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

  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},
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.



Biogenesis of mitochondria: the mitochondrial gene (aap1) coding for mitochondrial ATPase subunit 8 in Saccharomyces cerevisiae

Evidence is presented that the aap1 gene codes for a mitochondrially synthesized polypeptide associated with the mitochondrial ATPase complex.

Isolation, subunit composition, and site of synthesis of human cytochrome c oxidase.

It is concluded that human cytochrome c oxidase contains seven subunits, the three largest of which are synthesized on mitochondrial ribosomes, while the other four are synthesizing in the cytoplasm.

An analysis of the polypeptide composition of bovine heart mitochondrial NADH-ubiquinone oxidoreductase by two-dimensional polyacrylamide-gel electrophoresis.

Purified preparations of Complex I (NADH-ubiquinone oxidoreductase) from bovine heart mitochondria may be resolved into 26 polypeptides by two-dimensional analysis combining isoelectric focusing and

Drosophila melanogaster mitochondrial DNA, a novel organization and genetic code

Evidence is provided for a genetic code in which AGA codes for serine and the quadruplet ATAA is used in initiation of translation of Drosophila melanogaster mitochondrial DNA.

Identification of the polypeptides encoded in the ATPase 6 gene and in the unassigned reading frames 1 and 3 of human mtDNA.

The sizes of proteins 17, 12, and 24, as estimated from their electrophoretic mobilities, are compatible with their being the products of the ATPase 6 gene, URF1, and URF3, respectively.

Sequence and organization of the human mitochondrial genome

The complete sequence of the 16,569-base pair human mitochondrial genome is presented and shows extreme economy in that the genes have none or only a few noncoding bases between them, and in many cases the termination codons are not coded in the DNA but are created post-transcriptionally by polyadenylation of the mRNAs.

The organization of NADH dehydrogenase polypeptides in the inner mitochondrial membrane.

It is concluded that NADH dehydrogenase is asymmetrically organized across the inner mitochondrial membrane.

Purification and molecular and enzymic properties of mitochondrial NADH dehydrogenase.