Analysis of the Iron‐Sulfur Clusters Within the Complex I (NADH: Ubiquinone Oxidoreductase) Isolated from Potato Tuber Mitochondria

Lin, Tse‐I; Sled, Vladimir D.; Ohnishi, Tomo̧ko; Brennicke, Axel; Grohmann, Lutz

doi:10.1111/j.1432-1033.1995.1032g.x

Cited by 3 publications

(1 citation statement)

References 37 publications

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“…For wheat grown at OT, the specific activity of NADH dehydrogenases did not differ significantly between Mace and EGA2248, determined as 4.89 ± 0.25 and 5.49 ± 0.46 μmol min −1 mg −1 protein, respectively (Figure 3c). These values are in-line with previously reported specific activity of NADH dehydrogenases from plants (Soole et al 1992, Serge et al 1993, Lin et al 1995). When subjected to HT, the activity from mitochondria isolated from Mace increased significantly to 7.39 ± 0.39 μmol min − 1 mg −1 protein, whereas in the heat sensitive wheat EGA2248 there was a significant decrease in specific activity, to 4.09 ± 0.15 μmol min −1 mg −1 protein.…”

Section: Resultssupporting

confidence: 93%

Mitochondrial Complex I activity is inhibited by changes in the abundance of phosphatidylinositol and phosphatidylserine in wheat plants exposed to high temperatures

Malone

Rupasinghe

Roessner

et al. 2023

Preprint

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We evaluated changes to the lipo-protein network of wheat mitochondria of differing heat tolerance in response to heat shock.Using targeted mass spectrometry, candidate transitions were selected to quantify changes in membrane lipids and the embedded protein components of the electron transport chain, which play a vital role in maintaining respiration.A significant increase in phosphatidylserine was exclusive to the mitochondria of the heat-tolerant wheat cultivar. In the absence of this, the heat-sensitive cultivar displayed a reduced Complex I activity. The minor membrane constituent phosphatidylserine plays a role in conveying thermotolerance, making this membrane lipid a focal point for the breeding of future heat tolerant crops.

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Section: Resultssupporting

confidence: 93%

Mitochondrial Complex I activity is inhibited by changes in the abundance of phosphatidylinositol and phosphatidylserine in wheat plants exposed to high temperatures

Malone

Rupasinghe

Roessner

et al. 2023

Preprint

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The plant mitochondrial 22 kDa (PSST) subunit of respiratory chain complex I is encoded by a nuclear gene with enhanced transcript levels in flowers

1996

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Genes for subunits of respiratory chain complex I are found in mitochondrial, plastid and/or nuclear genomes with varying distributions in the diverse eukaryotic species. The intrinsic PSST subunit of complex I is a mitochondrially encoded protein in Paramecium but is specified by a nuclear gene in animals. In plants to date only the homologous plastid encoded NDH-K gene product has been described. The analogous plant mitochondrial protein is now identified as the 22 kDa complex I subunit and found to be encoded in the nuclear genome of Arabidopsis and potato. The cDNA sequences of clones isolated from both plants are 79% identical in the conserved coding region, while the 5' parts of the reading frames specifying the N-terminal presequences for mitochondrial import differ significantly. The expression of the genes examined in different organs of both plants by Northern blot analysis shows elevated steady-state mRNA levels in flowers. Hence, expression of the gene appears to be organ-specifically regulated by its transcription rate and/or mRNA stability. A 1.6 kb long genomic DNA sequence of Arabidopsis upstream of the transcribed gene region encoding the PSST subunit in Arabidopsis contains several putative promoter sequence motifs. The results are discussed with regard to the appearance of a nuclearly integrated, former mitochondrial gene.

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Molecular Characterisation of the 76 kDa Iron-Sulphur Protein Subunit of Potato Mitochondrial Complex I

Rasmusson¹,

Heiser²,

Irrgang³

et al. 1998

Plant and Cell Physiology

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Genes encoding subunits of complex I (EC 1.6.5.3) of the mitochondrial respiratory chain vary in their locations between the mitochondrial and nuclear genomes in different organisms, whereas genes for a homologous multisubunit complex in chloroplasts have to date only been found on the plastid genome. In potato (Solanum tuberosum L.), the gene coding for the mitochondrial 76 kDa iron-sulphur protein is identified in the nuclear genome. The gene is transcribed into polyadenylated mRNA which is most abundant in flowers, and more frequent in tubers than in leaves. The amino acid sequence is well conserved relative to the nuclear-encoded 75 kDa and 78 kDa subunits of Bos taurus and Neurospora crassa, respectively, and to the Paracoccus denitrificans homologue, most prominently in the region presumed to carry the iron-sulphur clusters. Polyclonal antibodies directed against the 78 kDa complex I subunit of N. crassa recognise the 76 kDa polypeptide in potato mitochondrial complex I, and additionally a polypeptide of 75 kDa in solubilised stroma thylakoids from spinach chloroplasts. The 32 amino acid residues long presequence of the potato mitochondrial 76 kDa complex I subunit targets the precursor polypeptide into isolated potato mitochondria but not into isolated chloroplasts. These results suggest that chloroplast stroma thylakoids contain a protein similar in size and antigenicity to, but genetically distinct from, the mitochondrial subunit.

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Analysis of the Iron‐Sulfur Clusters Within the Complex I (NADH: Ubiquinone Oxidoreductase) Isolated from Potato Tuber Mitochondria

Cited by 3 publications

References 37 publications

Mitochondrial Complex I activity is inhibited by changes in the abundance of phosphatidylinositol and phosphatidylserine in wheat plants exposed to high temperatures

Mitochondrial Complex I activity is inhibited by changes in the abundance of phosphatidylinositol and phosphatidylserine in wheat plants exposed to high temperatures

The plant mitochondrial 22 kDa (PSST) subunit of respiratory chain complex I is encoded by a nuclear gene with enhanced transcript levels in flowers

Molecular Characterisation of the 76 kDa Iron-Sulphur Protein Subunit of Potato Mitochondrial Complex I

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