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Volumn 37, Issue 9, 1999, Pages 629-643

The mitochondrial respiratory chain and ATP synthase complexes: Composition, structure and mutational studies

Author keywords

Mitochondria; mtDNA; Nuclear mitochondrial interactions; Respiratory chain complexes; Respiratory mutants

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE SYNTHASE; CATTLE; CYTOPLASMIC MALE STERILITY; ENZYME STRUCTURE; ENZYME SYNTHESIS; HOMO SAPIENS; MEMBRANE POTENTIAL; MITOCHONDRIAL GENETICS; NEUROSPORA CRASSA; PHENOTYPE; PROTEIN PHOSPHORYLATION; RIBOSOME; SACCHAROMYCES CEREVISIAE;

EID: 0032857089     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0981-9428(00)80093-5     Document Type: Review
Times cited : (30)

References (80)
  • 1
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams J.P., Leslie A.G.W., Lutter R., Walker J.E. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature. 370:1994;621-628.
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.W.2    Lutter, R.3    Walker, J.E.4
  • 2
    • 0030596417 scopus 로고    scopus 로고
    • Separate sexes and the mitochondrial theory of ageing
    • Allen J.F. Separate sexes and the mitochondrial theory of ageing. J. Theor. Biol. 180:1996;135-140.
    • (1996) J. Theor. Biol. , vol.180 , pp. 135-140
    • Allen, J.F.1
  • 3
    • 0028304827 scopus 로고
    • Disruption of the gene coding for the 21.3 kDa subunit of the peripheral arm of complex I from Neurospora crassa
    • Alves P.C., Videira A. Disruption of the gene coding for the 21.3 kDa subunit of the peripheral arm of complex I from Neurospora crassa. J. Mol. Biol. 269:1994;7777-7784.
    • (1994) J. Mol. Biol. , vol.269 , pp. 7777-7784
    • Alves, P.C.1    Videira, A.2
  • 4
    • 0029808314 scopus 로고    scopus 로고
    • ATP synthase of yeast mitochondria. Isolation of subunit h and disruption of the ATP14 gene
    • Arselin G., Vaillier J., Graves P.V., Velours J. ATP synthase of yeast mitochondria. Isolation of subunit h and disruption of the ATP14 gene. J. Biol. Chem. 271:1996;20284-20290.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20284-20290
    • Arselin, G.1    Vaillier, J.2    Graves, P.V.3    Velours, J.4
  • 5
    • 6844240206 scopus 로고    scopus 로고
    • Promoter analysis of the human succinate dehydrogenase iron-protein gene. Both nuclear respiratory factors NRF-1 and NRF-2 are required
    • Au H.C., Scheffler E. Promoter analysis of the human succinate dehydrogenase iron-protein gene. Both nuclear respiratory factors NRF-1 and NRF-2 are required. Eur. J. Biochem. 251:1998;164-174.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 164-174
    • Au, H.C.1    Scheffler, E.2
  • 6
    • 0027374223 scopus 로고
    • Expression of human cytochrome c oxidase subunits during fetal development
    • Bonne G., Seibel P., Possekel S., Marsac C., Kadenbach B. Expression of human cytochrome c oxidase subunits during fetal development. Eur. J. Biochem. 217:1993;1099-1107.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 1099-1107
    • Bonne, G.1    Seibel, P.2    Possekel, S.3    Marsac, C.4    Kadenbach, B.5
  • 7
    • 0032570865 scopus 로고    scopus 로고
    • The respiratory chain in yeast behaves as a single functional unit
    • Boumans H., Grivell L.A., Berden J.A. The respiratory chain in yeast behaves as a single functional unit. J. Biol. Chem. 273:1998;4872-4877.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4872-4877
    • Boumans, H.1    Grivell, L.A.2    Berden, J.A.3
  • 8
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase - A splendid molecular machine
    • Boyer P.D. The ATP synthase - A splendid molecular machine. Annu. Rev. Biochem. 66:1997;717-749.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 9
    • 0030917335 scopus 로고    scopus 로고
    • The nuclear ABC1 gene is essential for the correct conformation and functioning of the cytochrome bc1 complex and the neighbouring complexes II and IV in the mitochondrial respiratory chain
    • Brasseur G., Tron P., Dujardin G., Slonimski P., Brivet-Chevillotte P. The nuclear ABC1 gene is essential for the correct conformation and functioning of the cytochrome bc1 complex and the neighbouring complexes II and IV in the mitochondrial respiratory chain. Eur. J. Biochem. 246:1997;103-111.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 103-111
    • Brasseur, G.1    Tron, P.2    Dujardin, G.3    Slonimski, P.4    Brivet-Chevillotte, P.5
  • 10
    • 0028857080 scopus 로고
    • The bifunctional cytochrome c reductase/processing peptidase complex from plant mitochondria
    • Braun H.P., Schmitz U.K. The bifunctional cytochrome c reductase/processing peptidase complex from plant mitochondria. J. Bioenerg. Biomembr. 27:1995;423-436.
