메뉴 건너뛰기




Volumn 1782, Issue 5, 2008, Pages 317-325

The impact of mitochondrial tRNA mutations on the amount of ATP synthase differs in the brain compared to other tissues

Author keywords

Brain; COX cytochrome c oxidase; Leigh syndrome; MELAS syndrome; MERRF syndrome; Tissue specificity

Indexed keywords

CYTOCHROME C OXIDASE; MITOCHONDRIAL RNA; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); TRANSFER RNA;

EID: 42749083478     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2008.02.001     Document Type: Article
Times cited : (38)

References (42)
  • 1
    • 33744752749 scopus 로고    scopus 로고
    • The molecular basis for tissue specificity of the oxidative phosphorylation deficiencies in patients with mutations in the mitochondrial translation factor EFG1
    • Antonicka H., Sasarman F., Kennaway N.G., and Shoubridge E.A. The molecular basis for tissue specificity of the oxidative phosphorylation deficiencies in patients with mutations in the mitochondrial translation factor EFG1. Hum. Mol. Genet. 15 (2006) 1835-1846
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1835-1846
    • Antonicka, H.1    Sasarman, F.2    Kennaway, N.G.3    Shoubridge, E.A.4
  • 2
    • 33847792061 scopus 로고    scopus 로고
    • Mitochondrial transcription and its regulation in mammalian cells
    • Asin-Cayuela J., and Gustafsson C.M. Mitochondrial transcription and its regulation in mammalian cells. Trends Biochem. Sci. 32 (2007) 111-117
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 111-117
    • Asin-Cayuela, J.1    Gustafsson, C.M.2
  • 3
    • 0033060854 scopus 로고    scopus 로고
    • The mitochondrial genome: structure, transcription, translation and replication
    • Taanman J.W. The mitochondrial genome: structure, transcription, translation and replication. Biochim. Biophys. Acta 1410 (1999) 103-123
    • (1999) Biochim. Biophys. Acta , vol.1410 , pp. 103-123
    • Taanman, J.W.1
  • 5
    • 0031026069 scopus 로고    scopus 로고
    • Myoclonus epilepsy associated with ragged-red fibers: a G-to-A mutation at nucleotide pair 8363 in mitochondrial tRNA(Lys) in two families
    • Ozawa M., Nishino I., Horai S., Nonaka I., and Goto Y.I. Myoclonus epilepsy associated with ragged-red fibers: a G-to-A mutation at nucleotide pair 8363 in mitochondrial tRNA(Lys) in two families. Muscle Nerve 20 (1997) 271-278
    • (1997) Muscle Nerve , vol.20 , pp. 271-278
    • Ozawa, M.1    Nishino, I.2    Horai, S.3    Nonaka, I.4    Goto, Y.I.5
  • 6
    • 0029962873 scopus 로고    scopus 로고
    • Maternally inherited cardiomyopathy and hearing loss associated with a novel mutation in the mitochondrial tRNA(Lys) gene (G8363A)
    • Santorelli F.M., Mak S.C., El-Schahawi M., Casali C., Shanske S., Baram T.Z., Madrid R.E., and DiMauro S. Maternally inherited cardiomyopathy and hearing loss associated with a novel mutation in the mitochondrial tRNA(Lys) gene (G8363A). Am. J. Hum. Genet. 58 (1996) 933-939
    • (1996) Am. J. Hum. Genet. , vol.58 , pp. 933-939
    • Santorelli, F.M.1    Mak, S.C.2    El-Schahawi, M.3    Casali, C.4    Shanske, S.5    Baram, T.Z.6    Madrid, R.E.7    DiMauro, S.8
  • 7
    • 0026621445 scopus 로고
    • Distribution and threshold expression of the tRNA(Lys) mutation in skeletal muscle of patients with myoclonic epilepsy and ragged-red fibers (MERRF)
    • Boulet L., Karpati G., and Shoubridge E.A. Distribution and threshold expression of the tRNA(Lys) mutation in skeletal muscle of patients with myoclonic epilepsy and ragged-red fibers (MERRF). Am. J. Hum. Genet. 51 (1992) 1187-1200
    • (1992) Am. J. Hum. Genet. , vol.51 , pp. 1187-1200
    • Boulet, L.1    Karpati, G.2    Shoubridge, E.A.3
  • 9
    • 0034030344 scopus 로고    scopus 로고
    • Heterogeneous presentation in A3243G mutation in the mitochondrial tRNA(Leu(UUR)) gene
    • Koga Y., Akita Y., Takane N., Sato Y., and Kato H. Heterogeneous presentation in A3243G mutation in the mitochondrial tRNA(Leu(UUR)) gene. Arch. Dis. Child. 82 (2000) 407-411
