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Volumn 433, Issue 3, 2011, Pages 441-446

A human pathology-related mutation prevents import of an aminoacyl-tRNA synthetase into mitochondria

Author keywords

Aminoacyl tRNA synthetase; Organelle; Pathology related mutation; Protein import; Translation machinery; Translocation

Indexed keywords

AMINOACYL TRANSFER RNA; SYNTHETASE;

EID: 78751529272     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20101902     Document Type: Article
Times cited : (18)

References (27)
  • 2
    • 77953507107 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations in disease and aging
    • Wallace, D. C. (2010) Mitochondrial DNA mutations in disease and aging. Environ. Mol. Mutagen. 51, 440-450
    • (2010) Environ. Mol. Mutagen. , vol.51 , pp. 440-450
    • Wallace, D.C.1
  • 3
    • 19444380425 scopus 로고    scopus 로고
    • Nuclear genes and mitochondrial translation: A new class of genetic disease
    • Jacobs, H. T. and Turnbull, D. M. (2005) Nuclear genes and mitochondrial translation: a new class of genetic disease. Trends Genet. 21, 312-314
    • (2005) Trends Genet. , vol.21 , pp. 312-314
    • Jacobs, H.T.1    Turnbull, D.M.2
  • 5
    • 78650210763 scopus 로고    scopus 로고
    • Leukoencephalopathy with brainstem and spinal cord involvement and normal lactate: A new mutation in the DARS2 gene
    • Lin, J., Faria, E. C., Da Rocha, A. J., Masruha, M. R., Vilanova, L. C., Scheper, G. C. and Van Der Knaap, M. S. (2010) Leukoencephalopathy with brainstem and spinal cord involvement and normal lactate: a new mutation in the DARS2 gene. J. Child. Neurol. 25, 1425-1428
    • (2010) J. Child. Neurol. , vol.25 , pp. 1425-1428
    • Lin, J.1    Faria, E.C.2    Da Rocha, A.J.3    Masruha, M.R.4    Vilanova, L.C.5    Scheper, G.C.6    Van Der Knaap, M.S.7
  • 7
    • 35348983348 scopus 로고    scopus 로고
    • Deleterious mutation in the mitochondrial arginyl-transfer RNA synthetase gene is associated with pontocerebellar hypoplasia
    • Edvardson, S., Shaag, A., Kolesnikova, O., Gomori, J. M., Tarassov, I., Einbinder, T., Saada, A. and Elpeleg, O. (2007) Deleterious mutation in the mitochondrial arginyl-transfer RNA synthetase gene is associated with pontocerebellar hypoplasia. Am. J. Hum. Genet. 81, 857-862
    • (2007) Am. J. Hum. Genet. , vol.81 , pp. 857-862
    • Edvardson, S.1    Shaag, A.2    Kolesnikova, O.3    Gomori, J.M.4    Tarassov, I.5    Einbinder, T.6    Saada, A.7    Elpeleg, O.8
  • 10
    • 34547224267 scopus 로고    scopus 로고
    • Long-range structural effects of a Charcot-Marie-Tooth disease-causing mutation in human glycyl-tRNA synthetase
    • Xie, W., Nangle, L. A., Zhang, W., Schimmel, P. and Yang, X. L. (2007) Long-range structural effects of a Charcot-Marie-Tooth disease-causing mutation in human glycyl-tRNA synthetase. Proc. Natl. Acad. Sci. U.S.A. 104, 9976-9981
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 9976-9981
    • Xie, W.1    Nangle, L.A.2    Zhang, W.3    Schimmel, P.4    Yang, X.L.5
  • 11
    • 15444367104 scopus 로고    scopus 로고
    • Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: Characterization of AspRS and TyrRS
    • DOI 10.1021/bi047527z
    • Bonnefond, L., Fender, A., Rudinger-Thirion, J., Gieǵe, R., Florentz, C. and Sissler, M. (2005) Towards the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS. Biochemistry 44, 4805-4816 (Pubitemid 40396759)
    • (2005) Biochemistry , vol.44 , Issue.12 , pp. 4805-4816
    • Bonnefond, L.1    Fender, A.2    Rudinger-Thirion, J.3    Giege, R.4    Florentz, C.5    Sissler, M.6
  • 13
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert, W. and Herrmann, J. M. (2007) Translocation of proteins into mitochondria. Annu. Rev. Biochem. 76, 723-749
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 14
    • 34848823742 scopus 로고    scopus 로고
    • Mitochondrial protein-import machinery: Correlating structure with function
    • Baker, M. J., Frazier, A. E., Gulbis, J. M. and Ryan, M. T. (2007) Mitochondrial protein-import machinery: correlating structure with function. Trends Cell Biol. 17, 456-464
    • (2007) Trends Cell Biol. , vol.17 , pp. 456-464
    • Baker, M.J.1    Frazier, A.E.2    Gulbis, J.M.3    Ryan, M.T.4
  • 15
  • 16
    • 77953020406 scopus 로고    scopus 로고
    • On the mechanism of preprotein import by the mitochondrial presequence translocase
    • Van Der Laan, M., Hutu, D. P. and Rehling, P. (2010) On the mechanism of preprotein import by the mitochondrial presequence translocase. Biochim. Biophys. Acta 1803, 732-739
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 732-739
    • Van Der Laan, M.1    Hutu, D.P.2    Rehling, P.3
  • 18
    • 0029788381 scopus 로고    scopus 로고
