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Volumn 344, Issue 1, 2006, Pages 241-245

Ubiquinone accumulates in the mitochondria of yeast mutated in the ubiquinone binding protein, Qcr8p

Author keywords

Complex III; Qcr8p; Ubiquinone; Ubiquinone binding protein

Indexed keywords

CYTOCHROME B; MUTANT PROTEIN; PROLINE; UBIQUINOL CYTOCHROME C REDUCTASE; UBIQUINONE;

EID: 33646056986     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.03.110     Document Type: Article
Times cited : (4)

References (22)
  • 1
    • 0037285346 scopus 로고    scopus 로고
    • Structure and function of quinone binding membrane proteins
    • Iwata M., Abramson J., Byrne B., and Iwata S. Structure and function of quinone binding membrane proteins. Adv. Protein Chem. 62 (2003) 151-176
    • (2003) Adv. Protein Chem. , vol.62 , pp. 151-176
    • Iwata, M.1    Abramson, J.2    Byrne, B.3    Iwata, S.4
  • 2
    • 0025181995 scopus 로고
    • Membrane topography of the subunits of ubiquinol-cytochrome c oxidoreductase of Saccharomyces cerevisiae
    • Hemrika W., and Berden J.A. Membrane topography of the subunits of ubiquinol-cytochrome c oxidoreductase of Saccharomyces cerevisiae. Eur. J. Biochem. 192 (1990) 761-765
    • (1990) Eur. J. Biochem. , vol.192 , pp. 761-765
    • Hemrika, W.1    Berden, J.A.2
  • 3
    • 0028826926 scopus 로고
    • Cloning, gene sequencing, and expression of the small molecular mass ubiquinone-binding protein of mitochondrial ubiquinol-cytochrome c reductase
    • Yu L., Deng K.-P., and Yu C.-A. Cloning, gene sequencing, and expression of the small molecular mass ubiquinone-binding protein of mitochondrial ubiquinol-cytochrome c reductase. J. Biol. Chem. 270 (1995) 25634-25638
    • (1995) J. Biol. Chem. , vol.270 , pp. 25634-25638
    • Yu, L.1    Deng, K.-P.2    Yu, C.-A.3
  • 4
    • 0034660152 scopus 로고    scopus 로고
    • Structure at 2.3 Å resolution of the cytochrome bc1 complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment
    • Hunte C., Koepke J., Lange C., Rossmanith T., and Michel H. Structure at 2.3 Å resolution of the cytochrome bc1 complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment. Structure 8 (2000) 669-684
    • (2000) Structure , vol.8 , pp. 669-684
    • Hunte, C.1    Koepke, J.2    Lange, C.3    Rossmanith, T.4    Michel, H.5
  • 5
    • 0025299069 scopus 로고
    • The small molecular mass ubiquinone-binding protein (Qpc-9.5 kDa) in mitochondrial ubiquinol-cytochrome c reductase
    • Usui S., Yu L., and Yu C.-A. The small molecular mass ubiquinone-binding protein (Qpc-9.5 kDa) in mitochondrial ubiquinol-cytochrome c reductase. Biochemistry 29 (1990) 4618-4626
    • (1990) Biochemistry , vol.29 , pp. 4618-4626
    • Usui, S.1    Yu, L.2    Yu, C.-A.3
  • 6
    • 0028294434 scopus 로고
    • The aromatic nature of residue 66 of the 11-kDa subunit of ubiquinol-cytochrome c oxidoreductase of the yeast Saccharomyces cerevisiae is important for the assembly of a functional enzyme
    • Hemrika W., Lobo-Hajdu G., Berden J.A., and Grivell L.A. The aromatic nature of residue 66 of the 11-kDa subunit of ubiquinol-cytochrome c oxidoreductase of the yeast Saccharomyces cerevisiae is important for the assembly of a functional enzyme. FEBS Letts. 344 (1994) 15-19
    • (1994) FEBS Letts. , vol.344 , pp. 15-19
    • Hemrika, W.1    Lobo-Hajdu, G.2    Berden, J.A.3    Grivell, L.A.4
  • 7
    • 0030060974 scopus 로고    scopus 로고
    • Subunit 8 of the Saccharomyces cerevisiae cytochrome bc1 complex interacts with succinate-ubiquinone reductase complex
    • Bruel C., Brasseur R., and Trumpower B.L. Subunit 8 of the Saccharomyces cerevisiae cytochrome bc1 complex interacts with succinate-ubiquinone reductase complex. J. Bioenerg. Biomembr. 28 (1996) 59-68