    • (2000) Arch. Dis. Child. , vol.82 , pp. 407-411
    • Koga, Y.1    Akita, Y.2    Takane, N.3    Sato, Y.4    Kato, H.5
  • 10
    • 0034683245 scopus 로고    scopus 로고
    • Single-fiber PCR in MELAS(3243) patients: correlations between intratissue distribution and phenotypic expression of the mtDNA(A3243G) genotype
    • Silvestri G., Rana M., Odoardi F., Modoni A., Paris E., Papacci M., Tonali P., and Servidei S. Single-fiber PCR in MELAS(3243) patients: correlations between intratissue distribution and phenotypic expression of the mtDNA(A3243G) genotype. Am. J. Med. Genet. 94 (2000) 201-206
    • (2000) Am. J. Med. Genet. , vol.94 , pp. 201-206
    • Silvestri, G.1    Rana, M.2    Odoardi, F.3    Modoni, A.4    Paris, E.5    Papacci, M.6    Tonali, P.7    Servidei, S.8
  • 12
    • 34249722612 scopus 로고    scopus 로고
    • Yeast cells lacking the mitochondrial gene encoding the ATP synthase subunit 6 exhibit a selective loss of complex IV and unusual mitochondrial morphology
    • Rak M., Tetaud E., Godard F., Sagot I., Salin B., Duvezin-Caubet S., Slonimski P., Rytka J., and di Rago J.P. Yeast cells lacking the mitochondrial gene encoding the ATP synthase subunit 6 exhibit a selective loss of complex IV and unusual mitochondrial morphology. J. Biol. Chem. 282 (2007) 10853-10864
    • (2007) J. Biol. Chem. , vol.282 , pp. 10853-10864
    • Rak, M.1    Tetaud, E.2    Godard, F.3    Sagot, I.4    Salin, B.5    Duvezin-Caubet, S.6    Slonimski, P.7    Rytka, J.8    di Rago, J.P.9
  • 13
    • 0021776095 scopus 로고
    • Mitochondrial adenosine triphosphatase in mit-mutants of Saccharomyces cerevisiase with defective subunit 6 of the enzyme complex
    • Choo W.M., Hadikusumo R.G., and Marzuki S. Mitochondrial adenosine triphosphatase in mit-mutants of Saccharomyces cerevisiase with defective subunit 6 of the enzyme complex. Biochim. Biophys. Acta 806 (1985) 290-304
    • (1985) Biochim. Biophys. Acta , vol.806 , pp. 290-304
    • Choo, W.M.1    Hadikusumo, R.G.2    Marzuki, S.3
  • 14
    • 0024371971 scopus 로고
    • Mitochondrial H+-ATPase in mutants of Saccharomyces cerevisiae with defective subunit 8 of the enzyme complex
    • Marzuki S., Watkins L.C., and Choo W.M. Mitochondrial H+-ATPase in mutants of Saccharomyces cerevisiae with defective subunit 8 of the enzyme complex. Biochim. Biophys. Acta 975 (1989) 222-230
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 222-230
    • Marzuki, S.1    Watkins, L.C.2    Choo, W.M.3
  • 15
    • 0024447422 scopus 로고
    • The role of subunit 4, a nuclear-encoded protein of the F0 sector of yeast mitochondrial ATP synthase, in the assembly of the whole complex
    • Paul M.F., Velours J., Arselin de Chateaubodeau G., Aigle M., and Guerin B. The role of subunit 4, a nuclear-encoded protein of the F0 sector of yeast mitochondrial ATP synthase, in the assembly of the whole complex. Eur. J. Biochem. 185 (1989) 163-171
    • (1989) Eur. J. Biochem. , vol.185 , pp. 163-171
    • Paul, M.F.1    Velours, J.2    Arselin de Chateaubodeau, G.3    Aigle, M.4    Guerin, B.5
  • 16
    • 33748692881 scopus 로고    scopus 로고
    • Ultrastructural changes of mitochondria in the cultivated skin fibroblasts of patients with point mutations in mitochondrial DNA
    • Brantova O., Tesarova M., Hansikova H., Elleder M., Zeman J., and Sladkova J. Ultrastructural changes of mitochondria in the cultivated skin fibroblasts of patients with point mutations in mitochondrial DNA. Ultrastruct. Pathol. 30 (2006) 239-245
    • (2006) Ultrastruct. Pathol. , vol.30 , pp. 239-245
    • Brantova, O.1    Tesarova, M.2    Hansikova, H.3    Elleder, M.4    Zeman, J.5    Sladkova, J.6
  • 17
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger H., and von Jagow G. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199 (1991) 223-231
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schagger, H.1    von Jagow, G.2
  • 20
