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Volumn 43, Issue 21, 2015, Pages 10534-10545

SerRS-tRNASec complex structures reveal mechanism of the first step in selenocysteine biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

SELENOCYSTEINE; SERINE TRANSFER RNA LIGASE; PROTEIN BINDING; TRANSFER RNA; TRNA, SELENOCYSTEINE-;

EID: 84983770694     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkv996     Document Type: Article
Times cited : (39)

References (45)
  • 1
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba, M. and Söll, D. (2000) Aminoacyl-tRNA synthesis. Annu. Rev. Biochem., 69, 617-650.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 617-650
    • Ibba, M.1    Söll, D.2
  • 2
    • 0345436050 scopus 로고    scopus 로고
    • Selenocysteine inserting tRNAs: An overview
    • Commans, S. and Böck, A. (1999) Selenocysteine inserting tRNAs: an overview. FEMS Microbiol. Rev., 23, 335-351.
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 335-351
    • Commans, S.1    Böck, A.2
  • 3
    • 0023907071 scopus 로고
    • Gene for a novel tRNA species that accepts L-serine and cotranslationally inserts selenocysteine
    • Leinfelder, W., Zehelein, E., Mandrand-Berthelot, M.A. and Böck, A. (1988) Gene for a novel tRNA species that accepts L-serine and cotranslationally inserts selenocysteine. Nature, 331, 723-725.
    • (1988) Nature , vol.331 , pp. 723-725
    • Leinfelder, W.1    Zehelein, E.2    Mandrand-Berthelot, M.A.3    Böck, A.4
  • 5
    • 0034662094 scopus 로고    scopus 로고
    • The importance of selenium to human health
    • Rayman, M.P. (2000) The importance of selenium to human health. Lancet, 356, 233-241.
    • (2000) Lancet , vol.356 , pp. 233-241
    • Rayman, M.P.1
  • 8
    • 0025043116 scopus 로고
    • A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å
    • Cusack, S., Berthet-Colominas, C., Hartlein, M., Nassar, N. and Leberman, R. (1990) A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å. Nature, 347, 249-255.
    • (1990) Nature , vol.347 , pp. 249-255
    • Cusack, S.1    Berthet-Colominas, C.2    Hartlein, M.3    Nassar, N.4    Leberman, R.5
  • 9
    • 0035951403 scopus 로고    scopus 로고
    • Two classes of tRNA synthetases suggested by sterically compatible dockings on tRNA acceptor stem
    • Ribas de Pouplana, L. and Schimmel, P. (2001) Two classes of tRNA synthetases suggested by sterically compatible dockings on tRNA acceptor stem. Cell, 104, 191-193.
    • (2001) Cell , vol.104 , pp. 191-193
    • Ribas De Pouplana, L.1    Schimmel, P.2
  • 10
    • 0035788034 scopus 로고    scopus 로고
    • Formation of two classes of tRNA synthetases in relation to editing functions and genetic code
    • Schimmel, P. and Ribas de Pouplana, L. (2001) Formation of two classes of tRNA synthetases in relation to editing functions and genetic code. Cold Spring Harb. Symp. Quant. Biol., 66, 161-166.
    • (2001) Cold Spring Harb. Symp. Quant. Biol. , vol.66 , pp. 161-166
    • Schimmel, P.1    Ribas De Pouplana, L.2
  • 11
    • 0027741164 scopus 로고
    • The long extra arms of human tRNASer/Sec and tRNASer function as major identify elements for serylation in an orientation-dependent, but not sequence-specific manner
    • Wu, X.Q. and Gross, H.J. (1993) The long extra arms of human tRNASer/Sec and tRNASer function as major identify elements for serylation in an orientation-dependent, but not sequence-specific manner. Nucleic Acids Res., 21, 5589-5594.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5589-5594
    • Wu, X.Q.1    Gross, H.J.2
  • 13
    • 84874028131 scopus 로고    scopus 로고
    • Essential nontranslational functions of tRNA synthetases
    • Guo, M. and Schimmel, P. (2013) Essential nontranslational functions of tRNA synthetases. Nat. Chem. Biol., 9, 145-153.
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 145-153
    • Guo, M.1    Schimmel, P.2
  • 14
    • 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
  • 15
    • 67649891971 scopus 로고    scopus 로고
    • Noncanonical activity of seryl-tRNA synthetase is involved in vascular development
    • Fukui, H., Hanaoka, R. and Kawahara, A. (2009) Noncanonical activity of seryl-tRNA synthetase is involved in vascular development. Circ. Res., 104, 1253-1259.
    • (2009) Circ. Res. , vol.104 , pp. 1253-1259
    • Fukui, H.1    Hanaoka, R.2    Kawahara, A.3
  • 16
    • 0028105601 scopus 로고
    • The 2.9 Å crystal structure of T. Thermophilus seryl-tRNA synthetase complexed with tRNASer
    • Biou, V., Yaremchuk, A., Tukalo, M. and Cusack, S. (1994) The 2.9 Å crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNASer. Science, 263, 1404-1410.