    • (1995) J. Bioenerg. Biomembr. , vol.27 , pp. 423-436
    • Braun, H.P.1    Schmitz, U.K.2
  • 11
    • 0026681174 scopus 로고
    • A single amino-acid change in the iron-sulphur protein subunit of succinate dehydrogenase confers resistance to carboxin in Ustilago maydis
    • Broomfield P.L.E., Hargreaves J.A. A single amino-acid change in the iron-sulphur protein subunit of succinate dehydrogenase confers resistance to carboxin in Ustilago maydis. Curr. Genet. 22:1992;117-121.
    • (1992) Curr. Genet. , vol.22 , pp. 117-121
    • Broomfield, P.L.E.1    Hargreaves, J.A.2
  • 12
    • 0028275113 scopus 로고
    • Isolation and characterization of the Saccharomyces cerevisiae SDH4 gene encoding a membrane anchor subunit of succinate dehydrogenase
    • Bullis B.L., Lemire B.D. Isolation and characterization of the Saccharomyces cerevisiae SDH4 gene encoding a membrane anchor subunit of succinate dehydrogenase. J. Biol. Chem. 269:1994;6543-6549.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6543-6549
    • Bullis, B.L.1    Lemire, B.D.2
  • 13
    • 0030002977 scopus 로고    scopus 로고
    • Genes encoding the same three subunits of respiratory complex II are present in the mitochondrial DNA of two phylogenetically distant eucaryotes
    • Burger G., Lang B.F., Reith M., Gray M.W. Genes encoding the same three subunits of respiratory complex II are present in the mitochondrial DNA of two phylogenetically distant eucaryotes. Proc. Natl. Acad. Sci. USA. 93:1996;2328-2332.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2328-2332
    • Burger, G.1    Lang, B.F.2    Reith, M.3    Gray, M.W.4
  • 14
    • 0032481317 scopus 로고    scopus 로고
    • Identification of a functional respiratory complex in chloroplasts through analysis of tobacco mutants containing disrupted plastid ndh genes
    • Burrows P.A., Sazanov L.A., Svab Z., Maliga P., Nixon P.J. Identification of a functional respiratory complex in chloroplasts through analysis of tobacco mutants containing disrupted plastid ndh genes. EMBO J. 17:1998;868-876.
    • (1998) EMBO J. , vol.17 , pp. 868-876
    • Burrows, P.A.1    Sazanov, L.A.2    Svab, Z.3    Maliga, P.4    Nixon, P.J.5
  • 15
    • 0025322981 scopus 로고
    • Structure and function of cytochrome c oxidase
    • Capaldi R.A. Structure and function of cytochrome c oxidase. Annu. Rev. Biochem. 59:1990;569-596.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 569-596
    • Capaldi, R.A.1
  • 16
    • 0027157999 scopus 로고
    • Random mutant generation and its utility in uncovering structural and functional features of cytochrome b in Saccharomyces cerevisiae
    • Colson A.M. Random mutant generation and its utility in uncovering structural and functional features of cytochrome b in Saccharomyces cerevisiae. J. Bioenerg. Biomembr. 3:1993;211-220.
