The respiratory chain in yeast behaves as a single functional unit

被引:129
作者
Boumans, H
Grivell, LA
Berden, JA
机构
[1] Univ Amsterdam, EC Slater Inst, Bioctr, Dept Mol Cell Biol, NL-1018 TV Amsterdam, Netherlands
[2] Univ Amsterdam, Bioctr, Dept Mol Cell Biol, Mol Biol Sect, NL-1018 TV Amsterdam, Netherlands
关键词
D O I
10.1074/jbc.273.9.4872
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Inhibitor titrations using antimycin have been used to study the pool behavior of ubiquinone and cytochrome c in the respiratory chain of the yeast Saccharomyces cerevisiae, If present in a homogeneous pool, these carriers should be able to diffuse freely through or along the membrane respectively and accept and subsequently donate electrons to an infinite number of the respective respiratory complex, However, we show that under physiological conditions neither ubiquinone nor cyto chrome c exhibits pool behavior, implying that the respiratory chain in yeast is one functional unit, Pool behavior can be introduced for both small carriers by adding chaotropic agents to the reaction medium. We conclude that these agents disrupt the interaction between the respiratory complexes, thereby causing them to become randomly arranged in the membrane, In such a situation, ubiquinone and cytochrome c become mobile carriers, shuttling between the large respiratory complexes. Furthermore, we conclude from the respiratory activities found for different substrates that the respiratory units in yeast vary in composition with respect to the ubiquinone reducing enzyme, All units contain the cytochrome chain, supplemented with either succinate dehydrogenase or the internal or the external NADH dehydrogenase. This implies that when only one substrate is available, only a certain fraction of the cytochrome chain is used in respiration, The molecular organization of the respiratory chain in yeast is compared with that of higher eukaryotes and to the electron transfer systems of photosynthetic membranes, Differences between the organization of the respiratory chain of yeast and that of higher eukaryotes are discussed in terms of the ability of yeast to radically alter its metabolism in response to change of the available carbon source.
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页码:4872 / 4877
页数:6
相关论文
共 37 条
  • [1] DIRECT INTERACTION BETWEEN THE INTERNAL NADH - UBIQUINONE OXIDOREDUCTASE AND UBIQUINOL - CYTOCHROME-C OXIDOREDUCTASE IN THE REDUCTION OF EXOGENOUS QUINONES BY YEAST MITOCHONDRIA
    BEATTIE, DS
    JAPA, S
    HOWTON, M
    ZHU, QS
    [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1992, 292 (02) : 499 - 505
  • [2] BERRY EA, 1985, J BIOL CHEM, V260, P2458
  • [3] CLONING OF A HUMAN GENE INVOLVED IN CYTOCHROME-OXIDASE ASSEMBLY BY FUNCTIONAL COMPLEMENTATION OF AN OXA1(-) MUTATION IN SACCHAROMYCES-CEREVISIAE
    BONNEFOY, N
    KERMORGANT, M
    GROUDINSKY, O
    MINET, M
    SLONIMSKI, PP
    DUJARDIN, G
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (25) : 11978 - 11982
  • [4] Bonnefoy N, 1996, MOL GEN GENET, V251, P204
  • [5] ABC1, A NOVEL YEAST NUCLEAR GENE HAS A DUAL FUNCTION IN MITOCHONDRIA - IT SUPPRESSES A CYTOCHROME-B MESSENGER-RNA TRANSLATION DEFECT AND IS ESSENTIAL FOR THE ELECTRON-TRANSFER IN THE BC1 COMPLEX
    BOUSQUET, I
    DUJARDIN, G
    SLONIMSKI, PP
    [J]. EMBO JOURNAL, 1991, 10 (08) : 2023 - 2031
  • [6] The nuclear ABC1 gene is essential for the correct conformation and functioning of the cytochrome bc(1) complex and the neighbouring complexes II and IV in the mitochondrial respiratory chain
    Brasseur, G
    Tron, P
    Dujardin, G
    Slonimski, PP
    BrivetChevillotte, P
    [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1997, 246 (01): : 103 - 111
  • [7] Bruel C, 1996, J BIOENERG BIOMEMBR, V28, P59
  • [8] BRYLA J, 1969, BIOCHIM BIOPHYS ACTA, V189, P317
  • [9] CHAZOTTE B, 1989, J BIOL CHEM, V264, P4978
  • [10] THE TERMINAL OXIDASES OF PARACOCCUS-DENITRIFICANS
    DEGIER, JWL
    LUBBEN, M
    REIJNDERS, WNM
    TIPKER, CA
    SLOTBOOM, DJ
    VANSPANNING, RJM
    STOUTHAMER, AH
    VANDEROOST, J
    [J]. MOLECULAR MICROBIOLOGY, 1994, 13 (02) : 183 - 196