메뉴 건너뛰기




Volumn 18, Issue 4, 2013, Pages 567-577

The energetic state of mitochondria modulates complex III biogenesis through the atp-dependent activity of bcs1

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 84885177496     PISSN: 15504131     EISSN: 19327420     Source Type: Journal    
DOI: 10.1016/j.cmet.2013.08.017     Document Type: Article
Times cited : (19)

References (43)
  • 1
    • 0028114231 scopus 로고
    • Structure at 2. 8 A resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams, J.P., Leslie, A.G., Lutter, R., and Walker, J.E. (1994). Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Nature 370, 621-628.
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 2
    • 0025350272 scopus 로고
    • Identification of two nuclear genes (ATP11, ATP12) required for assembly of the yeast F1-ATPase
    • Ackerman, S.H., and Tzagoloff, A. (1990). Identification of two nuclear genes (ATP11, ATP12) required for assembly of the yeast F1-ATPase. Proc. Natl. Acad. Sci. USA 87, 4986-4990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4986-4990
    • Ackerman, S.H.1    Tzagoloff, A.2
  • 3
    • 33644686458 scopus 로고    scopus 로고
    • Function, structure, and biogenesis of mitochondrial ATP synthase
    • Ackerman, S.H., and Tzagoloff, A. (2005). Function, structure, and biogenesis of mitochondrial ATP synthase. Prog. Nucleic Acid Res. Mol. Biol. 80, 95-133.
    • (2005) Prog. Nucleic Acid Res. Mol. Biol. , vol.80 , pp. 95-133
    • Ackerman, S.H.1    Tzagoloff, A.2
  • 4
    • 69749089007 scopus 로고    scopus 로고
    • An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases
    • Augustin, S., Gerdes, F., Lee, S., Tsai, F.T.F., Langer, T., and Tatsuta, T. (2009). An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases. Mol. Cell 35, 574-585.
    • (2009) Mol. Cell , vol.35 , pp. 574-585
    • Augustin, S.1    Gerdes, F.2    Lee, S.3    Tsai, F.T.F.4    Langer, T.5    Tatsuta, T.6
  • 5
    • 0036137785 scopus 로고    scopus 로고
    • Regulation of cytochrome c oxidase by adenylic nucleotides. Is oxidative phosphorylation feedback regulated by its end-products?
    • Beauvoit, B., and Rigoulet, M. (2001). Regulation of cytochrome c oxidase by adenylic nucleotides. Is oxidative phosphorylation feedback regulated by its end-products? IUBMB Life 52, 143-152.
    • (2001) IUBMB Life , vol.52 , pp. 143-152
    • Beauvoit, B.1    Rigoulet, M.2
  • 6
    • 0027215424 scopus 로고
    • Interactions between glucose metabolism and oxidative phosphorylations on respiratory-competent Saccharomyces cerevisiae cells
    • Beauvoit, B., Rigoulet, M., Bunoust, O., Raffard, G., Canioni, P., and Guérin, B. (1993). Interactions between glucose metabolism and oxidative phosphorylations on respiratory-competent Saccharomyces cerevisiae cells. Eur. J. Biochem. 214, 163-172.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 163-172
    • Beauvoit, B.1    Rigoulet, M.2    Bunoust, O.3    Raffard, G.4    Canioni, P.5    Guérin, B.6
  • 7
    • 78650725430 scopus 로고    scopus 로고
    • Bcs1p can rescue a large and productive cytochrome bc(1) complex assembly intermediate in the inner membrane of yeast mitochondria
    • Conte, L., Trumpower, B.L., and Zara, V. (2011). Bcs1p can rescue a large and productive cytochrome bc(1) complex assembly intermediate in the inner membrane of yeast mitochondria. Biochim. Biophys. Acta 1813, 91-101.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 91-101
    • Conte, L.1    Trumpower, B.L.2    Zara, V.3
  • 9
    • 0033214782 scopus 로고    scopus 로고
    • Bcs1p, an AAA-family member, is a chaperone for the assembly of the cytochrome bc(1) complex
    • Cruciat, C.M., Hell, K., Fölsch, H., Neupert, W., and Stuart, R.A. (1999). Bcs1p, an AAA-family member, is a chaperone for the assembly of the cytochrome bc(1) complex. EMBO J. 18, 5226-5233.