    • (1993) J. Bioenerg. Biomembr. , vol.3 , pp. 211-220
    • Colson, A.M.1
  • 17
    • 0028302287 scopus 로고
    • Structure and regulation of SDH3, the yeast gene encoding the cytochrome b560 subunit of respiratory complex II
    • Daignan-Fornier B., Valens M., Lemire B.D., Bolotin-Fukuhara M. Structure and regulation of SDH3, the yeast gene encoding the cytochrome b560 subunit of respiratory complex II. J. Biol. Chem. 269:1994;15469-15472.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15469-15472
    • Daignan-Fornier, B.1    Valens, M.2    Lemire, B.D.3    Bolotin-Fukuhara, M.4
  • 19
    • 0029658688 scopus 로고    scopus 로고
    • The F1FO-type ATP synthase of bacteria : Structure and function of the FO complex
    • Deckers-Hebestreit G., Altendorf K. The F1FO-type ATP synthase of bacteria : structure and function of the FO complex. Annu. Rev. Microbiol. 50:1996;791-824.
    • (1996) Annu. Rev. Microbiol. , vol.50 , pp. 791-824
    • Deckers-Hebestreit, G.1    Altendorf, K.2
  • 20
    • 0027318751 scopus 로고
    • Specific mitochondrial proteins in pollen: Presence of an additional ATP synthase b subunit
    • De Paepe R., Forchioni A., Chétrit P., Vedel F. Specific mitochondrial proteins in pollen: presence of an additional ATP synthase b subunit. Proc. Natl. Acad. Sci. USA. 90:1993;5934-5938.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5934-5938
    • De Paepe, R.1    Forchioni, A.2    Chétrit, P.3    Vedel, F.4
  • 21
    • 0022704076 scopus 로고
    • The E35 stopper mutant of Neurospora crassa: Precise localization of deletion endpoints in mitochondrial DNA and evidence that the deleted DNA codes for a subunit of NADH dehydrogenase
    • de Vries H., Alzner-De Weerd B., Breitenberger C.A., Chang D.D., de Jonge J.C., RajBhandary U.L. The E35 stopper mutant of Neurospora crassa: precise localization of deletion endpoints in mitochondrial DNA and evidence that the deleted DNA codes for a subunit of NADH dehydrogenase. EMBO J. 5:1986;779-785.
    • (1986) EMBO J. , vol.5 , pp. 779-785
    • De Vries, H.1    Alzner-De Weerd, B.2    Breitenberger, C.A.3    Chang, D.D.4    De Jonge, J.C.5    Rajbhandary, U.L.6
  • 22
    • 0024288671 scopus 로고
    • Purification and characterization of a rotenone-insensitive NADH:Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae
    • de Vries S., Grivell L.A. Purification and characterization of a rotenone-insensitive NADH:Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae. Eur. J. Biochem. 176:1988;377-384.
    • (1988) Eur. J. Biochem. , vol.176 , pp. 377-384
    • De Vries, S.1    Grivell, L.A.2
  • 24
    • 0030990662 scopus 로고    scopus 로고
    • - yeast cells by a lack of assembly of the catalytic factor F1
    • - yeast cells by a lack of assembly of the catalytic factor F1. Eur. J. Biochem. 245:1997;813-818.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 813-818
    • Giraud, M.F.1    Velours, J.2
  • 25
    • 0026323440 scopus 로고
    • Import of proteins into mitochondria
    • Glick B., Schatz G. Import of proteins into mitochondria. Annu. Rev. Genet. 25:1991;21-44.
    • (1991) Annu. Rev. Genet. , vol.25 , pp. 21-44
    • Glick, B.1    Schatz, G.2
  • 26
    • 0027073347 scopus 로고
    • The endosymbiont hypothesis revisited in mitochondrial genomes
    • Gray M.W. The endosymbiont hypothesis revisited in mitochondrial genomes. Int. Rev. Cytol. 141:1992;233-357.
    • (1992) Int. Rev. Cytol. , vol.141 , pp. 233-357
    • Gray, M.W.1
  • 27
    • 0031004868 scopus 로고    scopus 로고
    • Nuclear genes for cytochrome c oxidase
    • Grossman L.I., Lomax M.I. Nuclear genes for cytochrome c oxidase. Biochim. Biophys. Acta. 1352:1997;174-192.
