메뉴 건너뛰기




Volumn 34, Issue 2, 1998, Pages 138-145

Molecular and biochemical analysis of Saccharomyces cerevisiae cox1 mutants

Author keywords

Complex assembly; Cytochrome c oxidase; Saccharomyces cerevisiae

Indexed keywords

CYTOCHROME C OXIDASE; FUNGAL PROTEIN; PROTEIN SUBUNIT;

EID: 0031665284     PISSN: 01728083     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002940050378     Document Type: Article
Times cited : (18)

References (36)
  • 1
    • 7344249807 scopus 로고
    • Recombinational analysis of oxi2 mutants and preliminary analysis of their translation products in S. cerevisiae
    • Baranowska H, Szcesniak B, Ejchart A, Kruszewska A, Claisse M (1983) Recombinational analysis of oxi2 mutants and preliminary analysis of their translation products in S. cerevisiae. Curr Genet 7:225-233
    • (1983) Curr Genet , vol.7 , pp. 225-233
    • Baranowska, H.1    Szcesniak, B.2    Ejchart, A.3    Kruszewska, A.4    Claisse, M.5
  • 2
    • 0019333281 scopus 로고
    • Assembly of the mitochondrial membrane system - Structure and nucleotide sequence of the gene coding for subunit I of yeast cytochrome oxidase
    • Bonitz S, Corruzi G, Thalenfeld B, Tzagoloff A, Macino G (1980) Assembly of the mitochondrial membrane system - structure and nucleotide sequence of the gene coding for subunit I of yeast cytochrome oxidase. J Biol Chem 255:11927-11941
    • (1980) J Biol Chem , vol.255 , pp. 11927-11941
    • Bonitz, S.1    Corruzi, G.2    Thalenfeld, B.3    Tzagoloff, A.4    Macino, G.5
  • 3
    • 0025335849 scopus 로고
    • Structure and assembly of cytochrome c oxidase
    • Capaldi RA (1990) Structure and assembly of cytochrome c oxidase. Arch Biochem Biophys 280:252-262
    • (1990) Arch Biochem Biophys , vol.280 , pp. 252-262
    • Capaldi, R.A.1
  • 4
    • 0022893771 scopus 로고
    • Expression of the mitochondrial split gene coding for cytochrome oxidase subunit I in S. cerevisiae: RNA splicing pathway
    • Carignani G, Netter P, Bergantino E, Robineau S (1986) Expression of the mitochondrial split gene coding for cytochrome oxidase subunit I in S. cerevisiae: RNA splicing pathway. Curr Genet 11:55-63
    • (1986) Curr Genet , vol.11 , pp. 55-63
    • Carignani, G.1    Netter, P.2    Bergantino, E.3    Robineau, S.4
  • 5
    • 0014883042 scopus 로고
    • Méthode d'estimation de la concentration des cytochromes dans les cellules entières de levure
    • Claisse M. Pere-Aubert G, Clavilier L, Slonimski PP (1970) Méthode d'estimation de la concentration des cytochromes dans les cellules entières de levure. Eur J Biochem 16:430-438
    • (1970) Eur J Biochem , vol.16 , pp. 430-438
    • Claisse, M.1    Pere-Aubert, G.2    Clavilier, L.3    Slonimski, P.P.4
  • 6
    • 0018850650 scopus 로고
    • Mutations within an intron and its flanking sites: Patterns of novel polypeptides generated by mutants in one segment of the cob-box region of yeast mitochondrial DNA
    • Claisse ML, Slonimski PP, Johnson J, Mahler HR (1980) Mutations within an intron and its flanking sites: patterns of novel polypeptides generated by mutants in one segment of the cob-box region of yeast mitochondrial DNA. Mol Gen Genet 177:375-387
    • (1980) Mol Gen Genet , vol.177 , pp. 375-387
    • Claisse, M.L.1    Slonimski, P.P.2    Johnson, J.3    Mahler, H.R.4
  • 7
    • 0019155697 scopus 로고
    • Long-range control circuits within mitochondria and between nucleus and mitochondria. I. Methodology and Phenomenology of Suppressors
    • Dujardin G, Pajot P, Groudinsky O, Slonimski PP (1980) Long-range control circuits within mitochondria and between nucleus and mitochondria. I. Methodology and Phenomenology of Suppressors. Mol Gen Genet 179:469-482
    • (1980) Mol Gen Genet , vol.179 , pp. 469-482
    • Dujardin, G.1    Pajot, P.2    Groudinsky, O.3    Slonimski, P.P.4