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 59-68
    • Bruel, C.1    Brasseur, R.2    Trumpower, B.L.3
  • 8
    • 0027267441 scopus 로고
    • A region of the C-terminal part of the 11-kDa subunit of ubiquinol-cytochrome-c oxidoreductase of the yeast Saccharomyces cerevisiae contributes to the structure of the Q out domain
    • Hemrika W., Berden J.A., and Grivell L.A. A region of the C-terminal part of the 11-kDa subunit of ubiquinol-cytochrome-c oxidoreductase of the yeast Saccharomyces cerevisiae contributes to the structure of the Q out domain. Eur. J. Biochem. 215 (1993) 601-609
    • (1993) Eur. J. Biochem. , vol.215 , pp. 601-609
    • Hemrika, W.1    Berden, J.A.2    Grivell, L.A.3
  • 9
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman F. Getting started with yeast. Methods Enzymol. 194 (1991) 3-21
    • (1991) Methods Enzymol. , vol.194 , pp. 3-21
    • Sherman, F.1
  • 10
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine M.S., McKenzie A., and Demarini D.J. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14 (1998) 953-961
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie, A.2    Demarini, D.J.3
  • 11
    • 0029009125 scopus 로고
    • Isolation and biochemical characterization of organelles from the yeast, Saccharomyces cerevisiae
    • Zinser E., and Daum G. Isolation and biochemical characterization of organelles from the yeast, Saccharomyces cerevisiae. Yeast 11 (1995) 493-536
    • (1995) Yeast , vol.11 , pp. 493-536
    • Zinser, E.1    Daum, G.2
  • 12
    • 0034822013 scopus 로고    scopus 로고
    • A mutation in the yeast mitochondrial ribosomal protein Rml2p is associated with a defect in catalase gene expression
    • Hagerman R.A., and Trotter P.J. A mutation in the yeast mitochondrial ribosomal protein Rml2p is associated with a defect in catalase gene expression. Mol. Cell Bio. Res. Commun. 4 (2001) 299-306
    • (2001) Mol. Cell Bio. Res. Commun. , vol.4 , pp. 299-306
    • Hagerman, R.A.1    Trotter, P.J.2
  • 13
    • 1942520301 scopus 로고    scopus 로고
    • Disruption of the interaction between the Rieske iron-sulfur protein and cytochrome b in the yeast bc1 complex owing to a human disease-associated mutation within cytochrome b
    • Fisher N., Bourges I., Hill P., Brasseur G., and Meunier B. Disruption of the interaction between the Rieske iron-sulfur protein and cytochrome b in the yeast bc1 complex owing to a human disease-associated mutation within cytochrome b. Eur. J. Biochem. 271 (2004) 1292-1298
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1292-1298
    • Fisher, N.1    Bourges, I.2    Hill, P.3    Brasseur, G.4    Meunier, B.5
  • 14
    • 0026611757 scopus 로고
    • Cytochrome bc1 complex [2Fe-2S] cluster and its interaction with ubiquinone and ubihydroquinone at the Q0 site
    • Ding H., Robertson D.E., Daldal F., and Dutton P.L. Cytochrome bc1 complex [2Fe-2S] cluster and its interaction with ubiquinone and ubihydroquinone at the Q0 site. Biochemistry 31 (1992) 3144-3158
    • (1992) Biochemistry , vol.31 , pp. 3144-3158
    • Ding, H.1    Robertson, D.E.2    Daldal, F.3    Dutton, P.L.4
  • 15
    • 0035450548 scopus 로고    scopus 로고
    • Solid-phase extraction of lipid from Saccharomyces cerevisiae followed by high-performance liquid chromatography analysis of coenzyme Q content
    • Hagerman R.A., Anthony M.J., and Willis R.A. Solid-phase extraction of lipid from Saccharomyces cerevisiae followed by high-performance liquid chromatography analysis of coenzyme Q content. Anal. Biochem. 296 (2001) 141-143
    • (2001) Anal. Biochem. , vol.296 , pp. 141-143