    • (1997) Biochim. Biophys. Acta , vol.1352 , pp. 174-192
    • Grossman, L.I.1    Lomax, M.I.2
  • 28
    • 0032512616 scopus 로고    scopus 로고
    • Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (Complex I)
    • Guénebaut V., Schlitt A., Weiss H., Leonard K., Friedrich T. Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (Complex I). J. Mol. Biol. 276:1998;105-112.
    • (1998) J. Mol. Biol. , vol.276 , pp. 105-112
    • Guénebaut, V.1    Schlitt, A.2    Weiss, H.3    Leonard, K.4    Friedrich, T.5
  • 29
    • 0031592480 scopus 로고    scopus 로고
    • Three-dimensional structure of NADH-dehydrogenase from Neurospora crassa by electron microscopy and conical tilt reconstruction
    • Guénebaut V., Vincentelli R., Mills D., Weiss H., Leonard K.R. Three-dimensional structure of NADH-dehydrogenase from Neurospora crassa by electron microscopy and conical tilt reconstruction. J. Mol. Biol. 265:1997;409-418.
    • (1997) J. Mol. Biol. , vol.265 , pp. 409-418
    • Guénebaut, V.1    Vincentelli, R.2    Mills, D.3    Weiss, H.4    Leonard, K.R.5
  • 30
    • 0342437206 scopus 로고    scopus 로고
    • In the Nicotiana sylvestris CMSII mutant, a recombination-mediated change 5' to the first exon of the mitochondrial nad1 gene is associated to lack of the NADH-ubiquinone oxidoreductase (complex I) NAD1 subunit
    • Gutierres S., Combettes B., De Paepe R., Mirande M., Lelandais C., Vedel F., Chétrit P. In the Nicotiana sylvestris CMSII mutant, a recombination-mediated change 5' to the first exon of the mitochondrial nad1 gene is associated to lack of the NADH-ubiquinone oxidoreductase (complex I) NAD1 subunit. Eur. J. Biochem. 261:1999;361-370.
    • (1999) Eur. J. Biochem. , vol.261 , pp. 361-370
    • Gutierres, S.1    Combettes, B.2    De Paepe, R.3    Mirande, M.4    Lelandais, C.5    Vedel, F.6    Chétrit, P.7
  • 32
    • 0001938909 scopus 로고    scopus 로고
    • Plant organelle gene expression: Altered by RNA editing
    • Hanson M.R., Sutton C.A., Lu B. Plant organelle gene expression: altered by RNA editing. Trends Plant Sci. 1:1996;57-64.
    • (1996) Trends Plant Sci. , vol.1 , pp. 57-64
    • Hanson, M.R.1    Sutton, C.A.2    Lu, B.3
  • 33
    • 0021891869 scopus 로고
    • The mitochondrial electron transport and oxidative phosphorylation system
    • Hatefi Y. The mitochondrial electron transport and oxidative phosphorylation system. Annu. Rev. Biochem. 54:1985;1015-1069.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 1015-1069
    • Hatefi, Y.1
  • 34
    • 0030835681 scopus 로고    scopus 로고
    • Antisense repression of the mitochondrial NADH-binding subunit of complex I in transgenic potato plants affects male fertility
    • Heiser V., Rasmusson A.G., Thieck O., Brennicke A., Grohmann L. Antisense repression of the mitochondrial NADH-binding subunit of complex I in transgenic potato plants affects male fertility. Plant Sci. 127:1997;61-69.
    • (1997) Plant Sci. , vol.127 , pp. 61-69
    • Heiser, V.1    Rasmusson, A.G.2    Thieck, O.3    Brennicke, A.4    Grohmann, L.5
  • 35
    • 0030963751 scopus 로고    scopus 로고
    • Cell type-specific loss of atp6 RNA editing in cytoplasmic male sterile Sorghum bicolor
    • Howad W., Kempken F. Cell type-specific loss of atp6 RNA editing in cytoplasmic male sterile Sorghum bicolor. Proc. Natl. Acad. Sci. USA. 94:1997;11090-11095.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11090-11095
    • Howad, W.1    Kempken, F.2
  • 37
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S., Ostermeier C., Ludwig B., Michel H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature. 376:1995;660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 38
    • 0030111226 scopus 로고    scopus 로고
    • New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria
    • Jänsch L., Kruft V., Schmitz U.K., Braun H.P. New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria. Plant J. 9:1996;357-368.