  • 8
    • 7344249220 scopus 로고
    • Thèse de Doctorat d'Etat. Université Paris
    • Dujardin G (1983) Thèse de Doctorat d'Etat. Université Paris 6
    • (1983) , pp. 6
    • Dujardin, G.1
  • 9
    • 0028816953 scopus 로고
    • Kinetic properties and ligand binding of the 11-subunit cytochrome c oxidase from Saccharomyces cerevisiae isolated with a novel large-scale purification method
    • Geier BM, Schagger H, Ortwein C, Link TA, Hagen WR, Brandt U (1995) Kinetic properties and ligand binding of the 11-subunit cytochrome c oxidase from Saccharomyces cerevisiae isolated with a novel large-scale purification method. Eur J Biochem 227: 296-302
    • (1995) Eur J Biochem , vol.227 , pp. 296-302
    • Geier, B.M.1    Schagger, H.2    Ortwein, C.3    Link, T.A.4    Hagen, W.R.5    Brandt, U.6
  • 10
    • 0030750778 scopus 로고    scopus 로고
    • Sub-mitochondrial distributions and stabilities of subunits 4, 5 and 6 of yeast cytochrome oxidase in assembly defective mutants
    • Glerum DM, Tzagoloff A (1997) Sub-mitochondrial distributions and stabilities of subunits 4, 5 and 6 of yeast cytochrome oxidase in assembly defective mutants. FEBS Lett 412:410-414
    • (1997) FEBS Lett , vol.412 , pp. 410-414
    • Glerum, D.M.1    Tzagoloff, A.2
  • 11
    • 0019770188 scopus 로고
    • Long-range control circuits within mitochondria and between nucleus and mitochondria. II. Genetic and biochemical analyses of suppressors which selectively alleviate the mitochondrial intron mutations
    • Groudinsky O, Dujardin G, Slonimski PP (1981) Long-range control circuits within mitochondria and between nucleus and mitochondria. II. Genetic and biochemical analyses of suppressors which selectively alleviate the mitochondrial intron mutations. Mol Gen Genet 184:493-503
    • (1981) Mol Gen Genet , vol.184 , pp. 493-503
    • Groudinsky, O.1    Dujardin, G.2    Slonimski, P.P.3
  • 12
    • 0020714483 scopus 로고
    • Two intron sequences in the yeast mitochondrial COX I gene: Homology among URF-containing introns and strain-dependent variation in flanking exons
    • Hensgens LAM, Bonen L, de Haan M, Horst G, Grivell LA (1983) Two intron sequences in the yeast mitochondrial COX I gene: homology among URF-containing introns and strain-dependent variation in flanking exons. Cell 32:379-389
    • (1983) Cell , vol.32 , pp. 379-389
    • Hensgens, L.A.M.1    Bonen, L.2    De Haan, M.3    Horst, G.4    Grivell, L.A.5
  • 13
    • 0028890031 scopus 로고
    • Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S, Ostermeier C, Ludwig B, Michel H (1995) Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376:660-669
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 14
    • 0004010867 scopus 로고
    • Mitochondrial mutants isolated by a new screening method based upon the use of the nuclear mutation opl
    • Bandlow W, Schweyen RJ, Wolf K, Kaudewitz F (eds) de Gruyter, Berlin New York
    • Kotylak Z, Slonimski PP (1977) Mitochondrial mutants isolated by a new screening method based upon the use of the nuclear mutation opl. In: Bandlow W, Schweyen RJ, Wolf K, Kaudewitz F (eds) Mitochondria (1977) Genetics and biogenesis of mitochondria, de Gruyter, Berlin New York, pp 83-89
    • (1977) Mitochondria (1977) Genetics and Biogenesis of Mitochondria , pp. 83-89
    • Kotylak, Z.1    Slonimski, P.P.2
  • 15
    • 0008095796 scopus 로고
    • Recombinational analysis of OXI1 and preliminary analysis of their translation products in S. cerevisiae
    • Kruszewska A, Szcesniak B, Claisse M (1980) Recombinational analysis of OXI1 and preliminary analysis of their translation products in S. cerevisiae. Curr Genet 2:45-51
    • (1980) Curr Genet , vol.2 , pp. 45-51
    • Kruszewska, A.1    Szcesniak, B.2    Claisse, M.3
