Nucleotide sequence of the cytochrome B gene and adjacent regions from rat liver mitochondrial DNA

Görtz, Gabriele; Feldmann, Horst

doi:10.1007/bf00391810

Cited by 15 publications

(2 citation statements)

References 18 publications

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“…Chloroplast genomes contain genes that encode homologues for the seven components of complex I encoded in vertebrate and invertebrate mitochondria (Anderson ct al., 1981(Anderson ct al., , 1982Bibb ct al., 1981; Gortz & Feldmann, 1982;Grosskopf & Feldmann, 1981;Koike ct al., 1982;Roe ct al., 1985;Clary & Wolstcnholmc, 1985; Canatatore et al" 1987; Wolstenholme ct al., 1987;Himcnoctal., 1987;Jacobs et al, 1988). In both liverwort and tobacco, four of these homologues are found in a gene cluster with the homologues of the 49and 23-kDa subunits (Fearnley et al, 1989;Dupuis et al, 1991).…”

Section: Resultsmentioning

confidence: 99%

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

Pilkington

Skehel²,

Walker³

1991

Biochemistry

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In cattle, 7 of the 30 or more subunits of the respiratory enzyme NADH:ubiquinone reductase (complex I) are encoded in mitochondrial DNA, and potential genes (open reading frames, orfs) for related proteins are found in the chloroplast genomes of Marchantia polymorpha and Nicotiana tabacum. Homologues of the nuclear-coded 49- and 23-kDa subunits are also coded in chloroplast DNA, and these orfs are clustered with four of the homologues of the mammalian mitochondrial genes. These findings have been taken to indicate that chloroplasts contain a relative of complex I. The present work provides further support. The 30-kDa subunit of the bovine enzyme is a component of the iron-sulfur protein fraction. Partial protein sequences have been determined, and synthetic oligonucleotide mixtures based on them have been employed as hybridization probes to identify cognate cDNA clones from a bovine library. Their sequences encode the mitochondrial import precursor of the 30-kDa subunit. The mature protein of 228 amino acids contains a segment of 57 amino acids which is closely related to parts of proteins encoded in orfs 169 and 158 in the chloroplast genomes of M. polymorpha and N. tabacum. Moreover, the chloroplast orfs are found near homologues of the mammalian mitochondrial genes for subunit ND3. Therefore, the plant chloroplast genomes have at least two separate clusters of potential genes encoding homologues of subunits of mitochondrial complex I. The bovine 30-kDa subunit has no extensive sequences of hydrophobic amino acids that could be folded into membrane-spanning alpha-helices, and although it contains two cysteine residues, there is no clear evidence in the sequence that it is an iron-sulfur protein.

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Section: Resultsmentioning

confidence: 99%

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

Pilkington

Skehel²,

Walker³

1991

Biochemistry

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“…It is not uncommon for the cytb of vertebrates to lack or have incomplete stop codons (e.g. Görtz & Feldmann 1982, Murray et al 1994, McKnight & Shaffer 1997, Glenn et al 2002. The cytb gene usually encodes 380 amino acids in vertebrates, but deviations from this number are not unusual.…”

Section: Discussionmentioning

confidence: 99%

Mitochondrial genomes for the Afrobatrachian Hyperolius substriatus (Anura: Hyperoliidae) obtained from museum specimens

Bittencourt-Silva,

Kamouyiaros,

Hartigan

et al. 2024

Journal of Vertebrate Biology

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Mass spectrometric characterization of mitochondrial electron transport complexes: subunits of the rat heart ubiquinol–cytochrome c reductase

2003

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Complex III of the mitochondrial electron transport chain, ubiquinol-cytochrome c reductase, was isolated by blue native polyacrylamide gel electrophoresis. Ten of the 11 polypeptides present in this complex were detected directly by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) following electroelution of the active complex. Tryptic and chymotryptic digestion of the complex permit the identification of specific peptides from all of the protein subunits with 70% coverage of the 250 kDa complex. The mass of all 11 proteins was confirmed by second dimension Tricine sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and elution of the separated polypeptides. Additionally, the identity of the core I, core II, cytochrome c and the Rieske iron-sulfur protein were confirmed by liquid chromatography/tandem mass spectrometry (LC/MS/MS) characterization of the peptides generated by in-gel trypsin digestion of the SDS-PAGE separated proteins. The methodology demonstrated for analyzing this membrane-bound electron transport complex should be applicable to other membrane complexes, particularly the other mitochondrial electron transport complexes. The MS analysis of the peptides obtained by in-gel digestion of the intact complex permits the simultaneous characterization of the native proteins and modifications that contribute to mitochondrial deficits that have been implicated as contributing to pathological conditions.

show abstract

Nucleotide sequence of the cytochrome B gene and adjacent regions from rat liver mitochondrial DNA

Cited by 15 publications

References 18 publications

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

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

Mitochondrial genomes for the Afrobatrachian Hyperolius substriatus (Anura: Hyperoliidae) obtained from museum specimens

Mass spectrometric characterization of mitochondrial electron transport complexes: subunits of the rat heart ubiquinol–cytochrome c reductase

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