    • Hagerman, R.A.1    Anthony, M.J.2    Willis, R.A.3
  • 16
    • 0018158109 scopus 로고
    • Determination of contents and redox states of ubiquinone and menaquinone
    • Kroger A. Determination of contents and redox states of ubiquinone and menaquinone. Methods Enzymol. 52 (1978) 579-591
    • (1978) Methods Enzymol. , vol.52 , pp. 579-591
    • Kroger, A.1
  • 17
    • 0028871868 scopus 로고
    • Tyrosine 147 of cytochrome b is required for efficient electron transfer at the ubihydroquinone oxidase site (Q sub(o)) of the cytochrome bc sub(1) complex
    • Sariba A.S., Ding H., Dutton P.L., and Daldal F. Tyrosine 147 of cytochrome b is required for efficient electron transfer at the ubihydroquinone oxidase site (Q sub(o)) of the cytochrome bc sub(1) complex. Biochemistry 34 (1995) 16004-16012
    • (1995) Biochemistry , vol.34 , pp. 16004-16012
    • Sariba, A.S.1    Ding, H.2    Dutton, P.L.3    Daldal, F.4
  • 18
    • 0035903018 scopus 로고    scopus 로고
    • Analysis of suppressor mutation reveals long distance interactions in the bc1 complex of Saccharomyces cerevisiae
    • Brasseur G., Di Rago J.-P., Slonimski P.P., and Lemesle-Meunier D. Analysis of suppressor mutation reveals long distance interactions in the bc1 complex of Saccharomyces cerevisiae. Biochim. Biophys. Acta 1506 (2001) 89-102
    • (2001) Biochim. Biophys. Acta , vol.1506 , pp. 89-102
    • Brasseur, G.1    Di Rago, J.-P.2    Slonimski, P.P.3    Lemesle-Meunier, D.4
  • 19
    • 2642559589 scopus 로고    scopus 로고
    • QO site deficiency can be compensated by extragenic mutations in the hinge region of the iron-sulfur protein in the bc1 complex of Saccharomyces cerevisiae
    • Brasseur G., Lemesle-Meunier D., Reinaud F., and Meunier B. QO site deficiency can be compensated by extragenic mutations in the hinge region of the iron-sulfur protein in the bc1 complex of Saccharomyces cerevisiae. J. Biol. Chem. 279 (2004) 24203-24211
    • (2004) J. Biol. Chem. , vol.279 , pp. 24203-24211
    • Brasseur, G.1    Lemesle-Meunier, D.2    Reinaud, F.3    Meunier, B.4
  • 20
    • 0030697520 scopus 로고    scopus 로고
    • The role of subunit VIII in the structural stability of the bc1 complex from Saccharomyces cerevisiae studied using hybrid complexes
    • Boumans H., Berden J.A., and Grivell L.A. The role of subunit VIII in the structural stability of the bc1 complex from Saccharomyces cerevisiae studied using hybrid complexes. Eur. J. Biochem. 249 (1997) 762-769
    • (1997) Eur. J. Biochem. , vol.249 , pp. 762-769
    • Boumans, H.1    Berden, J.A.2    Grivell, L.A.3
  • 21
    • 0037192846 scopus 로고    scopus 로고
    • Uptake of exogenous coenzyme Q and transport to mitochondria is required for bc1 complex stability in yeast coq mutants
    • Santos-Ocana C., Do T.Q., Padilla S., Navas P., and Clarke C.F. Uptake of exogenous coenzyme Q and transport to mitochondria is required for bc1 complex stability in yeast coq mutants. J. Biol. Chem. 277 (2002) 10973-10981
    • (2002) J. Biol. Chem. , vol.277 , pp. 10973-10981
    • Santos-Ocana, C.1    Do, T.Q.2    Padilla, S.3    Navas, P.4    Clarke, C.F.5
  • 22
    • 0035947594 scopus 로고    scopus 로고
    • A defect in coenzyme Q biosynthesis is responsible for the respiratory deficiency in Saccharomyces cerevisiae abc1 mutants
    • Do T.Q., Hsu A.Y., Jonassen T., Lee P.T., and Clarke C.F. A defect in coenzyme Q biosynthesis is responsible for the respiratory deficiency in Saccharomyces cerevisiae abc1 mutants. J. Biol. Chem. 276 (2001) 18161-18168
    • (2001) J. Biol. Chem. , vol.276 , pp. 18161-18168
    • Do, T.Q.1    Hsu, A.Y.2    Jonassen, T.3    Lee, P.T.4    Clarke, C.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.