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0030475162 scopus 로고    scopus 로고
    • Regulated protein degradation in mitochondria
    • Langer T, Neupert W (1996) Regulated protein degradation in mitochondria. Experientia 52:1069-1076
    • (1996) Experientia , vol.52 , pp. 1069-1076
    • Langer, T.1    Neupert, W.2
  • 18
    • 0026526374 scopus 로고
    • Isolation and characterization of COX12, the nuclear gene for a previously unrecognized subunit of S. cerevisiae cytochrome c oxidase
    • LaMarche AEP, Abate MI, Chan SHP, Trumpower BL (1992) Isolation and characterization of COX12, the nuclear gene for a previously unrecognized subunit of S. cerevisiae cytochrome c oxidase. J Biol Chem 267:22473-22480
    • (1992) J Biol Chem , vol.267 , pp. 22473-22480
    • LaMarche, A.E.P.1    Abate, M.I.2    Chan, S.H.P.3    Trumpower, B.L.4
  • 19
    • 0028029726 scopus 로고
    • Sequence analysis of three deficient mutants of cytochrome oxidase subunit I of Saccharomyces cerevisiae and their revenants
    • Lemarre P, Robineau S, Colson A-M, Netter P (1994) Sequence analysis of three deficient mutants of cytochrome oxidase subunit I of Saccharomyces cerevisiae and their revenants. Curr Genet 26:546-552
    • (1994) Curr Genet , vol.26 , pp. 546-552
    • Lemarre, P.1    Robineau, S.2    Colson, A.-M.3    Netter, P.4
  • 20
    • 0027264504 scopus 로고
    • Cytochrome b-deficient mutants of the ubiquinol-cytochrome c oxidoreductase in Saccharomyces cerevisiae. Consequence for the functional and structural characteristics of the complex
    • Lemesle-Meunier D, Brivet-Chevillotte P, di Rago J-P, Slonimski PP, Bruel C, Tron T, Forget N (1993) Cytochrome b-deficient mutants of the ubiquinol-cytochrome c oxidoreductase in Saccharomyces cerevisiae. Consequence for the functional and structural characteristics of the complex. J Biol Chem 268: 15626-15632
    • (1993) J Biol Chem , vol.268 , pp. 15626-15632
    • Lemesle-Meunier, D.1    Brivet-Chevillotte, P.2    Di Rago, J.-P.3    Slonimski, P.P.4    Bruel, C.5    Tron, T.6    Forget, N.7
  • 21
    • 0028090010 scopus 로고
    • Divalent metal iondependent mitochondrial degradation of unassembled subunits 2 and 3 of cytochrome c oxidase
    • Nakai T, Mera Y, Yasuhara T, Ohashi A (1994) Divalent metal iondependent mitochondrial degradation of unassembled subunits 2 and 3 of cytochrome c oxidase. J Biochem 116:752-758
    • (1994) J Biochem , vol.116 , pp. 752-758
    • Nakai, T.1    Mera, Y.2    Yasuhara, T.3    Ohashi, A.4
  • 22
    • 0020446673 scopus 로고
    • The cytochrome oxidase subunit I split gene in S. cerevisiae: Genetic and physical studies of the mtDNA segment encompassing the 'cytochrome b-homologous' intron
    • Netter P, Carignani G, Jacq C, Groudinsky O, Clavilier L, Slonimski PP (1982) The cytochrome oxidase subunit I split gene in S. cerevisiae: genetic and physical studies of the mtDNA segment encompassing the 'cytochrome b-homologous' intron. Mol Gen Genet 188:51-59
    • (1982) Mol Gen Genet , vol.188 , pp. 51-59
    • Netter, P.1    Carignani, G.2    Jacq, C.3    Groudinsky, O.4    Clavilier, L.5    Slonimski, P.P.6
  • 23
    • 0028910265 scopus 로고
    • Mutations in the mitochondria! split gene COX1 are preferentially located in exons: A mapping study of 172 mutants
    • Netter P, Robineau S, Lemaire C (1995) Mutations in the mitochondria! split gene COX1 are preferentially located in exons: a mapping study of 172 mutants. Mol Gen Genet 246:445-454
    • (1995) Mol Gen Genet , vol.246 , pp. 445-454
    • Netter, P.1    Robineau, S.2    Lemaire, C.3
  • 24
    • 0030857788 scopus 로고    scopus 로고
    • Structural and functional analysis of deficient mutants in subunit I of cytochrome c oxidase from Saccharomyces cerevisiae