    • 0002581535 scopus 로고
    • Citrate synthase
    • Colowick S.P., and Kaplan N.O. (Eds)
    • Srere P.A. Citrate synthase. In: Colowick S.P., and Kaplan N.O. (Eds). Methods in Enzymology (1969) 3-26
    • (1969) Methods in Enzymology , pp. 3-26
    • Srere, P.A.1
  • 23
    • 0347761272 scopus 로고    scopus 로고
    • Polarographic evaluation of mitochondrial enzymes activity in isolated mitochondria and in permeabilized human muscle cells with inherited mitochondrial defects
    • Wenchich L., Drahota Z., Honzik T., Hansikova H., Tesarova M., Zeman J., and Houstek J. Polarographic evaluation of mitochondrial enzymes activity in isolated mitochondria and in permeabilized human muscle cells with inherited mitochondrial defects. Physiol. Res. 52 (2003) 781-788
    • (2003) Physiol. Res. , vol.52 , pp. 781-788
    • Wenchich, L.1    Drahota, Z.2    Honzik, T.3    Hansikova, H.4    Tesarova, M.5    Zeman, J.6    Houstek, J.7
  • 26
    • 0346666699 scopus 로고    scopus 로고
    • The yeast counterparts of human 'MELAS' mutations cause mitochondrial dysfunction that can be rescued by overexpression of the mitochondrial translation factor EF-Tu
    • Feuermann M., Francisci S., Rinaldi T., De Luca C., Rohou H., Frontali L., and Bolotin-Fukuhara M. The yeast counterparts of human 'MELAS' mutations cause mitochondrial dysfunction that can be rescued by overexpression of the mitochondrial translation factor EF-Tu. EMBO Rep. 4 (2003) 53-58
    • (2003) EMBO Rep. , vol.4 , pp. 53-58
    • Feuermann, M.1    Francisci, S.2    Rinaldi, T.3    De Luca, C.4    Rohou, H.5    Frontali, L.6    Bolotin-Fukuhara, M.7
  • 27
    • 0037448605 scopus 로고    scopus 로고
    • Nucleo-mitochondrial interactions in Saccharomyces cerevisiae: characterization of a nuclear gene suppressing a defect in mitochondrial tRNA(Asp) processing
    • Rinaldi T., Gambadoro A., Francisci S., and Frontali L. Nucleo-mitochondrial interactions in Saccharomyces cerevisiae: characterization of a nuclear gene suppressing a defect in mitochondrial tRNA(Asp) processing. Gene 303 (2003) 63-68
    • (2003) Gene , vol.303 , pp. 63-68
    • Rinaldi, T.1    Gambadoro, A.2    Francisci, S.3    Frontali, L.4
  • 28
    • 0033010375 scopus 로고    scopus 로고
    • Suppression of a mitochondrial tRNA gene mutation phenotype associated with changes in the nuclear background
    • Hao H., Morrison L.E., and Moraes C.T. Suppression of a mitochondrial tRNA gene mutation phenotype associated with changes in the nuclear background. Hum. Mol. Genet. 8 (1999) 1117-1124
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1117-1124
    • Hao, H.1    Morrison, L.E.2    Moraes, C.T.3
  • 29
    • 0033858002 scopus 로고    scopus 로고
    • A biochemical basis for the inherited susceptibility to aminoglycoside ototoxicity
    • Guan M.X., Fischel-Ghodsian N., and Attardi G. A biochemical basis for the inherited susceptibility to aminoglycoside ototoxicity. Hum. Mol. Genet. 9 (2000) 1787-1793
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1787-1793
    • Guan, M.X.1    Fischel-Ghodsian, N.2    Attardi, G.3
  • 31
    • 34347256160 scopus 로고    scopus 로고
    • Normal levels of wild-type mitochondrial DNA maintain cytochrome c oxidase activity for two pathogenic mitochondrial DNA mutations but not for m.3243A->G
    • Durham S.E., Samuels D.C., Cree L.M., and Chinnery P.F. Normal levels of wild-type mitochondrial DNA maintain cytochrome c oxidase activity for two pathogenic mitochondrial DNA mutations but not for m.3243A->G. Am. J. Hum. Genet. 81 (2007) 189-195
    • (2007) Am. J. Hum. Genet. , vol.81 , pp. 189-195
    • Durham, S.E.1    Samuels, D.C.2    Cree, L.M.3    Chinnery, P.F.4
  • 32
    • 33748643416 scopus 로고    scopus 로고
    • Mitochondrial DNA-deletion mutations accumulate intracellularly to detrimental levels in aged human skeletal muscle fibers
