Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase

@article{Chomyn1985SixUR,
  title={Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase},
  author={Anne Chomyn and Paolo Mariottini and Michael W. J. Cleeter and C. Ian Ragan and Akemi Matsuno-Yagi and Youssef Hatefi and Russell F. Doolittle and Giuseppe Attardi},
  journal={Nature},
  year={1985},
  volume={314},
  pages={592-597}
}
The products of six unidentified reading frames of human mitochondrial DNA are precipitated from a mitochondrial lysate by antibodies against highly purified native beef heart NADH-ubiqutnone oxidoreductase (complex I). These products are enriched greatly in a human submitochondrial fraction enriched in NADH-Q1 and NADH-K3Fe(CN)6 oxidoreductase activities. We conclude that the six reading frames encode components of the respiratory-chain NADH dehydrogenase. 

URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit.

Almost 60% of the protein coding capacity of mammalian mitochondrial DNA is utilized for the assembly of the first enzyme complex of the respiratory chain, dramatizes the variability in gene content of different mitochondrial genomes.

cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed.

All currently known 41 proteins of human NADH:ubiquinone oxidoreductase have been characterized and reported in literature, which enables more complete mutational analysis studies of isolated complex I-deficient patients.

The 30-kilodalton subunit of bovine mitochondrial complex I is homologous to a protein coded in chloroplast DNA.

The present work provides further support to indicate that chloroplasts contain a relative of mitochondrial complex I, where the 30-kDa subunit of the bovine enzyme is a component of the iron-sulfur protein fraction.

A homologue of a nuclear-coded iron-sulfur protein subunit of bovine mitochondrial complex I is encoded in chloroplast genomes.

The chloroplast genomes of Marchantia polymorpha, Nicotiana tabacum, and Oryza sativa contain open reading frames (ORFs or potential genes) encoding homologues of some of the subunits of mitochondrial NADH:ubiquinone oxidoreductase, showing the presence in chloroplasts of an enzyme related to complex I, possibly an NAD(P)H:plastoquinone oxidationase, participating in chlororespiration.

cDNA of the 24 kDa subunit of the bovine respiratory chain NADH dehydrogenase: high sequence conservation in mammals and tissue-specific and growth-dependent expression

A comparison of the nucleotide and amino acid sequences of the bovine 24 kDa subunit with those recently determined for the rat homologue has shown that this nuclear-encoded subunit of an OXPHOS complex has diverged in these two species much less than the mitochondrial DNA- encoded subunits of the same enzyme complex, and also less than a set of available non-mitochondrial nuclear DNA-coded proteins.

Active transcription of the pseudogene for subunit 7 of the NADH dehydrogenase in Marchantia polymorpha mitochondria

Genomic DNA blot analysis and RNA blot analysis suggest that a structurally related nuclear gene encodes the mitochondrial ND7 polypeptide, which implies that this ψnad7 is a relic of a gene transfer event from the mitochondrial genome into the nuclear genome during mitochondrial evolution in M. polymorpha.

cDNA sequence and chromosomal localization of the remaining three human nuclear encoded iron sulphur protein (IP) subunits of complex I: the human IP fraction is completed.

The cloned cDNA of three remaining human NADH:ubiquinone oxidoreductase subunits of this IP fraction contain a highly conserved protein kinase C phosphorylation site and make them strong candidates for future mutation detection studies in enzymatic complex I-deficient patients.

The mtDNA‐encoded ND6 subunit of mitochondrial NADH dehydrogenase is essential for the assembly of the membrane arm and the respiratory function of the enzyme

Observations provide the first evidence of the essential role of the ND6 subunit in the respiratory function of Complex I and give some insights into the pathogenic mechanism of the known disease‐causing ND6 gene mutations.
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