    • (1996) Plant J. , vol.9 , pp. 357-368
    • Jänsch, L.1    Kruft, V.2    Schmitz, U.K.3    Braun, H.P.4
  • 40
    • 0032214417 scopus 로고    scopus 로고
    • Tissue-specific expression of genes encoding isoforms of the mitochondrial ATPase b subunit in Nicotiana sylvestris
    • Lalanne É., Mathieu C., Vedel F., De Paepe R. Tissue-specific expression of genes encoding isoforms of the mitochondrial ATPase b subunit in Nicotiana sylvestris. Plant Mol. Biol. 38:1998;885-888.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 885-888
    • Lalanne, É.1    Mathieu, C.2    Vedel, F.3    De Paepe, R.4
  • 41
    • 0031665194 scopus 로고    scopus 로고
    • Organization and expression of the mitochondrial genome in the Nicotiana sylvestris CMSII mutant
    • Lelandais C., Albert B., Gutierres S., De Paepe R., Godelle B., Vedel F., Chétrit P. Organization and expression of the mitochondrial genome in the Nicotiana sylvestris CMSII mutant. Genetics. 150:1998;873-882.
    • (1998) Genetics , vol.150 , pp. 873-882
    • Lelandais, C.1    Albert, B.2    Gutierres, S.3    De Paepe, R.4    Godelle, B.5    Vedel, F.6    Chétrit, P.7
  • 42
    • 0027134082 scopus 로고
    • Thoughts on cytoplasmic male sterility in cms-T maize
    • Levings III C.S. Thoughts on cytoplasmic male sterility in cms-T maize. Plant Cell. 5:1993;1285-1290.
    • (1993) Plant Cell , vol.5 , pp. 1285-1290
    • Levings C.S. III1
  • 43
    • 0032030309 scopus 로고    scopus 로고
    • Mutations in mitochondrial DNA accumulate differentially in three different human tissues during ageing
    • Liu V.W.S., Zhang C., Nagley P. Mutations in mitochondrial DNA accumulate differentially in three different human tissues during ageing. Nucleic Acids Res. 26:1998;1268-1275.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1268-1275
    • Liu, V.W.S.1    Zhang, C.2    Nagley, P.3
  • 44
    • 0025299986 scopus 로고
    • Cloning and characterization of the iron-sulfur subunit gene of succinate dehydrogenase from Saccharomyces cerevisiae
    • Lombardo A., Carine K., Scheffler I.E. Cloning and characterization of the iron-sulfur subunit gene of succinate dehydrogenase from Saccharomyces cerevisiae. J. Biol. Chem. 265:1990;10419-10423.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10419-10423
    • Lombardo, A.1    Carine, K.2    Scheffler, I.E.3
  • 45
    • 0027996631 scopus 로고
    • The maize NCS2 abnormal growth mutant has a chimeric nad4-nad7 mitochondrial gene and is associated with reduced complex I function
    • Marienfeld J.R., Newton K.J. The maize NCS2 abnormal growth mutant has a chimeric nad4-nad7 mitochondrial gene and is associated with reduced complex I function. Genetics. 138:1994;855-863.
    • (1994) Genetics , vol.138 , pp. 855-863
    • Marienfeld, J.R.1    Newton, K.J.2
  • 47
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the protonmotive function of cytochrome systems
    • Mitchell P. Possible molecular mechanisms of the protonmotive function of cytochrome systems. J. Theor. Biol. 62:1976;327-367.
    • (1976) J. Theor. Biol. , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 49
    • 0023960320 scopus 로고
    • Eukaryote membrane genetics: The FO sector of mitochondrial ATP synthase
    • Nagley P. Eukaryote membrane genetics: the FO sector of mitochondrial ATP synthase. Trends Genet. 4:1988;46-52.