    • (1994) Science , vol.263 , pp. 1404-1410
    • Biou, V.1    Yaremchuk, A.2    Tukalo, M.3    Cusack, S.4
  • 17
    • 84880533031 scopus 로고    scopus 로고
    • Tertiary structure of bacterial selenocysteine tRNA
    • Itoh, Y., Sekine, S., Suetsugu, S. and Yokoyama, S. (2013) Tertiary structure of bacterial selenocysteine tRNA. Nucleic Acids Res., 41, 6729-6738.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 6729-6738
    • Itoh, Y.1    Sekine, S.2    Suetsugu, S.3    Yokoyama, S.4
  • 18
    • 84876314972 scopus 로고    scopus 로고
    • Decameric SelA-tRNASec ring structure reveals mechanism of bacterial selenocysteine formation
    • Itoh, Y., Brocker, M.J., Sekine, S., Hammond, G., Suetsugu, S., Söll, D. and Yokoyama, S. (2013) Decameric SelA-tRNASec ring structure reveals mechanism of bacterial selenocysteine formation. Science, 340, 75-78.
    • (2013) Science , vol.340 , pp. 75-78
    • Itoh, Y.1    Brocker, M.J.2    Sekine, S.3    Hammond, G.4    Suetsugu, S.5    Söll, D.6    Yokoyama, S.7
  • 19
    • 77955486749 scopus 로고    scopus 로고
    • Structural basis for the major role of O-phosphoseryl-tRNA kinase in the UGA-specific encoding of selenocysteine
    • Chiba, S., Itoh, Y., Sekine, S. and Yokoyama, S. (2010) Structural basis for the major role of O-phosphoseryl-tRNA kinase in the UGA-specific encoding of selenocysteine. Mol. Cell, 39, 410-420.
    • (2010) Mol. Cell , vol.39 , pp. 410-420
    • Chiba, S.1    Itoh, Y.2    Sekine, S.3    Yokoyama, S.4
  • 20
    • 67650815502 scopus 로고    scopus 로고
    • The human SepSecS-tRNASec complex reveals the mechanism of selenocysteine formation
    • Palioura, S., Sherrer, R.L., Steitz, T.A., Söll, D. and Simonović, M. (2009) The human SepSecS-tRNASec complex reveals the mechanism of selenocysteine formation. Science, 325, 321-325.
    • (2009) Science , vol.325 , pp. 321-325
    • Palioura, S.1    Sherrer, R.L.2    Steitz, T.A.3    Söll, D.4    Simonović, M.5
  • 21
    • 84887404590 scopus 로고    scopus 로고
    • Crystal structure of human Seryl-tRNA synthetase and Ser-SA complex reveals a molecular lever specific to higher eukaryotes
    • Xu, X., Shi, Y. and Yang, X.L. (2013) Crystal structure of human Seryl-tRNA synthetase and Ser-SA complex reveals a molecular lever specific to higher eukaryotes. Structure, 21, 2078-2086.
    • (2013) Structure , vol.21 , pp. 2078-2086
    • Xu, X.1    Shi, Y.2    Yang, X.L.3
  • 22
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol., 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 24
    • 70350643682 scopus 로고    scopus 로고
    • Crystal structure of human selenocysteine tRNA
    • Itoh, Y., Chiba, S., Sekine, S. and Yokoyama, S. (2009) Crystal structure of human selenocysteine tRNA. Nucleic Acids Res., 37, 6259-6268.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 6259-6268
    • Itoh, Y.1    Chiba, S.2    Sekine, S.3    Yokoyama, S.4
  • 27
    • 79956351622 scopus 로고    scopus 로고
    • Crystal structure analysis reveals functional flexibility in the selenocysteine-specific tRNA from mouse
    • Ganichkin, O.M., Anedchenko, E.A. and Wahl, M.C. (2011) Crystal structure analysis reveals functional flexibility in the selenocysteine-specific tRNA from mouse. PloS One, 6, e20032.
    • (2011) PloS One , vol.6 , pp. e20032
    • Ganichkin, O.M.1    Anedchenko, E.A.2    Wahl, M.C.3
  • 28
    • 84863723708 scopus 로고    scopus 로고
    • Structural dynamics of the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase
    • Palencia, A., Crepin, T., Vu, M.T., Lincecum, T.L. Jr, Martinis, S.A. and Cusack, S. (2012) Structural dynamics of the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase. Nat. Struct. Mol. Biol., 19, 677-684.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 677-684
    • Palencia, A.1    Crepin, T.2    Vu, M.T.3    Lincecum, T.L.4    Martinis, S.A.5    Cusack, S.6
  • 29
    • 71049153753 scopus 로고    scopus 로고
    • Identification of amino acids in the N-terminal domain of atypical methanogenic-type seryl-tRNA synthetase critical for tRNA recognition
    • Jaric, J., Bilokapic, S., Lesjak, S., Crnkovic, A., Ban, N. and Weygand-Durasevic, I. (2009) Identification of amino acids in the N-terminal domain of atypical methanogenic-type seryl-tRNA synthetase critical for tRNA recognition. J. Biol. Chem., 284, 30643-30651.
