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Volumn 39, Issue 20, 2011, Pages 8857-8868

Role of tRNA amino acid-accepting end in aminoacylation and its quality control

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE;

EID: 80455178748     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkr595     Document Type: Article
Times cited : (30)

References (43)
  • 1
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba, M. and Soll, D. (2000) Aminoacyl-tRNA synthesis. Annu. Rev. Biochem., 69, 617-650.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 617-650
    • Ibba, M.1    Soll, D.2
  • 2
    • 0023061339 scopus 로고
    • Aminoacyl tRNA synthetases: General scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs
    • Schimmel, P. (1987) Aminoacyl tRNA synthetases: general scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs. Annu. Rev. Biochem., 56, 125-158.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 125-158
    • Schimmel, P.1
  • 4
    • 70349545940 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis and translational quality control
    • Ling, J., Reynolds, N. and Ibba, M. (2009) Aminoacyl-tRNA synthesis and translational quality control. Annu. Rev. Microbiol., 63, 61-78.
    • (2009) Annu. Rev. Microbiol. , vol.63 , pp. 61-78
    • Ling, J.1    Reynolds, N.2    Ibba, M.3
  • 5
    • 61349117470 scopus 로고    scopus 로고
    • The CP2 domain of leucyl-tRNA synthetase is crucial for amino acid activation and post-transfer editing
    • Zhou, X., Zhu, B. and Wang, E. (2008) The CP2 domain of leucyl-tRNA synthetase is crucial for amino acid activation and post-transfer editing. J. Biol. Chem., 283, 36608-36616.
    • (2008) J. Biol. Chem. , vol.283 , pp. 36608-36616
    • Zhou, X.1    Zhu, B.2    Wang, E.3
  • 6
    • 27144477810 scopus 로고    scopus 로고
    • The crystal structure of leucyl-tRNA synthetase complexed with tRNALeu in the post-transfer-editing conformation
    • Tukalo, M., Yaremchuk, A., Fukunaga, R., Yokoyama, S. and Cusack, S. (2005) The crystal structure of leucyl-tRNA synthetase complexed with tRNALeu in the post-transfer-editing conformation. Nat. Struct. Mol. Biol., 12, 923-930.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 923-930
    • Tukalo, M.1    Yaremchuk, A.2    Fukunaga, R.3    Yokoyama, S.4    Cusack, S.5
  • 7
    • 0034612210 scopus 로고    scopus 로고
    • CP1 domain in Escherichia coli leucyl-tRNA synthetase is crucial for its editing function
    • Chen, J., Guo, N., Li, T., Wang, E. and Wang, Y. (2000) CP1 domain in Escherichia coli leucyl-tRNA synthetase is crucial for its editing function. Biochemistry, 39, 6726-6731.
    • (2000) Biochemistry , vol.39 , pp. 6726-6731
    • Chen, J.1    Guo, N.2    Li, T.3    Wang, E.4    Wang, Y.5
  • 8
    • 77449099886 scopus 로고    scopus 로고
    • TRNA-dependent pre-transfer editing by prokaryotic leucyl-tRNA synthetase
    • Tan, M., Zhu, B., Zhou, X., He, R., Chen, X., Eriani, G. and Wang, E. (2010) tRNA-dependent pre-transfer editing by prokaryotic leucyl-tRNA synthetase. J. Biol. Chem., 285, 3235-3244.
    • (2010) J. Biol. Chem. , vol.285 , pp. 3235-3244
    • Tan, M.1    Zhu, B.2    Zhou, X.3    He, R.4    Chen, X.5    Eriani, G.6    Wang, E.7
  • 9
    • 78651286311 scopus 로고    scopus 로고
    • Modular pathways for editing non-cognate amino acids by human cytoplasmic leucyl-tRNA synthetase
    • Chen, X., Ma, J., Tan, M., Yao, P., Hu, Q., Eriani, G. and Wang, E. (2011) Modular pathways for editing non-cognate amino acids by human cytoplasmic leucyl-tRNA synthetase. Nucleic Acids Res., 39, 235-247.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 235-247
    • Chen, X.1    Ma, J.2    Tan, M.3    Yao, P.4    Hu, Q.5    Eriani, G.6    Wang, E.7
  • 10
    • 77954908008 scopus 로고    scopus 로고
    • Partitioning of tRNA-dependent editing between pre- and post-transfer pathways in Class i aminoacyl-tRNA synthetases
    • Dulic, M., Cvetesic, N., Perona, J.J. and Gruic-Sovulj, I. (2010) Partitioning of tRNA-dependent editing between pre- and post-transfer pathways in Class I aminoacyl-tRNA synthetases. J. Biol. Chem., 285, 23799-23809.