    • (1999) EMBO J. , vol.18 , pp. 5226-5233
    • Cruciat, C.M.1    Hell, K.2    Fölsch, H.3    Neupert, W.4    Stuart, R.A.5
  • 10
    • 0034674060 scopus 로고    scopus 로고
    • The cytochrome bc1 and cytochrome c oxidase complexes associate to form a single supracomplex in yeast mitochondria
    • Cruciat, C.M., Brunner, S., Baumann, F., Neupert, W., and Stuart, R.A. (2000). The cytochrome bc1 and cytochrome c oxidase complexes associate to form a single supracomplex in yeast mitochondria. J. Biol. Chem. 275, 18093-18098.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18093-18098
    • Cruciat, C.M.1    Brunner, S.2    Baumann, F.3    Neupert, W.4    Stuart, R.A.5
  • 11
    • 84868691750 scopus 로고    scopus 로고
    • Late-stage maturation of the Rieske Fe/S protein: Mzm1 stabilizes Rip1 but does not facilitate its translocation by the AAA ATPase Bcs1
    • Cui, T.Z., Smith, P.M., Fox, J.L., Khalimonchuk, O., and Winge, D.R. (2012). Late-stage maturation of the Rieske Fe/S protein: Mzm1 stabilizes Rip1 but does not facilitate its translocation by the AAA ATPase Bcs1. Mol. Cell. Biol. 32, 4400-4409.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 4400-4409
    • Cui, T.Z.1    Smith, P.M.2    Fox, J.L.3    Khalimonchuk, O.4    Winge, D.R.5
  • 12
    • 17944381521 scopus 로고    scopus 로고
    • A mutant mitochondrial respiratory chain assembly protein causes complex III deficiency in patients with tubulopathy, encephalopathy and liver failure
    • de Lonlay, P., Valnot, I., Barrientos, A., Gorbatyuk, M., Tzagoloff, A., Taanman, J.W., Benayoun, E., Chrétien, D., Kadhom, N., Lombès, A., et al. (2001). A mutant mitochondrial respiratory chain assembly protein causes complex III deficiency in patients with tubulopathy, encephalopathy and liver failure. Nat. Genet. 29, 57-60.
    • (2001) Nat. Genet. , vol.29 , pp. 57-60
    • De Lonlay, P.1    Valnot, I.2    Barrientos, A.3    Gorbatyuk, M.4    Tzagoloff, A.5    Taanman, J.W.6    Benayoun, E.7    Chrétien, D.8    Kadhom, N.9    Lombès, A.10
  • 14
    • 80053073046 scopus 로고    scopus 로고
    • Interaction of complexes I, III, and IV within the bovine respirasome by single particle cryoelectron tomography
    • Dudkina, N.V., Kudryashev, M., Stahlberg, H., and Boekema, E.J. (2011). Interaction of complexes I, III, and IV within the bovine respirasome by single particle cryoelectron tomography. Proc. Natl. Acad. Sci. USA 108, 15196-15200.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 15196-15200
    • Dudkina, N.V.1    Kudryashev, M.2    Stahlberg, H.3    Boekema, E.J.4
  • 16
    • 0030042248 scopus 로고    scopus 로고
    • Internal targeting signal of the BCS1 protein: A novel mechanism of import into mitochondria
    • Fölsch, H., Guiard, B., Neupert, W., and Stuart, R.A. (1996). Internal targeting signal of the BCS1 protein: a novel mechanism of import into mitochondria. EMBO J. 15, 479-487.
    • (1996) EMBO J. , vol.15 , pp. 479-487
    • Fölsch, H.1    Guiard, B.2    Neupert, W.3    Stuart, R.A.4
  • 17
    • 84855240784 scopus 로고    scopus 로고
    • Mitochondrial AAA proteases- towards a molecular understanding ofmembrane-boundproteolytic machines
    • Gerdes, F., Tatsuta, T., and Langer, T. (2012). Mitochondrial AAA proteases- towards a molecular understanding ofmembrane-boundproteolytic machines. Biochim. Biophys. Acta 1823, 49-55.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 49-55
    • Gerdes, F.1    Tatsuta, T.2    Langer, T.3
  • 19
    • 34249688217 scopus 로고    scopus 로고
    • A structural model of the cytochrome C reductase/oxidase supercomplex from yeast mitochondria
    • Heinemeyer, J., Braun, H.P., Boekema, E.J., and Kouril, R. (2007). A structural model of the cytochrome C reductase/oxidase supercomplex from yeast mitochondria. J. Biol. Chem. 282, 12240-12248.
