The alternative NADH dehydrogenase is present in mitochondria of some animal taxa

Matus-Ortega, Genaro; Salmerón-Santiago, Karina Gabriela; Flores-Herrera, Óscar; Guerra-Sánchez, Guadalupe; Martı́nez, Federico; Rendón, Juan L.; Pardo, Juan Pablo

doi:10.1016/j.cbd.2011.05.002

Cited by 23 publications

(22 citation statements)

References 59 publications

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“…Recently, the components of the alternative respiratory chain, including a rotenone-insensitive NADH dehydrogenase, have been found in several animal taxa, including tunicates (urochordates) [24]. However, the properties of these alternative NADH dehydrogenases remain uninvestigated, despite an accumulating literature on the alternative respiratory chain of some animals and protozoans, based on our own studies and those of others [25][26][27][28][29][30][31].…”

Section: Introductionmentioning

confidence: 97%

Ciona intestinalis NADH dehydrogenase NDX confers stress-resistance and extended lifespan on Drosophila

Gospodaryov

Lushchak

Rovenko

et al. 2014

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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An assembled cDNA coding for the putative single-subunit NADH dehydrogenase (NDX) of Ciona intestinalis was introduced into Drosophila melanogaster. The encoded protein was found to localize to mitochondria and to confer rotenone-insensitive substrate oxidation in organello. Transgenic flies exhibited increased resistance to menadione, starvation and temperature stress, and manifested a sex and diet-dependent increase in mean lifespan of 20-50%. However, NDX was able only weakly to complement the phenotypes produced by the knockdown of complex I subunits.

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Section: Introductionmentioning

confidence: 97%

Ciona intestinalis NADH dehydrogenase NDX confers stress-resistance and extended lifespan on Drosophila

Gospodaryov

Lushchak

Rovenko

et al. 2014

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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“…. The presence of NDA , NDC and AOX homologues was obtained from the following publications (superscript numbers): 1 (McDonald et al ), 2 (McDonald and Vanlerberghe ), 3 (Costa et al ), 4 (Neimanis et al ), 5 (Matus‐Ortega et al ), 6 (Melo et al ), 7 (Michalecka et al ), 8 (Xu et al ). Other homologues were found by database searches (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…5) for eukaryotes (Moreira et al 2007, Adl et al 2012, Leliaert et al 2012, Wickett et al 2014, Cavalier-Smith et al 2015, including also secondary endosymbiosis events (Lane and Archibald 2008). For comparison, the distributions of other energy-bypass enzymes, AOX, NDA-type and NDC-type, were taken from the literature (Michalecka et al 2003, Melo et al 2004, McDonald and Vanlerberghe 2006, McDonald et al 2009, Matus-Ortega et al 2011, Xu et al 2013, Costa et al 2014, and complemented with additional database searches (Fig. 5).…”

Section: Ndb-type Proteins Are Present In Most Major Eukaryotic Cladesmentioning

confidence: 99%

The evolution of substrate specificity‐associated residues and Ca²⁺‐binding motifs in EF‐hand‐containing type II NAD(P)H dehydrogenases

Hao

Rasmusson

2016

Physiologia Plantarum

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Most eukaryotic organisms, except some animal clades, have mitochondrial alternative electron transport enzymes that allow respiration to bypass the energy coupling in oxidative phosphorylation. The energy bypass enzymes in plants include the external type II NAD(P)H dehydrogenases (DHs) of the NDB family, which are characterized by an EF-hand domain for Ca(2+) binding. Here we investigate these plant enzymes by combining molecular modeling with evolutionary analysis. Molecular modeling of the Arabidopsis thaliana AtNDB1 with the yeast ScNDI1 as template revealed distinct similarities in the core catalytic parts, and highlighted the interaction between the pyridine nucleotide and residues correlating with NAD(P)H substrate specificity. The EF-hand domain of AtNDB1 has no counterpart in ScNDI1, and was instead modeled with Ca(2+) -binding signal transducer proteins. Combined models displayed a proximity of the AtNDB1 EF-hand domain to the substrate entrance side of the catalytic part. Evolutionary analysis of the eukaryotic NDB-type proteins revealed ancient and recent reversions between the motif observed in proteins specific for NADH (acidic type) and NADPH (non-acidic type), and that the clade of enzymes with acidic motifs in angiosperms derives from non-acidic-motif NDB-type proteins present in basal plants, fungi and protists. The results suggest that Ca(2+) -dependent external NADPH oxidation is an ancient process, indicating that it has a fundamental importance for eukaryotic cellular redox metabolism. In contrast, the external NADH DHs in plants are products of a recent expansion, mirroring the expansion of the alternative oxidase family.

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“…Alternative NAD(P)H dehydrogenases usually, but not always, contain FAD as the sole prosthetic group 457. Recently, an in silico approach identified putative alternative NAD(P)H dehydrogenases in a few metazoan organisms, but a functional verification is still missing 14.…”

Section: Branched Respiratory Systems In Fungimentioning

confidence: 99%

Mitochondrial type II NAD(P)H dehydrogenases in fungal cell death

Gonçalves¹,

Videira²

2015

MIC

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During aerobic respiration, cells produce energy through oxidative phosphorylation, which includes a specialized group of multi-subunit complexes in the inner mitochondrial membrane known as the electron transport chain. However, this canonical pathway is branched into single polypeptide alternative routes in some fungi, plants, protists and bacteria. They confer metabolic plasticity, allowing cells to adapt to different environmental conditions and stresses. Type II NAD(P)H dehydrogenases (also called alternative NAD(P)H dehydrogenases) are non-proton pumping enzymes that bypass complex I. Recent evidence points to the involvement of fungal alternative NAD(P)H dehydrogenases in the process of programmed cell death, in addition to their action as overflow systems upon oxidative stress. Consistent with this, alternative NAD(P)H dehydrogenases are phylogenetically related to cell death - promoting proteins of the apoptosis-inducing factor (AIF)-family.

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The alternative NADH dehydrogenase is present in mitochondria of some animal taxa

Cited by 23 publications

References 59 publications

Ciona intestinalis NADH dehydrogenase NDX confers stress-resistance and extended lifespan on Drosophila

Ciona intestinalis NADH dehydrogenase NDX confers stress-resistance and extended lifespan on Drosophila

The evolution of substrate specificity‐associated residues and Ca²⁺‐binding motifs in EF‐hand‐containing type II NAD(P)H dehydrogenases

Mitochondrial type II NAD(P)H dehydrogenases in fungal cell death

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The alternative NADH dehydrogenase is present in mitochondria of some animal taxa

Cited by 23 publications

References 59 publications

Ciona intestinalis NADH dehydrogenase NDX confers stress-resistance and extended lifespan on Drosophila

Ciona intestinalis NADH dehydrogenase NDX confers stress-resistance and extended lifespan on Drosophila

The evolution of substrate specificity‐associated residues and Ca2+‐binding motifs in EF‐hand‐containing type II NAD(P)H dehydrogenases

Mitochondrial type II NAD(P)H dehydrogenases in fungal cell death

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The evolution of substrate specificity‐associated residues and Ca²⁺‐binding motifs in EF‐hand‐containing type II NAD(P)H dehydrogenases