    • (1988) Trends Genet. , vol.4 , pp. 46-52
    • Nagley, P.1
  • 50
    • 0026494756 scopus 로고
    • Characterization of assembly intermediates of NADH:ubiquinone oxidoreductase (complex I) accumulated in Neurospora mitochondria by gene disruption
    • Nehls U., Friedrich T., Schmiede A., Ohnishi T., Weiss H. Characterization of assembly intermediates of NADH:ubiquinone oxidoreductase (complex I) accumulated in Neurospora mitochondria by gene disruption. J. Mol. Biol. 227:1992;1032-1042.
    • (1992) J. Mol. Biol. , vol.227 , pp. 1032-1042
    • Nehls, U.1    Friedrich, T.2    Schmiede, A.3    Ohnishi, T.4    Weiss, H.5
  • 51
    • 0025376631 scopus 로고
    • An abnormal growth mutant in maize has a defective mitochondrial cytochrome oxidase gene
    • Newton K.J., Knudsen C., Gabay-Laughnan S., Laughnan J.R. An abnormal growth mutant in maize has a defective mitochondrial cytochrome oxidase gene. Plant Cell. 2:1990;107-113.
    • (1990) Plant Cell , vol.2 , pp. 107-113
    • Newton, K.J.1    Knudsen, C.2    Gabay-Laughnan, S.3    Laughnan, J.R.4
  • 52
    • 0002801608 scopus 로고
    • Evolution of gene content and gene organization in flowering plant mitochondrial DNA: A general survey and further studies on cox2 gene transfer to the nucleus
    • A. Brennike, & U. Kück.
    • Nugent J.M., Palmer J.D. Evolution of gene content and gene organization in flowering plant mitochondrial DNA: a general survey and further studies on cox2 gene transfer to the nucleus. Brennike A, Kück U. Plant Mitochondria, VCH Chemie, Weinheim. 1993;163-170.
    • (1993) Plant Mitochondria, VCH Chemie, Weinheim , pp. 163-170
    • Nugent, J.M.1    Palmer, J.D.2
  • 53
    • 0027267299 scopus 로고
    • Group I introns in the liverwort mitochondrial genome: The gene coding for subunit 1 of cytochrome oxidase shares five intron positions with its fungal counterparts
    • Ohta E., Oda K., Yamato K., Nakamura Y., Takemura M., Nozato N., Akashi K., Ohyama K., Michel F. Group I introns in the liverwort mitochondrial genome: the gene coding for subunit 1 of cytochrome oxidase shares five intron positions with its fungal counterparts. Nucleic Acids Res. 21:1993;1297-1305.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1297-1305
    • Ohta, E.1    Oda, K.2    Yamato, K.3    Nakamura, Y.4    Takemura, M.5    Nozato, N.6    Akashi, K.7    Ohyama, K.8    Michel, F.9
  • 54
    • 0024468352 scopus 로고
    • Purification and characterization of a processing protease from rat liver mitochondria
    • Ou W.J., Ito A., Okazaki H., Omura T. Purification and characterization of a processing protease from rat liver mitochondria. EMBO J. 8:1989;2605-2612.
    • (1989) EMBO J. , vol.8 , pp. 2605-2612
    • Ou, W.J.1    Ito, A.2    Okazaki, H.3    Omura, T.4
  • 55
    • 0031440279 scopus 로고    scopus 로고
    • The carboxyl terminus of the Saccharomyces cerevisiae succinate dehydrogenase membrane subunit, SDH4p, is necessary for ubiquinone reduction and enzyme stability
    • Oyedotum K.S., Lemire B.D. The carboxyl terminus of the Saccharomyces cerevisiae succinate dehydrogenase membrane subunit, SDH4p, is necessary for ubiquinone reduction and enzyme stability. J. Biol. Chem. 272:1997;31382-31388.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31382-31388
    • Oyedotum, K.S.1    Lemire, B.D.2
  • 56
    • 0029134607 scopus 로고
    • Deletion of the last two exons of the mitochondrial nad7 gene results in lack of the NAD7 polypeptide in a Nicotiana sylvestris CMS mutant
    • Pla M., Mathieu C., De Paepe R., Chétrit P., Vedel F. Deletion of the last two exons of the mitochondrial nad7 gene results in lack of the NAD7 polypeptide in a Nicotiana sylvestris CMS mutant. Mol. Gen. Genet. 248:1995;79-88.
