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Volumn 56, Issue 6, 2014, Pages 763-776

Expression of Nuclear and Mitochondrial Genes Encoding ATP Synthase Is Synchronized by Disassembly of a Multisynthetase Complex

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ALCOHOL; AMINO ACID TRANSFER RNA LIGASE; ARC1 PROTEIN; CARBON DIOXIDE; CYTOCHROME C OXIDASE; GALACTOSE; GLUCOSE; GLYCEROL; HYBRID PROTEIN; LACTIC ACID; MITOCHONDRIAL PROTEIN; MULTIENZYME COMPLEX; MULTISYNTHETASE COMPLEX; PROTEIN; PROTON; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG; ARC1 PROTEIN, S CEREVISIAE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; RNA BINDING PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84918841061     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2014.10.015     Document Type: Article
Times cited : (45)

References (48)
  • 1
    • 33644686458 scopus 로고    scopus 로고
    • Function, structure, and biogenesis of mitochondrial ATP synthase
    • Ackerman S.H., Tzagoloff A. Function, structure, and biogenesis of mitochondrial ATP synthase. Prog. Nucleic Acid Res. Mol. Biol. 2005, 80:95-133.
    • (2005) Prog. Nucleic Acid Res. Mol. Biol. , vol.80 , pp. 95-133
    • Ackerman, S.H.1    Tzagoloff, A.2
  • 2
    • 0034100041 scopus 로고    scopus 로고
    • Glucose depletion rapidly inhibits translation initiation in yeast
    • Ashe M.P., De Long S.K., Sachs A.B. Glucose depletion rapidly inhibits translation initiation in yeast. Mol. Biol. Cell 2000, 11:833-848.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 833-848
    • Ashe, M.P.1    De Long, S.K.2    Sachs, A.B.3
  • 3
    • 0015243504 scopus 로고
    • Complex of aminoacyl-transfer RNA synthetases
    • Bandyopadhyay A.K., Deutscher M.P. Complex of aminoacyl-transfer RNA synthetases. J.Mol. Biol. 1971, 60:113-122.
    • (1971) J.Mol. Biol. , vol.60 , pp. 113-122
    • Bandyopadhyay, A.K.1    Deutscher, M.P.2
  • 4
    • 80053045925 scopus 로고    scopus 로고
    • Characterization of Gtf1p, the connector subunit of yeast mitochondrial tRNA-dependent amidotransferase
    • Barros M.H., Rak M., Paulela J.A., Tzagoloff A. Characterization of Gtf1p, the connector subunit of yeast mitochondrial tRNA-dependent amidotransferase. J.Biol. Chem. 2011, 286:32937-32947.
    • (2011) J.Biol. Chem. , vol.286 , pp. 32937-32947
    • Barros, M.H.1    Rak, M.2    Paulela, J.A.3    Tzagoloff, A.4
  • 6
    • 76049103000 scopus 로고    scopus 로고
    • Mammalian aminoacyl-tRNA synthetases: cell signaling functions of the protein translation machinery
    • Brown M.V., Reader J.S., Tzima E. Mammalian aminoacyl-tRNA synthetases: cell signaling functions of the protein translation machinery. Vascul. Pharmacol. 2010, 52:21-26.
    • (2010) Vascul. Pharmacol. , vol.52 , pp. 21-26
    • Brown, M.V.1    Reader, J.S.2    Tzima, E.3
  • 7
    • 0037295310 scopus 로고    scopus 로고
    • The S. cerevisiae HAP complex, a key regulator of mitochondrial function, coordinates nuclear and mitochondrial gene expression
    • Buschlen S., Amillet J.M., Guiard B., Fournier A., Marcireau C., Bolotin-Fukuhara M. The S. cerevisiae HAP complex, a key regulator of mitochondrial function, coordinates nuclear and mitochondrial gene expression. Comp. Funct. Genomics 2003, 4:37-46.
    • (2003) Comp. Funct. Genomics , vol.4 , pp. 37-46
    • Buschlen, S.1    Amillet, J.M.2    Guiard, B.3    Fournier, A.4    Marcireau, C.5    Bolotin-Fukuhara, M.6
  • 9
    • 84893108696 scopus 로고    scopus 로고
    • A multiple aminoacyl-tRNA synthetase complex that enhances tRNA-aminoacylation in African trypanosomes
    • Cestari I., Kalidas S., Monnerat S., Anupama A., Phillips M.A., Stuart K. A multiple aminoacyl-tRNA synthetase complex that enhances tRNA-aminoacylation in African trypanosomes. Mol. Cell. Biol. 2013, 33:4872-4888.
