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

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 bc1 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 similarity 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.

[1]  H. Braun,et al.  Molecular structure of the 8.0 kDa subunit of cytochrome-c reductase from potato and its Δψ-dependent import into isolated mitochondria , 1995 .

[2]  L. Grivell,et al.  The C-terminus of the 14-kDa subunit of ubiquinol-cytochrome-c oxidoreductase of the yeast Saccharomyces cerevisiae is involved in the assembly of a functional enzyme. , 1994, European journal of biochemistry.

[3]  M. Ryan,et al.  Isolation of a cDNA clone specifying rat chaperonin 10, a stress‐inducible mitochondrial matrix protein synthesised without a cleavable presequence , 1994, FEBS letters.

[4]  H. Braun,et al.  Characterization of the bifunctional cytochrome c reductase-processing peptidase complex from potato mitochondria. , 1993, The Journal of biological chemistry.

[5]  Chang-an Yu,et al.  Mitochondrial ubiquinol-cytochromec reductase complex: Crystallization and protein: Ubiquinone interaction , 1993, Journal of bioenergetics and biomembranes.

[6]  B. Trumpower,et al.  Isolation and characterization of COX12, the nuclear gene for a previously unrecognized subunit of Saccharomyces cerevisiae cytochrome c oxidase. , 1992, The Journal of biological chemistry.

[7]  H. Braun,et al.  Affinity purification of cytochrome c reductase from potato mitochondria. , 1992, European journal of biochemistry.

[8]  H. Braun,et al.  The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain. , 1992, The EMBO journal.

[9]  J. Walker,et al.  Sequences of 20 subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria. Application of a novel strategy for sequencing proteins using the polymerase chain reaction. , 1992, Journal of molecular biology.

[10]  S. Usui,et al.  Immunochemical study of subunit VI (Mr 13,400) of mitochondrial ubiquinol-cytochrome c reductase. , 1991, Archives of biochemistry and biophysics.

[11]  M. Kitakawa,et al.  Extended N‐terminal sequencing of proteins of the large ribosomal subunit from yeast mitochondria , 1991, FEBS letters.

[12]  E. Berry,et al.  Ubiquinol-cytochrome c oxidoreductase of higher plants. Isolation and characterization of the bc1 complex from potato tuber mitochondria. , 1991, The Journal of biological chemistry.

[13]  S. Papa,et al.  Structural and functional characteristics of polypeptide subunits of the bovine heart ubiquinol--cytochrome-c reductase complex. , 1991, European journal of biochemistry.

[14]  S. Ferguson-Miller,et al.  Structurally unique plant cytochrome c oxidase isolated from wheat germ, a rich source of plant mitochondrial enzymes. , 1990, Biochemistry.

[15]  J. Berden,et al.  Membrane topography of the subunits of ubiquinol-cytochrome-c oxidoreductase of Saccharomyces cerevisiae. The 14-kDa and the 11-kDa subunits face opposite sides of the mitochondrial inner membrane. , 1990, European journal of biochemistry.

[16]  L. Grivell.  Nucleo-mitochondrial interactions in yeast mitochondrial biogenesis. , 1989, European journal of biochemistry.

[17]  Y. Hosokawa,et al.  Isolation of a single nuclear gene encoding human ubiquinone-binding protein in complex III of mitochondrial respiratory chain. , 1989, Biochemical and biophysical research communications.

[18]  S. Papa,et al.  Effect of papain digestion on polypeptide subunits and electron-transfer pathways in mitochondrial b-c1 complex. , 1989, European journal of biochemistry.

[19]  Y. Hosokawa,et al.  Cloning and sequencing of a cDNA for human mitochondrial ubiquinone-binding protein of complex III. , 1988, Biochemical and biophysical research communications.

[20]  D. González-Halphen,et al.  Subunit arrangement in beef heart complex III. , 1988, Biochemistry.

[21]  H. Schägger,et al.  Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. , 1987, Analytical biochemistry.

[22]  D. S. Beattie,et al.  Subunit VII, the ubiquinone-binding protein, of the cytochrome b-c1 complex of yeast mitochondria is involved in electron transport at center o and faces the matrix side of the membrane. , 1987, The Journal of biological chemistry.

[23]  H. Schägger,et al.  Structural Analysis of the BC1 Complex from Beef Heart Mitochondria by the Sided Hydropathy Plot and by Comparison with other BC Complexes , 1987 .

[24]  Y. Shimomura,et al.  Cell-free synthesis of ubiquinone-binding protein of mitochondrial cytochrome bc1 complex. , 1986, Biochemical and biophysical research communications.

[25]  L. Yu,et al.  Identification of ubiquinone-binding proteins in yeast mitochondrial ubiquinol-cytochrome c reductase using an azido-ubiquinone derivative. , 1986, Biochimica et biophysica acta.

[26]  H. Schägger,et al.  Isolation of the eleven protein subunits of the bc1 complex from beef heart. , 1986, Methods in enzymology.

[27]  H. Weiss,et al.  Reconstitution of ubiquinol-cytochrome-c reductase from Neurospora mitochondria with regard to subunits I and II. , 1986, Methods in enzymology.

[28]  S. Wakabayashi,et al.  Complete amino acid sequence of the ubiquinone binding protein (QP-C), a protein similar to the 14,000-dalton subunit of the yeast ubiquinol-cytochrome c reductase complex. , 1985, Journal of Biological Chemistry.

[29]  J. Devereux,et al.  A comprehensive set of sequence analysis programs for the VAX , 1984, Nucleic Acids Res..

[30]  L. Grivell,et al.  The biosynthesis of the ubiquinol-cytochrome c reductase complex in yeast. DNA sequence analysis of the nuclear gene coding for the 14-kDa subunit. , 1984, European journal of biochemistry.

[31]  L. Grivell,et al.  Biosynthesis of the ubiquinol‐cytochrome c reductase complex in yeast. Discoordinate synthesis of the 11‐kd subunit in response to increased gene copy number. , 1983, The EMBO journal.

[32]  L. Yu,et al.  The interaction of arylazido ubiquinone derivative with mitochondrial ubiquinol-cytochrome c reductase. , 1982, The Journal of biological chemistry.

[33]  W. Neupert,et al.  Requirement of a membrane potential for the posttranslational transfer of proteins into mitochondria. , 1982, European journal of biochemistry.

[34]  H. Weiss,et al.  Isolation of mitochondrial succinate: ubiquinone reductase, cytochrome c reductase and cytochrome c oxidase from Neurospora crassa using nonionic detergent. , 1979, European journal of biochemistry.

[35]  H. Weiss,et al.  Isolation of a multiprotein complex containing cytochrome b and c1 from Neurospora crassa mitochondria by affinity chromatography on immobilized cytochrome c. Difference in the binding between ferricytochrome c and ferrocytochrome c to the multiprotein complex. , 1978, European journal of biochemistry.

[36]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[37]  I..,et al.  Isolation and Characterization of COX 12 , the Nuclear Gene for a Previously Unrecognized Subunit of Saccharomyces cerevisiae Cytochrome c Oxidase * , 2022 .