    • (2010) J. Biol. Chem. , vol.285 , pp. 23799-23809
    • Dulic, M.1    Cvetesic, N.2    Perona, J.J.3    Gruic-Sovulj, I.4
  • 11
    • 27144520077 scopus 로고    scopus 로고
    • Aminoacylation complex structures of leucyl-tRNA synthetase and tRNALeu reveal two modes of discriminator-base recognition
    • Fukunaga, R. and Yokoyama, S. (2005) Aminoacylation complex structures of leucyl-tRNA synthetase and tRNALeu reveal two modes of discriminator-base recognition. Nat. Struct. Mol. Biol., 12, 915-922.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 915-922
    • Fukunaga, R.1    Yokoyama, S.2
  • 12
    • 3643114575 scopus 로고    scopus 로고
    • Universal rules and idiosyncratic features in tRNA identity
    • Giege, R., Sissler, M. and Florentz, C. (1998) Universal rules and idiosyncratic features in tRNA identity. Nucleic Acids Res., 26, 5017-5035.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5017-5035
    • Giege, R.1    Sissler, M.2    Florentz, C.3
  • 13
    • 78149385338 scopus 로고    scopus 로고
    • How the CCA-adding enzyme selects adenine over cytosine at position 76 of tRNA
    • Pan, B., Xiong, Y. and Steitz, T.A. (2010) How the CCA-adding enzyme selects adenine over cytosine at position 76 of tRNA. Science, 330, 937-940.
    • (2010) Science , vol.330 , pp. 937-940
    • Pan, B.1    Xiong, Y.2    Steitz, T.A.3
  • 14
    • 0033928672 scopus 로고    scopus 로고
    • Unusual synthesis by the Escherichia coli CCA-adding enzyme
    • Hou, Y.M. (2000) Unusual synthesis by the Escherichia coli CCA-adding enzyme. RNA, 6, 1031-1043.
    • (2000) RNA , vol.6 , pp. 1031-1043
    • Hou, Y.M.1
  • 17
    • 0141558842 scopus 로고    scopus 로고
    • Trial for peptide bond formation using model molecules based on the interactions between the CCA sequence of tRNA and 23S rRNA
    • Tamura, K. and Schimmel, P. (2000) Trial for peptide bond formation using model molecules based on the interactions between the CCA sequence of tRNA and 23S rRNA. Nucleic Acids Symp. Ser., 44, 251-252.
    • (2000) Nucleic Acids Symp. Ser. , vol.44 , pp. 251-252
    • Tamura, K.1    Schimmel, P.2
  • 18
    • 0015145949 scopus 로고
    • Isolation and partial characterization of temperature-sensitive Escherichia coli mutants with altered leucyl- and seryl-transfer ribonucleic acid synthetases
    • Low, B., Gates, F., Goldstein, T. and Soll, D. (1971) Isolation and partial characterization of temperature-sensitive Escherichia coli mutants with altered leucyl- and seryl-transfer ribonucleic acid synthetases. J. Bacteriol., 108, 742-750.
    • (1971) J. Bacteriol. , vol.108 , pp. 742-750
    • Low, B.1    Gates, F.2    Goldstein, T.3    Soll, D.4
  • 19
    • 0033166764 scopus 로고    scopus 로고
    • A modified procedure for fast purification of T7 RNA polymerase
    • Li, Y., Wang, E. and Wang, Y. (1999) A modified procedure for fast purification of T7 RNA polymerase. Protein Expr. Purif., 16, 355-358.
