The Saccharomyces cerevisiae NDE1 and NDE2 Genes Encode Separate Mitochondrial NADH Dehydrogenases Catalyzing the Oxidation of Cytosolic NADH

Luttik, Marijke A. H.; Overkamp, Karin; Kötter, Peter; Vries, Simon de; Dijken, Johannes P. van; Pronk, Jack T.

doi:10.1074/jbc.273.38.24529

Cited by 280 publications

(297 citation statements)

References 44 publications

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“…The presence of this motif in the plant NDB-like NAD(P)H DH sequences is not unexpected because the corresponding activities are sensitive to calcium levels (Møller, 2001). This motif was not seen in ScNDE1 or ScNDE2, which is consistent with these yeast NADH DHs being calcium insensitive (Luttik et al, 1998). However, the insertion sequence and EF hand motif was also absent from the AT4g21490 sequence and the NDA-like NAD(P)H DH sequences.…”

Section: Sequence Analysissupporting

confidence: 62%

“…There is evidence from complementation studies in yeast and N. crassa that ScNDE1, ScNDE2, and ScNDE1 are NADH-specific enzymes (Marres et al, 1991;Luttik et al, 1998), whereas NcNDE1 is an NADPH-specific enzyme (Melo et al, 2001). From an examination of the NcNDE1 sequence, Melo et al (2001) speculated that the more N-terminal DNF domain binds NADPH as the third Gly is replaced by Ser, and the negative charge at the end of the second ␤-sheet is missing.…”

Section: Substrate Specificity Of Atndi1mentioning

confidence: 99%

“…These have been well characterized (Marres et al, 1991;de Vries et al, 1992;Luttik et al, 1998). Kinetic analyses have also shown these enzyme activities to be present in mitochondria from the fungus Neurospora crassa (Weiss et al, 1970).…”

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confidence: 99%

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Identification of AtNDI1, an Internal Non-Phosphorylating NAD(P)H Dehydrogenase in Arabidopsis Mitochondria

et al. 2003

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Plant mitochondria contain non-phosphorylating NAD(P)H dehydrogenases (DHs) that are not found in animal mitochondria. The physiological function, substrate specificity, and location of enzymes within this family have yet to be conclusively determined. We have linked genome sequence information to protein and biochemical data to identify that At1g07180 (SwissProt Q8GWA1) from the Arabidopsis Genome Initiative database encodes AtNDI1, an internal NAD(P)H DH in Arabidopsis mitochondria. Three lines of evidence are presented: (a) The predicted protein sequence of AtNDI1 has high homology with other designated NAD(P)H DHs from microorganisms, (b) the capacity for matrix NAD(P)H oxidation via the rotenone-insensitive pathway is significantly reduced in the Atndi1 mutant plant line, and (c) the in vitro translation product of AtNDI1 is imported into isolated mitochondria and located on the inside of the inner membrane.

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Section: Sequence Analysissupporting

confidence: 62%

Section: Substrate Specificity Of Atndi1mentioning

confidence: 99%

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Identification of AtNDI1, an Internal Non-Phosphorylating NAD(P)H Dehydrogenase in Arabidopsis Mitochondria

et al. 2003

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“…They might be involved in situations of NAD(P)H stress, but their specific role is unclear. In addition to metabolic functions (7,8,10), a regulatory role in response to the redox state of the plastoquinone pool has been suggested in cyanobacteria (9). This is the first time that the gene for a mitochondrial NADPH dehydrogenase has been identified and that evidence for at least two external NAD(P)H dehydrogenases in N. crassa mitochondria has been obtained.…”

Section: Resultsmentioning

confidence: 99%

The External Calcium-dependent NADPH Dehydrogenase from Neurospora crassa Mitochondria