    • Bua E., Johnson J., Herbst A., Delong B., McKenzie D., Salamat S., and Aiken J.M. Mitochondrial DNA-deletion mutations accumulate intracellularly to detrimental levels in aged human skeletal muscle fibers. Am. J. Hum. Genet. 79 (2006) 469-480
    • (2006) Am. J. Hum. Genet. , vol.79 , pp. 469-480
    • Bua, E.1    Johnson, J.2    Herbst, A.3    Delong, B.4    McKenzie, D.5    Salamat, S.6    Aiken, J.M.7
  • 33
    • 34250733466 scopus 로고    scopus 로고
    • Mitochondrial dysfunction, bioenergetic impairment, and metabolic down-regulation in sepsis
    • Levy R.J. Mitochondrial dysfunction, bioenergetic impairment, and metabolic down-regulation in sepsis. Shock 28 (2007) 24-28
    • (2007) Shock , vol.28 , pp. 24-28
    • Levy, R.J.1
  • 34
    • 10644277053 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in liver disease and organ transplantation
    • Hassanein T., and Frederick T. Mitochondrial dysfunction in liver disease and organ transplantation. Mitochondrion 4 (2004) 609-620
    • (2004) Mitochondrion , vol.4 , pp. 609-620
    • Hassanein, T.1    Frederick, T.2
  • 35
    • 0029063911 scopus 로고
    • Myoclonic epilepsy with ragged-red fibers (MERRF): an immunohistochemical study of the brain
    • Sparaco M., Schon E.A., DiMauro S., and Bonilla E. Myoclonic epilepsy with ragged-red fibers (MERRF): an immunohistochemical study of the brain. Brain Pathol. 5 (1995) 125-133
    • (1995) Brain Pathol. , vol.5 , pp. 125-133
    • Sparaco, M.1    Schon, E.A.2    DiMauro, S.3    Bonilla, E.4
  • 36
    • 0035794142 scopus 로고    scopus 로고
    • Impaired ATP synthase assembly associated with a mutation in the human ATP synthase subunit 6 gene
    • Nijtmans L.G., Henderson N.S., Attardi G., and Holt I.J. Impaired ATP synthase assembly associated with a mutation in the human ATP synthase subunit 6 gene. J. Biol. Chem. 276 (2001) 6755-6762
    • (2001) J. Biol. Chem. , vol.276 , pp. 6755-6762
    • Nijtmans, L.G.1    Henderson, N.S.2    Attardi, G.3    Holt, I.J.4
  • 38
    • 0029560518 scopus 로고
    • Assembly of mitochondrial ATP synthase in cultured human cells: implications for mitochondrial diseases
    • Nijtmans L.G., Klement P., Houstek J., and van den Bogert C. Assembly of mitochondrial ATP synthase in cultured human cells: implications for mitochondrial diseases. Biochim. Biophys. Acta 1272 (1995) 190-198
    • (1995) Biochim. Biophys. Acta , vol.1272 , pp. 190-198
    • Nijtmans, L.G.1    Klement, P.2    Houstek, J.3    van den Bogert, C.4
  • 39
    • 0034177951 scopus 로고    scopus 로고
    • Tissue variation in the control of oxidative phosphorylation: implication for mitochondrial diseases
    • Rossignol R., Letellier T., Malgat M., Rocher C., and Mazat J.P. Tissue variation in the control of oxidative phosphorylation: implication for mitochondrial diseases. Biochem. J. 347 Pt 1 (2000) 45-53
    • (2000) Biochem. J. , vol.347 , Issue.PART 1 , pp. 45-53
    • Rossignol, R.1    Letellier, T.2    Malgat, M.3    Rocher, C.4    Mazat, J.P.5
  • 41
    • 0345255615 scopus 로고    scopus 로고
    • The two rotor components of yeast mitochondrial ATP synthase are mechanically coupled by subunit delta
    • Duvezin-Caubet S., Caron M., Giraud M.F., Velours J., and di Rago J.P. The two rotor components of yeast mitochondrial ATP synthase are mechanically coupled by subunit delta. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 13235-13240
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 13235-13240
    • Duvezin-Caubet, S.1    Caron, M.2    Giraud, M.F.3    Velours, J.4    di Rago, J.P.5
  • 42
    • 0027459190 scopus 로고
    • ATP synthase of yeast mitochondria. Isolation and disruption of the ATP epsilon gene
    • Guelin E., Chevallier J., Rigoulet M., Guerin B., and Velours J. ATP synthase of yeast mitochondria. Isolation and disruption of the ATP epsilon gene. J. Biol. Chem. 268 (1993) 161-167
    • (1993) J. Biol. Chem. , vol.268 , pp. 161-167
    • Guelin, E.1    Chevallier, J.2    Rigoulet, M.3    Guerin, B.4    Velours, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.