    • (1995) Mol. Gen. Genet. , vol.248 , pp. 79-88
    • Pla, M.1    Mathieu, C.2    De Paepe, R.3    Chétrit, P.4    Vedel, F.5
  • 57
    • 0029894544 scopus 로고    scopus 로고
    • Crosstalk between nuclear and mitochondrial genomes
    • Poynton R.O., McEwen J.E. Crosstalk between nuclear and mitochondrial genomes. Annu. Rev. Biochem. 65:1996;563-607.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 563-607
    • Poynton, R.O.1    McEwen, J.E.2
  • 59
    • 0032053605 scopus 로고    scopus 로고
    • Molecular characterization of the 76 kDa iron-sulphur protein subunit of potato mitochondrial complex I
    • Rasmusson A.G., Heiser V., Irrgang K.D., Brennicke A., Grohmann L. Molecular characterization of the 76 kDa iron-sulphur protein subunit of potato mitochondrial complex I. Plant Cell Physiol. 39:1998;373-381.
    • (1998) Plant Cell Physiol. , vol.39 , pp. 373-381
    • Rasmusson, A.G.1    Heiser, V.2    Irrgang, K.D.3    Brennicke, A.4    Grohmann, L.5
  • 61
    • 0028948314 scopus 로고
    • Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60
    • Rassow J., Mohrs K., Koidl S., Barthelmess I.B., Pfanner N., Tropschug M. Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60. Mol. Cell. Biol. 15:1995;2654-2662.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2654-2662
    • Rassow, J.1    Mohrs, K.2    Koidl, S.3    Barthelmess, I.B.4    Pfanner, N.5    Tropschug, M.6
  • 62
    • 0030726098 scopus 로고    scopus 로고
    • A novel nuclear gene, CBT1, essential for mitochondrial cytochrome b formation: Terminal processing of mRNA and intron dependence
    • Rieger K.J., Aljinovic G., Lazowska J., Pohl T.M., Slonimski P. A novel nuclear gene, CBT1, essential for mitochondrial cytochrome b formation: terminal processing of mRNA and intron dependence. Curr. Genet. 32:1997;163-174.
    • (1997) Curr. Genet. , vol.32 , pp. 163-174
    • Rieger, K.J.1    Aljinovic, G.2    Lazowska, J.3    Pohl, T.M.4    Slonimski, P.5
  • 64
    • 0242559473 scopus 로고    scopus 로고
    • Mitochondrial complex I dysfunction: Compatibility with survival and reproduction in cytoplasmic and nuclear male-sterile mutants of Nicotiana sylvestris
    • I.M. Moller, P. Gardestrom, K. Glimelius, & E. Glaser.
    • Sabar M., de Kouchkovsky Y., Gutierres S., Vedel F., De Paepe R. Mitochondrial complex I dysfunction: compatibility with survival and reproduction in cytoplasmic and nuclear male-sterile mutants of Nicotiana sylvestris. Moller I.M, Gardestrom P, Glimelius K, Glaser E. Proceedings 5th Intern. Congress Plant Mitochondria, Backhuys Publishers, Leiden. 1998;87-90.
    • (1998) Proceedings 5th Intern. Congress Plant Mitochondria, Backhuys Publishers, Leiden , pp. 87-90
    • Sabar, M.1    De Kouchkovsky, Y.2    Gutierres, S.3    Vedel, F.4    De Paepe, R.5
  • 65
    • 0032080597 scopus 로고    scopus 로고
    • The molecular basis of cytoplasmic male sterility and fertility restoration
    • Schnable P.S., Wise R.P. The molecular basis of cytoplasmic male sterility and fertility restoration. Trends Plant Sci. 3:1998;175-180.