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 4872-4888
    • Cestari, I.1    Kalidas, S.2    Monnerat, S.3    Anupama, A.4    Phillips, M.A.5    Stuart, K.6
  • 11
    • 0345255615 scopus 로고    scopus 로고
    • The two rotor components of yeast mitochondrial ATP synthase are mechanically coupled by subunit δ
    • Duvezin-Caubet S., Caron M., Giraud M.-F., Velours J., di Rago J.-P. The two rotor components of yeast mitochondrial ATP synthase are mechanically coupled by subunit δ. Proc. Natl. Acad. Sci. USA 2003, 100:13235-13240.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13235-13240
    • Duvezin-Caubet, S.1    Caron, M.2    Giraud, M.-F.3    Velours, J.4    di Rago, J.-P.5
  • 12
    • 84870669523 scopus 로고    scopus 로고
    • Mitochondrial protein synthesis, import, and assembly
    • Fox T.D. Mitochondrial protein synthesis, import, and assembly. Genetics 2012, 192:1203-1234.
    • (2012) Genetics , vol.192 , pp. 1203-1234
    • Fox, T.D.1
  • 13
    • 65449172879 scopus 로고    scopus 로고
    • Yeast mitochondrial Gln-tRNA(Gln) is generated by a GatFAB-mediated transamidation pathway involving Arc1p-controlled subcellular sorting of cytosolic GluRS
    • Frechin M., Senger B., Brayé M., Kern D., Martin R.P., Becker H.D. Yeast mitochondrial Gln-tRNA(Gln) is generated by a GatFAB-mediated transamidation pathway involving Arc1p-controlled subcellular sorting of cytosolic GluRS. Genes Dev. 2009, 23:1119-1130.
    • (2009) Genes Dev. , vol.23 , pp. 1119-1130
    • Frechin, M.1    Senger, B.2    Brayé, M.3    Kern, D.4    Martin, R.P.5    Becker, H.D.6
  • 15
    • 13444302274 scopus 로고    scopus 로고
    • Role of Arc1p in the modulation of yeast glutamyl-tRNA synthetase activity
    • Graindorge J.S., Senger B., Tritch D., Simos G., Fasiolo F. Role of Arc1p in the modulation of yeast glutamyl-tRNA synthetase activity. Biochemistry 2005, 44:1344-1352.
    • (2005) Biochemistry , vol.44 , pp. 1344-1352
    • Graindorge, J.S.1    Senger, B.2    Tritch, D.3    Simos, G.4    Fasiolo, F.5
  • 16
    • 84874028131 scopus 로고    scopus 로고
    • Essential nontranslational functions of tRNA synthetases
    • Guo M., Schimmel P. Essential nontranslational functions of tRNA synthetases. Nat. Chem. Biol. 2013, 9:145-153.
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 145-153
    • Guo, M.1    Schimmel, P.2
  • 17
    • 77956095201 scopus 로고    scopus 로고
    • New functions of aminoacyl-tRNA synthetases beyond translation
    • Guo M., Yang X.L., Schimmel P. New functions of aminoacyl-tRNA synthetases beyond translation. Nat. Rev. Mol. Cell Biol. 2010, 11:668-674.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 668-674
    • Guo, M.1    Yang, X.L.2    Schimmel, P.3
  • 18
    • 0242664909 scopus 로고    scopus 로고
    • The Snf1 protein kinase controls the induction of genes of the iron uptake pathway at the diauxic shift in Saccharomyces cerevisiae
    • Haurie V., Boucherie H., Sagliocco F. The Snf1 protein kinase controls the induction of genes of the iron uptake pathway at the diauxic shift in Saccharomyces cerevisiae. J.Biol. Chem. 2003, 278:45391-45396.
    • (2003) J.Biol. Chem. , vol.278 , pp. 45391-45396
    • Haurie, V.1    Boucherie, H.2    Sagliocco, F.3
  • 19
    • 44849096180 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetase complexes: molecular multitasking revealed
    • Hausmann C.D., Ibba M. Aminoacyl-tRNA synthetase complexes: molecular multitasking revealed. FEMS Microbiol. Rev. 2008, 32:705-721.
