메뉴 건너뛰기




Volumn 45, Issue 13, 2017, Pages 8091-8104

Alternative stable conformation capable of protein misinteraction links tRNA synthetase to peripheral neuropathy

Author keywords

[No Author keywords available]

Indexed keywords

TYROSINE TRANSFER RNA LIGASE; MUTANT PROTEIN; PROTEIN BINDING; RECOMBINANT PROTEIN; REPRESSOR PROTEIN; TRIM28 PROTEIN, HUMAN;

EID: 85026399899     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkx455     Document Type: Article
Times cited : (34)

References (53)
  • 1
    • 0016266593 scopus 로고
    • Genetic and clinical aspects of Charcot-Marie-Tooth's disease
    • Skre, H. (1974) Genetic and clinical aspects of Charcot-Marie-Tooth's disease. Clin. Genet., 6, 98-118.
    • (1974) Clin. Genet , vol.6 , pp. 98-118
    • Skre, H.1
  • 9
    • 0027255483 scopus 로고
    • Cognition, mechanism, and evolutionary relationships in aminoacyl-tRNA synthetases
    • Carter, C.W. Jr (1993) Cognition, mechanism, and evolutionary relationships in aminoacyl-tRNA synthetases. Annu. Rev. Biochem., 62, 715-748.
    • (1993) Annu. Rev. Biochem , vol.62 , pp. 715-748
    • Carter, C.W.1
  • 10
    • 33750998821 scopus 로고    scopus 로고
    • The early history of tRNA recognition by aminoacyl-tRNA synthetases
    • Giege, R. (2006) The early history of tRNA recognition by aminoacyl-tRNA synthetases. J. Biosci., 31, 477-488.
    • (2006) J. Biosci , vol.31 , pp. 477-488
    • Giege, R.1
  • 11
    • 0034053846 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process
    • Woese, C.R., Olsen, G.J., Ibba, M. and Soll, D. (2000) Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process. Microbiol. Mol. Biol. Rev., 64, 202-236.
    • (2000) Microbiol. Mol. Biol. Rev , vol.64 , pp. 202-236
    • Woese, C.R.1    Olsen, G.J.2    Ibba, M.3    Soll, D.4
  • 14
    • 71549128376 scopus 로고    scopus 로고
    • Functional expansion of human tRNA synthetases achieved by structural inventions
    • Guo, M., Schimmel, P. and Yang, X.L. (2010) Functional expansion of human tRNA synthetases achieved by structural inventions. FEBS Lett., 584, 434-442.
    • (2010) FEBS Lett , vol.584 , pp. 434-442
    • Guo, M.1    Schimmel, P.2    Yang, X.L.3
  • 15
    • 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
  • 16
    • 80053152058 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases and tumorigenesis: More than housekeeping
    • Kim, S., You, S. and Hwang, D. (2011) Aminoacyl-tRNA synthetases and tumorigenesis: more than housekeeping. Nat. Rev. Cancer, 11, 708-718.
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 708-718
    • Kim, S.1    You, S.2    Hwang, D.3
  • 18
    • 75749132024 scopus 로고    scopus 로고
    • GARS axonopathy: Not every neuron's cup of tRNA
    • Motley, W.W., Talbot, K. and Fischbeck, K.H. (2010) GARS axonopathy: not every neuron's cup of tRNA. Trends Neurosci., 33, 59-66.
    • (2010) Trends Neurosci , vol.33 , pp. 59-66
    • Motley, W.W.1    Talbot, K.2    Fischbeck, K.H.3
  • 20
    • 79961094170 scopus 로고    scopus 로고
    • Dispersed disease-causing neomorphic mutations on a single protein promote the same localized conformational opening
    • He, W., Zhang, H.M., Chong, Y.E., Guo, M., Marshall, A.G. and Yang, X.L. (2011) Dispersed disease-causing neomorphic mutations on a single protein promote the same localized conformational opening. Proc. Natl. Acad. Sci. U.S.A., 108, 12307-12312.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 12307-12312
    • He, W.1    Zhang, H.M.2    Chong, Y.E.3    Guo, M.4    Marshall, A.G.5    Yang, X.L.6
  • 21
  • 22
    • 84937512242 scopus 로고    scopus 로고
    • Rare variants in methionyl- and tyrosyl-tRNA synthetase genes in late-onset autosomal dominant Charcot-Marie-Tooth neuropathy
    • Hyun, Y.S., Park, H.J., Heo, S.H., Yoon, B.R., Nam, S.H., Kim, S.B., Park, C.I., Choi, B.O. and Chung, K.W. (2014) Rare variants in methionyl- and tyrosyl-tRNA synthetase genes in late-onset autosomal dominant Charcot-Marie-Tooth neuropathy. Clin. Genet., 86, 592-594.
    • (2014) Clin. Genet , vol.86 , pp. 592-594
    • Hyun, Y.S.1    Park, H.J.2    Heo, S.H.3    Yoon, B.R.4    Nam, S.H.5    Kim, S.B.6    Park, C.I.7    Choi, B.O.8    Chung, K.W.9
  • 24
    • 80051754461 scopus 로고    scopus 로고
    • Dominant Intermediate Charcot-Marie-Tooth disorder is not due to a catalytic defect in tyrosyl-tRNA synthetase