    • (2009) J. Biol. Chem. , vol.284 , pp. 30643-30651
    • Jaric, J.1    Bilokapic, S.2    Lesjak, S.3    Crnkovic, A.4    Ban, N.5    Weygand-Durasevic, I.6
  • 30
    • 22044445670 scopus 로고    scopus 로고
    • Thiol-disulfide balance: From the concept of oxidative stress to that of redox regulation
    • Ghezzi, P., Bonetto, V. and Fratelli, M. (2005) Thiol-disulfide balance: from the concept of oxidative stress to that of redox regulation. Antioxid. Redox Signal., 7, 964-972.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 964-972
    • Ghezzi, P.1    Bonetto, V.2    Fratelli, M.3
  • 32
    • 77956905616 scopus 로고    scopus 로고
    • The conserved CXXC motif of hepatic stimulator substance is essential for its role in mitochondrial protection in H2O2-induced cell apoptosis
    • Li, W., Zhang, J. and An, W. (2010) The conserved CXXC motif of hepatic stimulator substance is essential for its role in mitochondrial protection in H2O2-induced cell apoptosis. FEBS Lett., 584, 3929-3935.
    • (2010) FEBS Lett. , vol.584 , pp. 3929-3935
    • Li, W.1    Zhang, J.2    An, W.3
  • 33
    • 84870877138 scopus 로고    scopus 로고
    • Loss of the oxidative stress sensor NPGPx compromises GRP78 chaperone activity and induces systemic disease
    • Wei, P.C., Hsieh, Y.H., Su, M.I., Jiang, X., Hsu, P.H., Lo, W.T., Weng, J.Y., Jeng, Y.M., Wang, J.M., Chen, P.L. et al. (2012) Loss of the oxidative stress sensor NPGPx compromises GRP78 chaperone activity and induces systemic disease. Mol. Cell, 48, 747-759.
    • (2012) Mol. Cell , vol.48 , pp. 747-759
    • Wei, P.C.1    Hsieh, Y.H.2    Su, M.I.3    Jiang, X.4    Hsu, P.H.5    Lo, W.T.6    Weng, J.Y.7    Jeng, Y.M.8    Wang, J.M.9    Chen, P.L.10
  • 34
    • 79551685246 scopus 로고    scopus 로고
    • Generation of the oxidized form protects human brain type creatine kinase against cystine-induced inactivation
    • Li, X.H., Chen, Z., Gao, Y.S., Yan, Y.B., Zhang, F., Meng, F.G. and Zhou, H.M. (2011) Generation of the oxidized form protects human brain type creatine kinase against cystine-induced inactivation. Int. J. Biol. Macromol., 48, 239-242.
    • (2011) Int. J. Biol. Macromol. , vol.48 , pp. 239-242
    • Li, X.H.1    Chen, Z.2    Gao, Y.S.3    Yan, Y.B.4    Zhang, F.5    Meng, F.G.6    Zhou, H.M.7
  • 35
    • 0025651675 scopus 로고
    • Conversion of aminoacylation specificity from tRNATyr to tRNASer in vitro
    • Himeno, H., Hasegawa, T., Ueda, T., Watanabe, K. and Shimizu, M. (1990) Conversion of aminoacylation specificity from tRNATyr to tRNASer in vitro. Nucleic Acids Res., 18, 6815-6819.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6815-6819
    • Himeno, H.1    Hasegawa, T.2    Ueda, T.3    Watanabe, K.4    Shimizu, M.5
  • 36
    • 0027442959 scopus 로고
    • Contributions of discrete tRNASer domains to aminoacylation by E.coli seryl-tRNA synthetase: A kinetic analysis using model RNA substrates
    • Sampson, J.R. and Saks, M.E. (1993) Contributions of discrete tRNASer domains to aminoacylation by E.coli seryl-tRNA synthetase: a kinetic analysis using model RNA substrates. Nucleic Acids Res., 21, 4467-4475.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4467-4475
    • Sampson, J.R.1    Saks, M.E.2
  • 37
    • 0030592461 scopus 로고    scopus 로고
    • Selenocysteine synthesis in mammalia: An identity switch from tRNASer to tRNASec
    • Amberg, R., Mizutani, T., Wu, X.Q. and Gross, H.J. (1996) Selenocysteine synthesis in mammalia: an identity switch from tRNASer to tRNASec. J. Mol. Biol., 263, 8-19.
