Cloning and sequencing of a cDNA for human mitochondrial ubiquinone-binding protein of complex III

Suzuki, Hiroshi; Hosokawa, Yoshitaka; Toda, Hirofumi; Nishikimi, Morimitsu; Ozawa, Takayuki

doi:10.1016/s0006-291x(88)80941-0

Cited by 30 publications

(16 citation statements)

References 25 publications

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“…This enzymatic complex in bovine heart mitochondria consists of 11 different polypeptide subunits; subunit X is considered to play a role in the proper assembly of the cytochrome bc1 complex. In the human, ten subunits of this complex had already been identified and their primary structures determined (Islam et al 1994(Islam et al , 1997Duncan et al 1993Duncan et al , 1994aDuncan et al , 1994bAnderson et al 1981;Suzuki et al 1988;Hosokawa et al 1990;Ohta et al 1987). The human counterpart of bovine subunit X was the only component remaining to be identified.…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterization of a human cDNA encoding a protein homologous to the 7.2-kDa protein (subunit X) of bovine ubiquinol-cytochrome C reductase

et al. 2000

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Section: Discussionmentioning

confidence: 99%

Isolation and characterization of a human cDNA encoding a protein homologous to the 7.2-kDa protein (subunit X) of bovine ubiquinol-cytochrome C reductase

et al. 2000

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“…One of these ESTs, WI-7092, was developed from the 3Ј untranslated region of the mitochondrial ubiquinone-binding protein, a nuclear-encoded component of ubiquinol-cytochrome c oxidoreductase (33). Although this sequence appears to map to both Xp11.21 and to chromosome 8, RT-PCR analysis suggests that only the X chromosome locus is expressed (data not shown).…”

Section: Identification Of Expressed Sequencesmentioning

confidence: 99%

Chromosomal basis of X chromosome inactivation: Identification of a multigene domain in Xp11.21-p11.22 that escapes X inactivation

Miller

Willard

1998

Proc. Natl. Acad. Sci. U.S.A.

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A number of genes have been identified that escape mammalian X chromosome inactivation and are expressed from both active and inactive X chromosomes. The basis for escape from inactivation is unknown and, a priori, could be a result of local factors that act in a gene-specific manner or of chromosomal control elements that act regionally. Models invoking the latter predict that such genes should be clustered in specific domains on the X chromosome, rather than distributed at random along the length of the X. To distinguish between these possibilities, we have constructed a transcription map composed of at least 23 distinct expressed sequences in an Ϸ5.5-megabase region on the human X chromosome spanning Xp11.21-p11.22. The inactivation status of these transcribed sequences has been determined in a somatic cell hybrid system and correlated with the position of the genes on the physical map. Although the majority of transcribed sequences in this region are subject to X inactivation, eight expressed sequences (representing at least six different genes) escape inactivation, and all are localized to within a region of less than 370 kb. Genes located both distal and proximal to this cluster are subject to inactivation, thereby defining a unique multigene domain on the proximal short arm that is transcriptionally active on the inactive X chromosome.

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“…The 14-kD subunit from potato, yeast, and mammals has a net positive charge and is predicted to have a high helical content. As reported previously these helices have amphiphilic properties (Wakabayashi et al, 1985;Link et al, 1987;Suzuki et al, 1988) that might enable this hydrophilic subunit to interact with the mitochondrial membrane or with ubiquinol. The 14-kD protein lacks potential membrane-spanning helices and is, therefore, most likely anchored by proteinprotein interactions with other components of the bcj complex.…”

Section: Discussionmentioning

confidence: 67%

Molecular Features and Mitochondrial Import Pathway of the 14-Kilodalton Subunit of Cytochrome c Reductase from Potato

Braun

Schmitz

1995

Plant Physiol.

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The cytochrome c reductase complexes from fungi and mammals both contain a 14-kD protein (yeast, 14.4 kD; bovine, 13.4 kD) that does not directly participate in electron transfer but possibly is indirectly involved in the function of the complex and has a role in assembly of the multimeric enzyme. A subunit of comparable size was identified for the bc, complex of higher plants. The 14-kD protein from potato (Solanum tuberosum) was specifically separated from the isolated protein complex in the presence of 6 M urea and is, therefore, assumed to be a peripheral component. Direct sequence analysis of the proteins from potato and wheat (Triticum aestivum) and isolation of corresponding cDNA clones for the subunit from potato revealed clear similaríty to the equivalent proteins from yeast and bovine. The wheat 14-kD protein seems to occur in two isoforms. The 14-kD protein from plants is very hydrophilic, has a characteristic charge distribution, and contains no potential membrane-spanning helices. In vitro import of the radiolabeled 14-kD protein from potato into isolated mitochondria depends on the membrane potential across the inner mitochondrial membrane. The protein seems to lack a cleavable mitochondrial presequence, because it is not processed upon translocation. Possible intramolecular regions involved in targeting of the 14-kD protein to plant mitochondria are discussed.The mitochondriaI bc, complex (EC 1.10.2.2.) is the middle segment of the respiratory chain and catalyzes the reduction of Cyt c by the oxidation of ubiquinol. Coupled with this reaction it contributes to the chemiosmotic gradient across the inner mitochondrial membrane by translocating protons from the matrix to the intermembrane space. In fungi and mammals the Cyt c reductase is an oligomeric protein complex comprising 9 to 11 subunits (reviewed by Trumpower, 1990; Bechmann et al., 1992): two large "core" proteins, three respiratory proteins that directly participate in electron transport (Cyt b, Cyt cl, and the "Rieske" iron sulfur protein), and four to six small proteins with molecular masses of less than 20 kD. Since bacterial bc, complexes that contain only the respiratory subunits have the same activity as the eukaryotic enzymes (Trumpower, 19901, the role of the supplementary subunits is not quite understood. One of them is the bovine subunit VI (13.4 kD), which was shown to be similar to subunit VI1 This work was supported by the Deutsche Forschungsgemein-

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Cloning and sequencing of a cDNA for human mitochondrial ubiquinone-binding protein of complex III

Cited by 30 publications

References 25 publications

Isolation and characterization of a human cDNA encoding a protein homologous to the 7.2-kDa protein (subunit X) of bovine ubiquinol-cytochrome C reductase

Isolation and characterization of a human cDNA encoding a protein homologous to the 7.2-kDa protein (subunit X) of bovine ubiquinol-cytochrome C reductase

Chromosomal basis of X chromosome inactivation: Identification of a multigene domain in Xp11.21-p11.22 that escapes X inactivation

Molecular Features and Mitochondrial Import Pathway of the 14-Kilodalton Subunit of Cytochrome c Reductase from Potato

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