    • Froelich, C.A. and First, E.A. (2011) Dominant Intermediate Charcot-Marie-Tooth disorder is not due to a catalytic defect in tyrosyl-tRNA synthetase. Biochemistry, 50, 7132-7145.
    • (2011) Biochemistry , vol.50 , pp. 7132-7145
    • Froelich, C.A.1    First, E.A.2
  • 26
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • Whitmore, L. and Wallace, B.A. (2008) Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers, 89, 392-400.
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 29
    • 0242571958 scopus 로고    scopus 로고
    • Small-angle scattering studies of biological macromolecules in solution
    • Svergun, D.I. and Koch, M.H.J. (2003) Small-angle scattering studies of biological macromolecules in solution. Rep. Prog. Phys., 66, 1735-1782.
    • (2003) Rep. Prog. Phys , vol.66 , pp. 1735-1782
    • Svergun, D.I.1    Koch, M.H.J.2
  • 30
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering
    • Franke, D. and Svergun, D.I. (2009) DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering. J. Appl. Crystallogr., 42, 342-346.
    • (2009) J. Appl. Crystallogr , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 31
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov, V.V. and Svergun, D.I. (2003) Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr., 36, 860-864.
    • (2003) J. Appl. Crystallogr , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 32
    • 79955961854 scopus 로고    scopus 로고
    • Mechanism of intracellular cAMP sensor Epac2 activation: CAMP-induced conformational changes identified by amide hydrogen/deuterium exchange mass spectrometry (DXMS)
    • Li, S., Tsalkova, T., White, M.A., Mei, F.C., Liu, T., Wang, D., Woods, V.L. Jr and Cheng, X. (2011) Mechanism of intracellular cAMP sensor Epac2 activation: cAMP-induced conformational changes identified by amide hydrogen/deuterium exchange mass spectrometry (DXMS). J. Biol. Chem., 286, 17889-17897.
    • (2011) J. Biol. Chem , vol.286 , pp. 17889-17897
    • Li, S.1    Tsalkova, T.2    White, M.A.3    Mei, F.C.4    Liu, T.5    Wang, D.6    Woods, V.L.7    Cheng, X.8
  • 34
    • 84868575176 scopus 로고    scopus 로고
    • Minimizing back exchange in the hydrogen exchange-mass spectrometry experiment
    • Walters, B.T., Ricciuti, A., Mayne, L. and Englander, S.W. (2012) Minimizing back exchange in the hydrogen exchange-mass spectrometry experiment. J. Am. Soc. Mass Spectrom., 23, 2132-2139.
    • (2012) J. Am. Soc. Mass Spectrom , vol.23 , pp. 2132-2139
    • Walters, B.T.1    Ricciuti, A.2    Mayne, L.3    Englander, S.W.4
  • 35
    • 84881656622 scopus 로고    scopus 로고
    • Structural insights into fibrinogen dynamics using amide hydrogen/deuterium exchange mass spectrometry
    • Marsh, J.J., Guan, H.S., Li, S., Chiles, P.G., Tran, D. and Morris, T.A. (2013) Structural insights into fibrinogen dynamics using amide hydrogen/deuterium exchange mass spectrometry. Biochemistry, 52, 5491-5502.
    • (2013) Biochemistry , vol.52 , pp. 5491-5502
    • Marsh, J.J.1    Guan, H.S.2    Li, S.3    Chiles, P.G.4    Tran, D.5    Morris, T.A.6
  • 36
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
    • Zhang, Z. and Smith, D.L. (1993) Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation. Protein Sci., 2, 522-531.
    • (1993) Protein Sci , vol.2 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 38
    • 0037099498 scopus 로고    scopus 로고
    • Class i tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition
    • Yaremchuk, A., Kriklivyi, I., Tukalo, M. and Cusack, S. (2002) Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition. EMBO J., 21, 3829-3840.
    • (2002) EMBO J , vol.21 , pp. 3829-3840
    • Yaremchuk, A.1    Kriklivyi, I.2    Tukalo, M.3    Cusack, S.4
  • 39
    • 0030945598 scopus 로고    scopus 로고
    • Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine
    • Kleeman, T.A., Wei, D., Simpson, K.L. and First, E.A. (1997) Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine. J. Biol. Chem., 272, 14420-14425.
    • (1997) J. Biol. Chem , vol.272 , pp. 14420-14425
    • Kleeman, T.A.1    Wei, D.2    Simpson, K.L.3    First, E.A.4
  • 40
    • 0033515887 scopus 로고    scopus 로고
    • Two distinct cytokines released from a human aminoacyl-tRNA synthetase
    • Wakasugi, K. and Schimmel, P. (1999) Two distinct cytokines released from a human aminoacyl-tRNA synthetase. Science, 284, 147-151.
    • (1999) Science , vol.284 , pp. 147-151