    • (1996) J. Mol. Biol. , vol.263 , pp. 8-19
    • Amberg, R.1    Mizutani, T.2    Wu, X.Q.3    Gross, H.J.4
  • 39
    • 0028148904 scopus 로고
    • Seryl-tRNA synthetase from Escherichia coli: Implication of its N-terminal domain in aminoacylation activity and specificity
    • Borel, F., Vincent, C., Leberman, R. and Hartlein, M. (1994) Seryl-tRNA synthetase from Escherichia coli: implication of its N-terminal domain in aminoacylation activity and specificity. Nucleic Acids Res., 22, 2963-2969.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 2963-2969
    • Borel, F.1    Vincent, C.2    Leberman, R.3    Hartlein, M.4
  • 40
    • 0027174921 scopus 로고
    • Crystallization of the seryl-tRNA synthetase: TRNASer complex of Escherichia coli
    • Price, S., Cusack, S., Borel, F., Berthet-Colominas, C. and Leberman, R. (1993) Crystallization of the seryl-tRNA synthetase: tRNASer complex of Escherichia coli. FEBS Lett., 324, 167-170.
    • (1993) FEBS Lett. , vol.324 , pp. 167-170
    • Price, S.1    Cusack, S.2    Borel, F.3    Berthet-Colominas, C.4    Leberman, R.5
  • 41
    • 0026644744 scopus 로고
    • A new crystal form of the complex between seryl-tRNA synthetase and tRNASer from Thermus thermophilus that diffracts to 2.8 Å resolution
    • Yaremchuk, A.D., Tukalo, M.A., Krikliviy, I., Malchenko, N., Biou, V., Berthet-Colominas, C. and Cusack, S. (1992) A new crystal form of the complex between seryl-tRNA synthetase and tRNASer from Thermus thermophilus that diffracts to 2.8 Å resolution. FEBS Lett., 310, 157-161.
    • (1992) FEBS Lett. , vol.310 , pp. 157-161
    • Yaremchuk, A.D.1    Tukalo, M.A.2    Krikliviy, I.3    Malchenko, N.4    Biou, V.5    Berthet-Colominas, C.6    Cusack, S.7
  • 42
    • 0031463939 scopus 로고    scopus 로고
    • Detection of noncovalent tRNA aminoacyl-tRNA synthetase complexes by matrix-assisted laser desorption/Ionization mass spectrometry
    • Gruic-Sovulj, I., Lüdemann, H.-C., Hillenkamp, F., Weygand-Durasevic, I., Kucan, Z. and Peter-Katalinic, J. (1997) Detection of noncovalent tRNA aminoacyl-tRNA synthetase complexes by matrix-assisted laser desorption/Ionization mass spectrometry. J. Biol. Chem., 272, 32084-32091.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32084-32091
    • Gruic-Sovulj, I.1    Lüdemann, H.-C.2    Hillenkamp, F.3    Weygand-Durasevic, I.4    Kucan, Z.5    Peter-Katalinic, J.6
  • 43
    • 0016734742 scopus 로고
    • Equivalent and non-equivalent binding sites for tRNA on aminoacyl-tRNA synthetases
    • Krauss, G., Pingoud, A., Boehme, D., Riesner, D., Peters, F. and Maass, G. (1975) Equivalent and non-equivalent binding sites for tRNA on aminoacyl-tRNA synthetases. Eur. J. Biochem., 55, 517-529.
    • (1975) Eur. J. Biochem. , vol.55 , pp. 517-529
    • Krauss, G.1    Pingoud, A.2    Boehme, D.3    Riesner, D.4    Peters, F.5    Maass, G.6
  • 44
    • 0017174834 scopus 로고
    • On the interaction of seryl-tRNA synthetase with tRNASer
    • Rigler, R., Pachmann, U., Hirsch, R. and Zachau, H.G. (1976) On the interaction of seryl-tRNA synthetase with tRNASer. Eur. J. Biochem., 65, 307-315.
    • (1976) Eur. J. Biochem. , vol.65 , pp. 307-315
    • Rigler, R.1    Pachmann, U.2    Hirsch, R.3    Zachau, H.G.4
  • 45
    • 84908093596 scopus 로고    scopus 로고
    • Structural asymmetry of the terminal catalytic complex in selenocysteine synthesis
    • French, R.L., Gupta, N., Copeland, P.R. and Simonović, M. (2014) Structural asymmetry of the terminal catalytic complex in selenocysteine synthesis. J. Biol. Chem., 289, 28783-28794.
    • (2014) J. Biol. Chem. , vol.289 , pp. 28783-28794
    • French, R.L.1    Gupta, N.2    Copeland, P.R.3    Simonović, M.4


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