    • (2007) J. Biol. Chem. , vol.282 , pp. 12240-12248
    • Heinemeyer, J.1    Braun, H.P.2    Boekema, E.J.3    Kouril, R.4
  • 22
    • 0034660152 scopus 로고    scopus 로고
    • Structure at 2. 3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment
    • Hunte, C., Koepke, J., Lange, C., Rossmanith, T., and Michel, H. (2000). Structure at 2.3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment. Structure 8, 669-684.
    • (2000) Structure , vol.8 , pp. 669-684
    • Hunte, C.1    Koepke, J.2    Lange, C.3    Rossmanith, T.4    Michel, H.5
  • 24
    • 0033543650 scopus 로고    scopus 로고
    • Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH
    • Karata, K., Inagawa, T., Wilkinson, A.J., Tatsuta, T., and Ogura, T. (1999). Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH. J. Biol. Chem. 274, 26225-26232.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26225-26232
    • Karata, K.1    Inagawa, T.2    Wilkinson, A.J.3    Tatsuta, T.4    Ogura, T.5
  • 26
    • 67349139921 scopus 로고    scopus 로고
    • Biochemical consequences in yeast of the human mitochondrial DNA 8993T>C mutation in the ATPase6 gene found in NARP/MILS patients
    • Kucharczyk, R., Rak, M., and di Rago, J.P. (2009). Biochemical consequences in yeast of the human mitochondrial DNA 8993T>C mutation in the ATPase6 gene found in NARP/MILS patients. Biochim. Biophys. Acta 1793, 817-824.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 817-824
    • Kucharczyk, R.1    Rak, M.2    Di Rago, J.P.3
  • 29
    • 24044525272 scopus 로고    scopus 로고
    • Failure to assemble the alpha 3 beta 3 subcomplex of the ATP synthase leads to accumulation of the alpha and beta subunits within inclusion bodies and the loss of mitochondrial cristae in Saccharomyces cerevisiae
    • Lefebvre-Legendre, L., Salin, B., Schaëffer, J., Brèthes, D., Dautant, A., Ackerman, S.H., and di Rago, J.P. (2005). Failure to assemble the alpha 3 beta 3 subcomplex of the ATP synthase leads to accumulation of the alpha and beta subunits within inclusion bodies and the loss of mitochondrial cristae in Saccharomyces cerevisiae. J. Biol. Chem. 280, 18386-18392.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18386-18392
    • Lefebvre-Legendre, L.1    Salin, B.2    Schaëffer, J.3    Brèthes, D.4    Dautant, A.5    Ackerman, S.H.6    Di Rago, J.P.7
  • 30
    • 84934437830 scopus 로고    scopus 로고
    • Preparation of respiratory chain complexes from Saccharomyces cerevisiae wild-type and mutant mitochondria: Activity measurement and subunit composition analysis
    • Lemaire, C., and Dujardin, G. (2008). Preparation of respiratory chain complexes from Saccharomyces cerevisiae wild-type and mutant mitochondria: activity measurement and subunit composition analysis. Methods Mol. Biol. 432, 65-81.
    • (2008) Methods Mol. Biol. , vol.432 , pp. 65-81
    • Lemaire, C.1    Dujardin, G.2
  • 31
    • 79251499574 scopus 로고    scopus 로고
    • The GRACILE mutation introduced into Bcs1l causes postnatal complex III deficiency: A viable mouse model for mitochondrial hepatopathy
    • Levéen, P., Kotarsky, H., Mörgelin, M., Karikoski, R., Elmér, E., and Fellman, V. (2011). The GRACILE mutation introduced into Bcs1l causes postnatal complex III deficiency: a viable mouse model for mitochondrial hepatopathy. Hepatology 53, 437-447.
