carbonylation patterns of proteins at the CN of seed ageing in rice. The results showed that the germination rate of seeds decreased by less than 20% at the CN; however, the abundance of 112 proteins and the carbonylation levels of 68 proteins markedly changed, indicating oxidative damage. The abundance and activity of mitochondrial, glycolytic, and pentose phosphate pathway proteins were reduced; consequently, this negatively affected energy production and germination. Proteins related to defense, including antioxidant system and heat shock proteins, also reduced in abundance. Overall, energy metabolism was reduced at the CN, leading to a decrease in the antioxidant capacity, whereas seed storage proteins were up-regulated and carbonylated, indicating that the seed had a lower ability to utilize seed storage proteins for germination. Thus, the significant decrease in metabolic activities at the CN might accelerate the loss of seed viability.A notable characteristic of seed viability is the reverse S-shaped survival curve during ageing, which includes a plateau phase (Phase I; P-I), followed by a rapid decreasing phase (Phase II; P-II) and a slow decreasing phase (Phase III; P-III). The transformation from P-I to P-II is defined as the critical node (CN), which is highly important for seed conservation 1 . The average germination of approximately 42,000 diverse accessions stored for 16 to 81 years at the National Center for Genetic Resources Preservation, USA has been decreased by 42% 2 . The average germination rate of peanut (stored for 34 years), soybean (stored for 36 years), wheat (stored for 43.6 years), and barley (stored for 44.4 years) is 6%, 21%, 73%, and 86%, respectively 3 . Similar results have been also reported by the Genebank of the Leibniz Institute of Plant Genetics and Crop Plant Research (IPK), Germany 4 . Rice is extremely important food crop. One of main aims in genebanks is maintaining the rice seed safe conservation. At the T.T. Chang Genetic Resources Center in International Rice Research Institute, 183 rice accessions stored up to 30 years showed more than 70% germination 5 , and more than 93% of seed lots produced in 1980 still maintained 85% germination after 33 years in storage 6 . Owing to the reduction in seed viability, the regeneration of genetic resources is considered crucial for maintaining genetic integrity. Previous studies have shown that seed regeneration needs to be carried out prior to the CN in order to prevent a large decrease in viability, which can lead to changes in genetic composition 7,8 . Previously, we showed that the mitochondrial ultrastructure of seed at the CN is abnormal owing to the decre...

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“…Phylogenetic analysis of SDHAF2‐like proteins separates plant‐lineage proteins from those of animals and fungi (Figure S1), although known species relationships within plants are not recovered precisely. In human SDHAF2, the glycine at position 78 (G78R) is essential for the SDHAF2–SDH1 interaction and the accumulation of flavinylated SDH1 (Hao et al ., ), and this glycine residue is conserved across all species (Huang and Millar, 2013a). Mutation of G78R in Serratia SdhE also inhibited the accumulation of flavinylated SDH1 (McNeil et al ., ).…”

Section: Complex II Assembly Machinery Sdhaf1–sdhaf4mentioning

confidence: 99%

Mitochondrial complex II of plants: subunit composition, assembly, and function in respiration and signaling

et al. 2019

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Complex II [succinate dehydrogenase (succinate-ubiquinone oxidoreductase); EC 1.3.5.1; SDH] is the only enzyme shared by both the electron transport chain and the tricarboxylic acid (TCA) cycle in mitochondria. Complex II in plants is considered unusual because of its accessory subunits (SDH5-SDH8), in addition to the catalytic subunits of SDH found in all eukaryotes (SDH1-SDH4). Here, we review compositional and phylogenetic analysis and biochemical dissection studies to both clarify the presence and propose a role for these subunits. We also consider the wider functional and phylogenetic evidence for SDH assembly factors and the reports from plants on the control of SDH1 flavination and SDH1-SDH2 interaction. Plant complex II has been shown to influence stomatal opening, the plant defense response and reactive oxygen speciesdependent stress responses. Signaling molecules such as salicyclic acid (SA) and nitric oxide (NO) are also reported to interact with the ubiquinone (UQ) binding site of SDH, influencing signaling transduction in plants. Future directions for SDH research in plants and the specific roles of its different subunits and assembly factors are suggested, including the potential for reverse electron transport to explain the succinate-dependent production of reactive oxygen species in plants and new avenues to explore the evolution of plant mitochondrial complex II and its utility.

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Sequence diversity and conservation in factors influencing succinate dehydrogenase flavinylation

Cited by 7 publications

References 11 publications

The Conserved RGxxE Motif of the Bacterial FAD Assembly Factor SdhE Is Required for Succinate Dehydrogenase Flavinylation and Activity

The Conserved RGxxE Motif of the Bacterial FAD Assembly Factor SdhE Is Required for Succinate Dehydrogenase Flavinylation and Activity

Proteomic and Carbonylation Profile Analysis at the Critical Node of Seed Ageing in Oryza sativa

Mitochondrial complex II of plants: subunit composition, assembly, and function in respiration and signaling

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