Melo

Duarte

Møller

et al. 2001

Journal of Biological Chemistry

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We have inactivated the nuclear gene coding for a putative NAD(P)H dehydrogenase from the inner membrane of Neurospora crassa mitochondria by repeat-induced point mutations. The respiratory rates of mitochondria from the resulting mutant (nde-1) were measured, using NADH or NADPH as substrates under different assay conditions. The results showed that the mutant lacks an external calcium-dependent NADPH dehydrogenase. The observation of NADH and NADPH oxidation by intact mitochondria from the nde-1 mutant suggests the existence of a second external NAD(P)H dehydrogenase. The topology of the NDE1 protein was further studied by protease accessibility, in vitro import experiments, and in silico analysis of the amino acid sequence. Taken together, it appears that most of the NDE1 protein extends into the intermembrane space in a tightly folded conformation and that it remains anchored to the inner mitochondrial membrane by an Nterminal transmembrane domain.In nonphotosynthetic eukaryotes, the mitochondrion is the cellular organelle responsible for producing most of the energy required for cellular metabolism. The process of oxidative phosphorylation takes place in the inner mitochondrial membrane, whereby the electrons produced by the oxidation of substrates like NAD(P)H are transported through the electron transport chain to oxygen, coupled to the generation of a transmembrane proton gradient that eventually leads to ATP synthesis (1). In contrast to mammals, the electron transport chains of plants and fungi possess several nonproton-pumping NAD(P)H dehydrogenases for transferring electrons to ubiquinone (2). In the case of potato tubers, four rotenone-insensitive NAD(P)H dehydrogenases have been identified in the inner mitochondrial membrane, two with the catalytic site facing the matrix (3, 4) and two facing the intermembrane space (5). In mitochondria from Saccharomyces cerevisiae, where the proton-pumping complex I is not present, the oxidation of NADH and NADPH is performed exclusively by three nonproton-pumping enzymes, one facing the matrix and two facing the intermembrane space (6 -8). In addition, the genome analysis of Synechocystis revealed three open reading frames that may code for such type II NAD(P)H dehydrogenases (9). On the other hand, only one external type II NADH dehydrogenase was reported for the fungus Yarrowia lipolytica (10). Although NAD(P)H dehydrogenases have been studied for a long time, our understanding of protein function at the molecular level is still very incomplete. The cloning of genes encoding several of these rotenoneinsensitive NAD(P)H dehydrogenases from mitochondria of different organisms (7, 10 -13) provides important tools for further research in this field. These enzymes might constitute a wasteful system acting to prevent the overreduction of the electron transport components and the production of reactive oxygen species, but their exact roles remain unclear.Both proton-pumping and nonproton-pumping NAD(P)H dehydrogenases have been described in Neurospora crassa mitochon...

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“…Sample from lane 3 (FPL-UC7) was obtained through an extra sucrose gradient purification and therefore the background for this sample is lower. Other samples were isolated by the mechanical method (Luttik et al, 1998). Lane 1, wild-type CBS 6054; lanes 2 and 3, FPL-UC7 (ura3-3); lane 4, FPL-Shi31 (sto1-); lane 5, FPL-Shi21 (cyc1-).…”

Section: Cytochrome Spectra Studiesmentioning

confidence: 99%

SHAM‐sensitive alternative respiration in the xylose‐metabolizing yeast Pichia stipitis

Shi

Cruz

Sherman

et al. 2002

Yeast

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SHAM-sensitive (STO) alternative respiration is present in the xylose-metabolizing, Crabtree-negative yeast, Pichia stipitis, but its pathway components and physiological roles during xylose metabolism are poorly understood. We cloned PsSTO1, which encodes the SHAM-sensitive terminal oxidase (PsSto1p), by genome walking from wild-type CBS 6054 and subsequently deleted PsSTO1 by targeted gene disruption. The resulting sto1-deletion mutant, FPL-Shi31, did not contain other isoforms of Sto protein that were detectable by Western blot analysis using an alternative oxidase monoclonal antibody raised against the Sto protein from Sauromatum guttatum. Levels of cytochromes b, c, c 1 and a·a 3 did not change in the sto1-mutant, which indicated that deleting PsSto1p did not alter the cytochrome pool. Interestingly, the sto1-deletion mutant stopped growing earlier than the parent and produced 20% more ethanol from xylose. Heterologous expression of PsSTO1 in Saccharomyces cerevisiae increased its total oxygen consumption rate and imparted cyanide-resistant oxygen uptake but did not enable growth on ethanol, indicating that PsSto1p is not coupled to ATP synthesis. We present evidence that the mitochondrial NADH dehydrogenase complex (Complex I) was present in wild-type CBS 6054 but was bypassed in the cells during xylose metabolism. Unexpectedly, deleting PsSto1p led to the use of Complex I in the mutant cells when xylose was the carbon source. We propose that the non-proton-translocating NAD(P)H dehydrogenases are linked to PsSto1p in xylose-metabolizing cells and that this non-ATP-generating route serves a regulatory function in the complex redox network of P. stipitis. Published in

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The Saccharomyces cerevisiae NDE1 and NDE2 Genes Encode Separate Mitochondrial NADH Dehydrogenases Catalyzing the Oxidation of Cytosolic NADH

Cited by 280 publications

References 44 publications

Identification of AtNDI1, an Internal Non-Phosphorylating NAD(P)H Dehydrogenase in Arabidopsis Mitochondria

Identification of AtNDI1, an Internal Non-Phosphorylating NAD(P)H Dehydrogenase in Arabidopsis Mitochondria

The External Calcium-dependent NADPH Dehydrogenase from Neurospora crassa Mitochondria

SHAM‐sensitive alternative respiration in the xylose‐metabolizing yeast Pichia stipitis

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