    • (1998) Trends Plant Sci. , vol.3 , pp. 175-180
    • Schnable, P.S.1    Wise, R.P.2
  • 66
    • 0028087047 scopus 로고
    • The plant mitochondrial genome: Physical structure, information content, RNA editing and gene migration to the nucleus
    • Schuster W., Brennicke A. The plant mitochondrial genome: physical structure, information content, RNA editing and gene migration to the nucleus. Annu. Rev. Plant Physiol. Plant Mol. Biol. 45:1994;61-78.
    • (1994) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.45 , pp. 61-78
    • Schuster, W.1    Brennicke, A.2
  • 67
    • 0028831761 scopus 로고
    • Plant mitochondrial electron transfer and molecular biology
    • Siedow J.N., Umbach A.L. Plant mitochondrial electron transfer and molecular biology. Plant Cell. 7:1995;821-831.
    • (1995) Plant Cell , vol.7 , pp. 821-831
    • Siedow, J.N.1    Umbach, A.L.2
  • 68
    • 0030746112 scopus 로고    scopus 로고
    • The subunit f of mitochondrial yeast ATP synthase, characterization of the protein and disruption of the structural gene ATP17
    • Spannagel C., Vaillier J., Arselin G., Graves P.V., Velours J. The subunit f of mitochondrial yeast ATP synthase, characterization of the protein and disruption of the structural gene ATP17. Eur. J. Biochem. 247:1997;1111-1117.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 1111-1117
    • Spannagel, C.1    Vaillier, J.2    Arselin, G.3    Graves, P.V.4    Velours, J.5
  • 69
    • 0026860017 scopus 로고
    • The chloroplast genome
    • Sugiura M. The chloroplast genome. Plant Mol. Biol. 19:1992;149-168.
    • (1992) Plant Mol. Biol. , vol.19 , pp. 149-168
    • Sugiura, M.1
  • 70
    • 0028290824 scopus 로고
    • Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: The enzymology of coupling electron transfer reactions to transmembrane proton translocation
    • Trumpower B.L., Gennis R.B. Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: the enzymology of coupling electron transfer reactions to transmembrane proton translocation. Annu. Rev. Biochem. 63:1994;675-716.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 675-716
    • Trumpower, B.L.1    Gennis, R.B.2
  • 72
    • 0028787699 scopus 로고
    • Ubiquinol-cytochrome c oxidoreductase from Saccharomyces cerevisiae
    • Tzagoloff A. Ubiquinol-cytochrome c oxidoreductase from Saccharomyces cerevisiae. Methods Enzymol. 260:1995;51-63.
    • (1995) Methods Enzymol. , vol.260 , pp. 51-63
    • Tzagoloff, A.1
  • 73
    • 0031021278 scopus 로고    scopus 로고
    • The mitochondrial genome of Arabidopsis thaliana contains 57 genes in 366 924 nucleotides
    • Unseld M., Marienfeld J.K., Brandt P., Brennicke A. The mitochondrial genome of Arabidopsis thaliana contains 57 genes in 366 924 nucleotides. Nature Genet. 15:1997;57-61.
    • (1997) Nature Genet. , vol.15 , pp. 57-61
    • Unseld, M.1    Marienfeld, J.K.2    Brandt, P.3    Brennicke, A.4
  • 78
    • 0029045299 scopus 로고
    • Mitochondrial DNA variation in human evolution, degenerative disease and ageing
    • Wallace D.C. Mitochondrial DNA variation in human evolution, degenerative disease and ageing. Am. J. Hum. Genet. 57:1995;201-223.
    • (1995) Am. J. Hum. Genet. , vol.57 , pp. 201-223
    • Wallace, D.C.1
  • 79
    • 0025760073 scopus 로고
    • The respiratory-chain NADH dehydrogenase (complex I) of mitochondria
    • Weiss H., Friedrich T., Hofhaus G., Preis D. The respiratory-chain NADH dehydrogenase (complex I) of mitochondria. Eur. J. Biochem. 197:1991;563-576.
    • (1991) Eur. J. Biochem. , vol.197 , pp. 563-576
    • Weiss, H.1    Friedrich, T.2    Hofhaus, G.3    Preis, D.4


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