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 705-721
    • Hausmann, C.D.1    Ibba, M.2
  • 20
    • 80051503319 scopus 로고    scopus 로고
    • Caenorhabditis elegans evolves a new architecture for the multi-aminoacyl-tRNA synthetase complex
    • Havrylenko S., Legouis R., Negrutskii B., Mirande M. Caenorhabditis elegans evolves a new architecture for the multi-aminoacyl-tRNA synthetase complex. J.Biol. Chem. 2011, 286:28476-28487.
    • (2011) J.Biol. Chem. , vol.286 , pp. 28476-28487
    • Havrylenko, S.1    Legouis, R.2    Negrutskii, B.3    Mirande, M.4
  • 21
    • 38449110592 scopus 로고    scopus 로고
    • SNF1/AMPK pathways in yeast
    • Hedbacker K., Carlson M. SNF1/AMPK pathways in yeast. Front. Biosci. 2008, 13:2408-2420.
    • (2008) Front. Biosci. , vol.13 , pp. 2408-2420
    • Hedbacker, K.1    Carlson, M.2
  • 22
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba M., Söll D. Aminoacyl-tRNA synthesis. Annu. Rev. Biochem. 2000, 69:617-650.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 617-650
    • Ibba, M.1    Söll, D.2
  • 24
    • 0034192459 scopus 로고    scopus 로고
    • Nucleolar localization of human methionyl-tRNA synthetase and its role in ribosomal RNA synthesis
    • Ko Y.G., Kang Y.S., Kim E.K., Park S.G., Kim S. Nucleolar localization of human methionyl-tRNA synthetase and its role in ribosomal RNA synthesis. J.Cell Biol. 2000, 149:567-574.
    • (2000) J.Cell Biol. , vol.149 , pp. 567-574
    • Ko, Y.G.1    Kang, Y.S.2    Kim, E.K.3    Park, S.G.4    Kim, S.5
  • 25
    • 0035794147 scopus 로고    scopus 로고
    • Identification of a nuclear gene (FMC1) required for the assembly/stability of yeast mitochondrial F(1)-ATPase in heat stress conditions
    • Lefebvre-Legendre L., Vaillier J., Benabdelhak H., Velours J., Slonimski P.P., di Rago J.-P. Identification of a nuclear gene (FMC1) required for the assembly/stability of yeast mitochondrial F(1)-ATPase in heat stress conditions. J.Biol. Chem. 2001, 276:6789-6796.
    • (2001) J.Biol. Chem. , vol.276 , pp. 6789-6796
    • Lefebvre-Legendre, L.1    Vaillier, J.2    Benabdelhak, H.3    Velours, J.4    Slonimski, P.P.5    di Rago, J.-P.6
  • 26
    • 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., di Rago J.-P. 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. 2005, 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
  • 27
    • 0035965277 scopus 로고    scopus 로고
    • Regulation of Snf1 kinase. Activation requires phosphorylation of threonine 210 by an upstream kinase as well as a distinct step mediated by the Snf4 subunit
    • McCartney R.R., Schmidt M.C. Regulation of Snf1 kinase. Activation requires phosphorylation of threonine 210 by an upstream kinase as well as a distinct step mediated by the Snf4 subunit. J.Biol. Chem. 2001, 276:36460-36466.
    • (2001) J.Biol. Chem. , vol.276 , pp. 36460-36466
    • McCartney, R.R.1    Schmidt, M.C.2
  • 28
    • 0020729912 scopus 로고
    • Seven mammalian aminoacyl-tRNA synthetases associated within the same complex are functionally independent
    • Mirande M., Cirakoğlu B., Waller J.-P. Seven mammalian aminoacyl-tRNA synthetases associated within the same complex are functionally independent. Eur. J. Biochem. 1983, 131:163-170.
    • (1983) Eur. J. Biochem. , vol.131 , pp. 163-170
    • Mirande, M.1    Cirakoğlu, B.2    Waller, J.-P.3
  • 30
    • 0033664269 scopus 로고    scopus 로고
    • Increasing galactose consumption by Saccharomyces cerevisiae through metabolic engineering of the GAL gene regulatory network
    • Ostergaard S., Olsson L., Johnston M., Nielsen J. Increasing galactose consumption by Saccharomyces cerevisiae through metabolic engineering of the GAL gene regulatory network. Nat. Biotechnol. 2000, 18:1283-1286.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 1283-1286
    • Ostergaard, S.1    Olsson, L.2    Johnston, M.3    Nielsen, J.4
  • 32
    • 49649110170 scopus 로고    scopus 로고
    • Aminoacyl tRNA synthetases and their connections to disease
    • Park S.G., Schimmel P., Kim S. Aminoacyl tRNA synthetases and their connections to disease. Proc. Natl. Acad. Sci. USA 2008, 105:11043-11049.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 11043-11049
    • Park, S.G.1    Schimmel, P.2    Kim, S.3
  • 33
    • 0001363302 scopus 로고
    • Changes in the activities of respiratory enzymes during the aerobic growth of yeast on different carbon sources
    • Polakis E.S., Bartley W., Meek G.A. Changes in the activities of respiratory enzymes during the aerobic growth of yeast on different carbon sources. Biochem. J. 1965, 97:298-302.