    • The role of positive charges and structural segments in the presequence of rat liver aldehyde dehydrogenase in import into mitochondria
    • Hammen, P. K., Waltner, M., Hahnemann, B., Heard, T. S. and Weiner, H. (1996) The role of positive charges and structural segments in the presequence of rat liver aldehyde dehydrogenase in import into mitochondria. J. Biol. Chem. 271, 21041-21048
    • (1996) J. Biol. Chem. , vol.271 , pp. 21041-21048
    • Hammen, P.K.1    Waltner, M.2    Hahnemann, B.3    Heard, T.S.4    Weiner, H.5
  • 19
    • 0024468352 scopus 로고
    • Purification and characterization of a processing protease from rat liver mitochondria
    • Ou, W. J., Ito, A., Okazaki, H. and Omura, T. (1989) Purification and characterization of a processing protease from rat liver mitochondria. EMBO J. 8, 2605-2612 (Pubitemid 19273345)
    • (1989) EMBO Journal , vol.8 , Issue.9 , pp. 2605-2612
    • Ou, W.-J.1    Okazaki, H.2    Omura, T.3
  • 20
    • 37549015259 scopus 로고    scopus 로고
    • Precursor protein is readily degraded in mitochondrial matrix space if the leader is not processed by mitochondrial processing peptidase
    • Mukhopadhyay, A., Yang, C. S., Wei, B. and Weiner, H. (2007) Precursor protein is readily degraded in mitochondrial matrix space if the leader is not processed by mitochondrial processing peptidase. J. Biol. Chem. 282, 37266-37275
    • (2007) J. Biol. Chem. , vol.282 , pp. 37266-37275
    • Mukhopadhyay, A.1    Yang, C.S.2    Wei, B.3    Weiner, H.4
  • 21
    • 34247562746 scopus 로고    scopus 로고
    • How can organellar protein N-terminal sequences be dual targeting signals? In silico analysis and mutagenesis approach
    • Pujol, C., Maréchal-Drouard, L. and Duchêne, A. M. (2007) How can organellar protein N-terminal sequences be dual targeting signals? In silico analysis and mutagenesis approach. J. Mol. Biol. 369, 356-367
    • (2007) J. Mol. Biol. , vol.369 , pp. 356-367
    • Pujol, C.1    Maréchal-Drouard, L.2    Duchêne, A.M.3
  • 22
    • 77956095201 scopus 로고    scopus 로고
    • New functions of aminoacyl-tRNA synthetases beyond translation
    • Guo, M., Yang, X. L. and Schimmel, P. (2010) New functions of aminoacyl-tRNA synthetases beyond translation. Nat. Rev. Mol. Cell Biol. 11, 668-674
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 668-674
    • Guo, M.1    Yang, X.L.2    Schimmel, P.3
  • 23
    • 34247127747 scopus 로고    scopus 로고
    • Mitochondrial protein import and human health and disease
    • MacKenzie, J. A. and Payne, R. M. (2007) Mitochondrial protein import and human health and disease. Biochim. Biophys. Acta 1772, 509-523
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 509-523
    • MacKenzie, J.A.1    Payne, R.M.2
  • 25
    • 33646427709 scopus 로고    scopus 로고
    • Mutation of DNAJC19, a human homologue of yeast inner mitochondrial membrane co-chaperones, causes DCMA syndrome, a novel autosomal recessive Barth syndrome-like condition
    • Davey, K. M., Parboosingh, J. S., McLeod, D. R., Chan, A., Casey, R., Ferreira, P., Snyder, F. F., Bridge, P. J. and Bernier, F. P. (2006) Mutation of DNAJC19, a human homologue of yeast inner mitochondrial membrane co-chaperones, causes DCMA syndrome, a novel autosomal recessive Barth syndrome-like condition. J. Med. Genet. 43, 385-393
    • (2006) J. Med. Genet. , vol.43 , pp. 385-393
    • Davey, K.M.1    Parboosingh, J.S.2    McLeod, D.R.3    Chan, A.4    Casey, R.5    Ferreira, P.6    Snyder, F.F.7    Bridge, P.J.8    Bernier, F.P.9
  • 26
    • 0029162897 scopus 로고
    • An amino acid substitution in the pyruvate dehydrogenase E1 alpha gene, affecting mitochondrial import of the precursor protein
    • Takakubo, F., Cartwright, P., Hoogenraad, N., Thorburn, D. R., Collins, F., Lithgow, T. and Dahl, H. H. (1995) An amino acid substitution in the pyruvate dehydrogenase E1 alpha gene, affecting mitochondrial import of the precursor protein. Am. J. Hum. Genet. 57, 772-780
    • (1995) Am. J. Hum. Genet. , vol.57 , pp. 772-780
    • Takakubo, F.1    Cartwright, P.2    Hoogenraad, N.3    Thorburn, D.R.4    Collins, F.5    Lithgow, T.6    Dahl, H.H.7
  • 27
    • 0037339203 scopus 로고    scopus 로고
    • 16Val genetic dimorphism modulates the import of human manganese superoxide dismutase into rat liver mitochondria
    • DOI 10.1097/00008571-200303000-00004
    • Sutton, A., Khoury, H., Prip-Buus, C., Cepanec, C., Pessayre, D. and Degoul, F. (2003) The Ala16Val genetic dimorphism modulates the import of human manganese superoxide dismutase into rat liver mitochondria. Pharmacogenetics 13, 145-157 (Pubitemid 36324244)
    • (2003) Pharmacogenetics , vol.13 , Issue.3 , pp. 145-157
    • Sutton, A.1    Khoury, H.2    Prip-Buus, C.3    Cepanec, C.4    Pessayre, D.5    Degoul, F.6


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