    • (2011) Hepatology , vol.53 , pp. 437-447
    • Levéen, P.1    Kotarsky, H.2    Mörgelin, M.3    Karikoski, R.4    Elmér, E.5    Fellman, V.6
  • 32
    • 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., 3rd, Demarini, D.J., Shah, N.G., Wach, A., Brachat, A., Philippsen, P., and Pringle, J.R. (1998). Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14, 953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 34
    • 0026702012 scopus 로고
    • BCS1, a novel gene required for the expression of functional Rieske iron-sulfur protein in Saccharomyces cerevisiae
    • Nobrega, F.G., Nobrega, M.P., and Tzagoloff, A. (1992). BCS1, a novel gene required for the expression of functional Rieske iron-sulfur protein in Saccharomyces cerevisiae. EMBO J. 11, 3821-3829.
    • (1992) EMBO J. , vol.11 , pp. 3821-3829
    • Nobrega, F.G.1    Nobrega, M.P.2    Tzagoloff, A.3
  • 35
    • 64049084434 scopus 로고    scopus 로고
    • Functional analysis of yeast bcs1 mutants highlights the role of Bcs1p-specific amino acids in the AAA domain
    • Nouet, C., Truan, G., Mathieu, L., and Dujardin, G. (2009). Functional analysis of yeast bcs1 mutants highlights the role of Bcs1p-specific amino acids in the AAA domain. J. Mol. Biol. 388, 252-261.
    • (2009) J. Mol. Biol. , vol.388 , pp. 252-261
    • Nouet, C.1    Truan, G.2    Mathieu, L.3    Dujardin, G.4
  • 37
    • 77954760554 scopus 로고    scopus 로고
    • Mitochondrial respiration and membrane potential are regulated by the allosteric ATP-inhibition of cytochrome c oxidase
    • Ramzan, R., Staniek, K., Kadenbach, B., and Vogt, S. (2010). Mitochondrial respiration and membrane potential are regulated by the allosteric ATP-inhibition of cytochrome c oxidase. Biochim. Biophys. Acta 1797, 1672-1680.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1672-1680
    • Ramzan, R.1    Staniek, K.2    Kadenbach, B.3    Vogt, S.4
  • 38
    • 0038230469 scopus 로고    scopus 로고
    • Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
    • Schägger, H., and Pfeiffer, K. (2000). Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J. 19, 1777-1783.
    • (2000) EMBO J. , vol.19 , pp. 1777-1783
    • Schägger, H.1    Pfeiffer, K.2
  • 39
    • 84655167921 scopus 로고    scopus 로고
    • Biogenesis of the cytochrome bc(1) complex and role of assembly factors
    • Smith, P.M., Fox, J.L., and Winge, D.R. (2012). Biogenesis of the cytochrome bc(1) complex and role of assembly factors. Biochim. Biophys. Acta 1817, 276-286.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 276-286
    • Smith, P.M.1    Fox, J.L.2    Winge, D.R.3
  • 40
    • 0038070088 scopus 로고    scopus 로고
    • Investigation of the role and mechanism of IF1 and STF1 proteins, twin inhibitory peptides which interact with the yeast mitochondrial ATP synthase
    • Venard, R., Brèthes, D., Giraud, M.F., Vaillier, J., Velours, J., and Haraux, F. (2003). Investigation of the role and mechanism of IF1 and STF1 proteins, twin inhibitory peptides which interact with the yeast mitochondrial ATP synthase. Biochemistry 42, 7626-7636.
    • (2003) Biochemistry , vol.42 , pp. 7626-7636
    • Venard, R.1    Brèthes, D.2    Giraud, M.F.3    Vaillier, J.4    Velours, J.5    Haraux, F.6
  • 42
    • 82455219093 scopus 로고    scopus 로고
    • A pathway of protein translocation in mitochondria mediated by the AAA-ATPase Bcs1
    • Wagener, N., Ackermann, M., Funes, S., and Neupert, W. (2011). A pathway of protein translocation in mitochondria mediated by the AAA-ATPase Bcs1. Mol. Cell 44, 191-202.
    • (2011) Mol. Cell , vol.44 , pp. 191-202
    • Wagener, N.1    Ackermann, M.2    Funes, S.3    Neupert, W.4
  • 43
    • 56349100659 scopus 로고    scopus 로고
    • Biogenesis of the yeast cytochrome bc1 complex
    • Zara, V., Conte, L., and Trumpower, B.L. (2009). Biogenesis of the yeast cytochrome bc1 complex. Biochim. Biophys. Acta 1793, 89-96.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 89-96
    • Zara, V.1    Conte, L.2    Trumpower, B.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.