    • (1965) Biochem. J. , vol.97 , pp. 298-302
    • Polakis, E.S.1    Bartley, W.2    Meek, G.A.3
  • 34
    • 73249131024 scopus 로고    scopus 로고
    • F1-dependent translation of mitochondrially encoded Atp6p and Atp8p subunits of yeast ATP synthase
    • Rak M., Tzagoloff A. F1-dependent translation of mitochondrially encoded Atp6p and Atp8p subunits of yeast ATP synthase. Proc. Natl. Acad. Sci. USA 2009, 106:18509-18514.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 18509-18514
    • Rak, M.1    Tzagoloff, A.2
  • 36
    • 34247131410 scopus 로고    scopus 로고
    • Macromolecular complexes as depots for releasable regulatory proteins
    • Ray P.S., Arif A., Fox P.L. Macromolecular complexes as depots for releasable regulatory proteins. Trends Biochem. Sci. 2007, 32:158-164.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 158-164
    • Ray, P.S.1    Arif, A.2    Fox, P.L.3
  • 37
    • 0042388199 scopus 로고    scopus 로고
    • When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism
    • Roy H., Becker H.D., Reinbolt J., Kern D. When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism. Proc. Natl. Acad. Sci. USA 2003, 100:9837-9842.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9837-9842
    • Roy, H.1    Becker, H.D.2    Reinbolt, J.3    Kern, D.4
  • 39
    • 33645130011 scopus 로고    scopus 로고
    • Glucose signaling in Saccharomyces cerevisiae
    • Santangelo G.M. Glucose signaling in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 2006, 70:253-282.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 253-282
    • Santangelo, G.M.1
  • 40
    • 0343618479 scopus 로고    scopus 로고
    • Footprints of aminoacyl-tRNA synthetases are everywhere
    • Schimmel P., Ribas De Pouplana L. Footprints of aminoacyl-tRNA synthetases are everywhere. Trends Biochem. Sci. 2000, 25:207-209.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 207-209
    • Schimmel, P.1    Ribas De Pouplana, L.2
  • 41
    • 0037774738 scopus 로고    scopus 로고
    • Transcriptional control of nonfermentative metabolism in the yeast Saccharomyces cerevisiae
    • Schüller H.J. Transcriptional control of nonfermentative metabolism in the yeast Saccharomyces cerevisiae. Curr. Genet. 2003, 43:139-160.
    • (2003) Curr. Genet. , vol.43 , pp. 139-160
    • Schüller, H.J.1
  • 42
    • 33748568146 scopus 로고    scopus 로고
    • Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes
    • Simader H., Hothorn M., Köhler C., Basquin J., Simos G., Suck D. Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes. Nucleic Acids Res. 2006, 34:3968-3979.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 3968-3979
    • Simader, H.1    Hothorn, M.2    Köhler, C.3    Basquin, J.4    Simos, G.5    Suck, D.6
  • 43
    • 0029790980 scopus 로고    scopus 로고
    • The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases
    • Simos G., Segref A., Fasiolo F., Hellmuth K., Shevchenko A., Mann M., Hurt E.C. The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases. EMBO J. 1996, 15:5437-5448.
    • (1996) EMBO J. , vol.15 , pp. 5437-5448
    • Simos, G.1    Segref, A.2    Fasiolo, F.3    Hellmuth, K.4    Shevchenko, A.5    Mann, M.6    Hurt, E.C.7
  • 44
    • 77956921819 scopus 로고
    • Aminoacyl-tRNA synthetases
    • Söll D., Schimmel P.R. Aminoacyl-tRNA synthetases. Enzyme 1974, 10:489-538.
    • (1974) Enzyme , vol.10 , pp. 489-538
    • Söll, D.1    Schimmel, P.R.2


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