    • Ortwein C, Link TA, Meunier B, Colson-Corbisier A-M, Rich PR, Brandt U (1997) Structural and functional analysis of deficient mutants in subunit I of cytochrome c oxidase from Saccharomyces cerevisiae. Biochim Biophys Acta 1321:79-92
    • (1997) Biochim Biophys Acta , vol.1321 , pp. 79-92
    • Ortwein, C.1    Link, T.A.2    Meunier, B.3    Colson-Corbisier, A.-M.4    Rich, P.R.5    Brandt, U.6
  • 25
    • 0023657503 scopus 로고
    • Subunit II of yeast QH2: Cytochrome-c oxidoreductase. Nucleotide sequence of the gene and features of the protein
    • Oudshoorn P, Van Steeg H, Swinkels BW, Schoppink P, Grivell LA (1987) Subunit II of yeast QH2: cytochrome-c oxidoreductase. Nucleotide sequence of the gene and features of the protein. Eur J Biochem 163:97-103
    • (1987) Eur J Biochem , vol.163 , pp. 97-103
    • Oudshoorn, P.1    Van Steeg, H.2    Swinkels, B.W.3    Schoppink, P.4    Grivell, L.A.5
  • 27
    • 0029894544 scopus 로고    scopus 로고
    • Cross-talk between nuclear and mitochondrial genomes
    • Poyton RO, Mc Ewen JE (1996) Cross-talk between nuclear and mitochondrial genomes. Annu Rev Biochem 65:563-607
    • (1996) Annu Rev Biochem , vol.65 , pp. 563-607
    • Poyton, R.O.1    Mc Ewen, J.E.2
  • 28
    • 0015849670 scopus 로고
    • Assembly of the mitochondrial membrane system. X. Mitochondrial synthesis of three of the subunit proteins of yeast cytochrome oxidase
    • Rubin MS, Tzagoloff A (1973) Assembly of the mitochondrial membrane system. X. Mitochondrial synthesis of three of the subunit proteins of yeast cytochrome oxidase. J Biol Chem 249:4269-4274
    • (1973) J Biol Chem , vol.249 , pp. 4269-4274
    • Rubin, M.S.1    Tzagoloff, A.2
  • 31
    • 0027209265 scopus 로고
    • Subunit VIa of yeast cytochrome c oxidase is not necessary for assembly of the enzyme complex but modulates the enzyme activity. Isolation and characterization of the nuclear-coded gene
    • Taanman JW, Capaldi RA (1993) Subunit VIa of yeast cytochrome c oxidase is not necessary for assembly of the enzyme complex but modulates the enzyme activity. Isolation and characterization of the nuclear-coded gene. J Biol Chem 268: 18754-18761
    • (1993) J Biol Chem , vol.268 , pp. 18754-18761
    • Taanman, J.W.1    Capaldi, R.A.2
  • 32
    • 0029984584 scopus 로고    scopus 로고
    • Subunit-specific monoclonal antibodies show different steady state levels of various cytochrome-c oxidase subunits in chronic progressive external ophthalmoplegia
    • Taanman J-W, Burton MD, Marusich MF, Kennaway NG, Capaldi RA (1996) Subunit-specific monoclonal antibodies show different steady state levels of various cytochrome-c oxidase subunits in chronic progressive external ophthalmoplegia. Biochim Biophys Acta 1315:199-207
    • (1996) Biochim Biophys Acta , vol.1315 , pp. 199-207
    • Taanman, J.-W.1    Burton, M.D.2    Marusich, M.F.3    Kennaway, N.G.4    Capaldi, R.A.5
  • 33
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and applications
    • Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and applications. Proc Natl Acad Sci USA 76:4350-4354
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 34
    • 0025678870 scopus 로고
    • Two substitutions at the same position in the mitochondrial cytochrome b gene of S. cerevisiae induce a mitochondrial myxothiazol resistance and impair the respiratory growth of the mutated strains albeit maintaining a good electron transfer activity
    • Tron T, Lemesle-Meunier D (1990) Two substitutions at the same position in the mitochondrial cytochrome b gene of S. cerevisiae induce a mitochondrial myxothiazol resistance and impair the respiratory growth of the mutated strains albeit maintaining a good electron transfer activity. Curr Genet 18:413-419
    • (1990) Curr Genet , vol.18 , pp. 413-419
    • Tron, T.1    Lemesle-Meunier, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.