    • Wakasugi, K.1    Schimmel, P.2
  • 41
    • 0038014233 scopus 로고    scopus 로고
    • Crystal structure of an EMAP-II-like cytokine released from a human tRNA synthetase
    • Yang, X.L., Liu, J., Skene, R.J., McRee, D.E. and Schimmel, P. (2003) Crystal structure of an EMAP-II-like cytokine released from a human tRNA synthetase. Helv. Chim. Acta., 86, 1246-1257.
    • (2003) Helv. Chim. Acta , vol.86 , pp. 1246-1257
    • Yang, X.L.1    Liu, J.2    Skene, R.J.3    McRee, D.E.4    Schimmel, P.5
  • 42
    • 84862001100 scopus 로고    scopus 로고
    • Uncovering of a short internal peptide activates a tRNA synthetase procytokine
    • Lee, P.S., Zhang, H.M., Marshall, A.G., Yang, X.L. and Schimmel, P. (2012) Uncovering of a short internal peptide activates a tRNA synthetase procytokine. J. Biol. Chem., 287, 20504-20508.
    • (2012) J. Biol. Chem , vol.287 , pp. 20504-20508
    • Lee, P.S.1    Zhang, H.M.2    Marshall, A.G.3    Yang, X.L.4    Schimmel, P.5
  • 43
    • 84892758904 scopus 로고    scopus 로고
    • Molecular dynamics of DNA-protein conjugates on electrified surfaces: Solutions to the drift-diffusion equation
    • Langer, A., Kaiser, W., Svejda, M., Schwertler, P. and Rant, U. (2014) Molecular dynamics of DNA-protein conjugates on electrified surfaces: solutions to the drift-diffusion equation. J. Phys. Chem. B, 118, 597-607.
    • (2014) J. Phys. Chem. B , vol.118 , pp. 597-607
    • Langer, A.1    Kaiser, W.2    Svejda, M.3    Schwertler, P.4    Rant, U.5
  • 44
    • 84863357487 scopus 로고    scopus 로고
    • TRNA-controlled nuclear import of a human tRNA synthetase
    • Fu, G., Xu, T., Shi, Y., Wei, N. and Yang, X.L. (2012) tRNA-controlled nuclear import of a human tRNA synthetase. J. Biol. Chem., 287, 9330-9334.
    • (2012) J. Biol. Chem , vol.287 , pp. 9330-9334
    • Fu, G.1    Xu, T.2    Shi, Y.3    Wei, N.4    Yang, X.L.5
  • 46
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto, C. (2003) Unfolding the role of protein misfolding in neurodegenerative diseases. Nat. Rev. Neurosci., 4, 49-60.
    • (2003) Nat. Rev. Neurosci , vol.4 , pp. 49-60
    • Soto, C.1
  • 47
    • 84901355639 scopus 로고    scopus 로고
    • The amyloid state and its association with protein misfolding diseases
    • Knowles, T.P., Vendruscolo, M. and Dobson, C.M. (2014) The amyloid state and its association with protein misfolding diseases. Nat. Rev. Mol. Cell. Biol., 15, 384-396.
    • (2014) Nat. Rev. Mol. Cell. Biol , vol.15 , pp. 384-396
    • Knowles, T.P.1    Vendruscolo, M.2    Dobson, C.M.3
  • 48
    • 84866702836 scopus 로고    scopus 로고
    • Alpha-Synuclein in Parkinson's disease
    • Stefanis, L. (2012) alpha-Synuclein in Parkinson's disease. Cold Spring Harb. Perspect. Med., 2, a009399.
    • (2012) Cold Spring Harb. Perspect. Med , vol.2 , pp. a009399
    • Stefanis, L.1
  • 49
    • 84892408458 scopus 로고    scopus 로고
    • Mechanisms of protein-folding diseases at a glance
    • Valastyan, J.S. and Lindquist, S. (2014) Mechanisms of protein-folding diseases at a glance. Dis. Model. Mech., 7, 9-14.
    • (2014) Dis. Model. Mech , vol.7 , pp. 9-14
    • Valastyan, J.S.1    Lindquist, S.2
  • 50
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fandrich, M., Fletcher, M.A. and Dobson, C.M. (2001) Amyloid fibrils from muscle myoglobin. Nature, 410, 165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 51
    • 34547478151 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease-associated mutant tRNA synthetases linked to altered dimer interface and neurite distribution defect
    • Nangle, L.A., Zhang, W., Xie, W., Yang, X.L. and Schimmel, P. (2007) Charcot-Marie-Tooth disease-associated mutant tRNA synthetases linked to altered dimer interface and neurite distribution defect. Proc. Natl. Acad. Sci. U.S.A., 104, 11239-11244.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 11239-11244
    • Nangle, L.A.1    Zhang, W.2    Xie, W.3    Yang, X.L.4    Schimmel, P.5
  • 53
    • 84983417725 scopus 로고    scopus 로고
    • Peripheral neuropathy via mutant tRNA synthetases: Inhibition of protein translation provides a possible explanation
    • Storkebaum, E. (2016) Peripheral neuropathy via mutant tRNA synthetases: Inhibition of protein translation provides a possible explanation. Bioessays, 38, 818-829.
    • (2016) Bioessays , vol.38 , pp. 818-829
    • Storkebaum, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.