    • (1999) Protein Expr. Purif. , vol.16 , pp. 355-358
    • Li, Y.1    Wang, E.2    Wang, Y.3
  • 20
    • 1942471991 scopus 로고    scopus 로고
    • Groups on the side chain of T252 in Escherichia coli leucyl-tRNA synthetase are important for discrimination of amino acids and cell viability
    • Xu, M., Li, J., Du, X. and Wang, E. (2004) Groups on the side chain of T252 in Escherichia coli leucyl-tRNA synthetase are important for discrimination of amino acids and cell viability. Biochem. Biophys. Res. Commun., 318, 11-16.
    • (2004) Biochem. Biophys. Res. Commun. , vol.318 , pp. 11-16
    • Xu, M.1    Li, J.2    Du, X.3    Wang, E.4
  • 21
    • 43349096966 scopus 로고    scopus 로고
    • Recognition of tRNALeu by Aquifex aeolicus leucyl-tRNA synthetase during the aminoacylation and editing steps
    • Yao, P., Zhu, B., Jaeger, S., Eriani, G. and Wang, E. (2008) Recognition of tRNALeu by Aquifex aeolicus leucyl-tRNA synthetase during the aminoacylation and editing steps. Nucleic Acids Res., 36, 2728-2738.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2728-2738
    • Yao, P.1    Zhu, B.2    Jaeger, S.3    Eriani, G.4    Wang, E.5
  • 22
    • 0020476264 scopus 로고
    • Covalent attachment of aspartic acid to yeast aspartyl-tRNA synthetase induced by the enzyme
    • Lorber, B., Kern, D., Gieg, R. and Ebel, J.P. (1982) Covalent attachment of aspartic acid to yeast aspartyl-tRNA synthetase induced by the enzyme. FEBS Lett., 146, 59-64.
    • (1982) FEBS Lett. , vol.146 , pp. 59-64
    • Lorber, B.1    Kern, D.2    Gieg, R.3    Ebel, J.P.4
  • 23
    • 0022355306 scopus 로고
    • Covalent modification of phenylalanyl-tRNA synthetase with phenylalanine during the amino acid activation reaction catalyzed by the enzyme
    • Rapaport, E., Yogeeswaran, G., Zamecnik, P.C. and Remy, P. (1985) Covalent modification of phenylalanyl-tRNA synthetase with phenylalanine during the amino acid activation reaction catalyzed by the enzyme. J. Biol. Chem., 260, 9509-9512.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9509-9512
    • Rapaport, E.1    Yogeeswaran, G.2    Zamecnik, P.C.3    Remy, P.4
  • 24
    • 0018145586 scopus 로고
    • Tryptophanyl-tRNA synthetase: Evidence for an anhydrous bond involved in the tryptophanyl enzyme formation
    • Kovaleva, G.K., Moroz, S.G., Favorova, O.O. and Kisselev, L.L. (1978) Tryptophanyl-tRNA synthetase: evidence for an anhydrous bond involved in the tryptophanyl enzyme formation. FEBS Lett., 95, 81-84.
    • (1978) FEBS Lett. , vol.95 , pp. 81-84
    • Kovaleva, G.K.1    Moroz, S.G.2    Favorova, O.O.3    Kisselev, L.L.4
  • 25
    • 21244439199 scopus 로고    scopus 로고
    • TRNA-dependent aminoacyl-adenylate hydrolysis by a nonediting Class i aminoacyl-tRNA synthetase
    • Gruic-Sovulj, I., Uter, N., Bullock, T. and Perona, J.J. (2005) tRNA-dependent aminoacyl-adenylate hydrolysis by a nonediting Class I aminoacyl-tRNA synthetase. J. Biol. Chem., 280, 23978-23986.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23978-23986
    • Gruic-Sovulj, I.1    Uter, N.2    Bullock, T.3    Perona, J.J.4
  • 26
    • 63649123391 scopus 로고    scopus 로고
    • TRNA-independent pretransfer editing by Class i leucyl-tRNA synthetase
    • Zhu, B., Yao, P., Tan, M., Eriani, G. and Wang, E. (2009) tRNA-independent pretransfer editing by Class I leucyl-tRNA synthetase. J. Biol. Chem., 284, 3418-3424.
    • (2009) J. Biol. Chem. , vol.284 , pp. 3418-3424
    • Zhu, B.1    Yao, P.2    Tan, M.3    Eriani, G.4    Wang, E.5
  • 27
    • 1542631893 scopus 로고    scopus 로고
    • Overproduction and purification of Escherichia coli tRNALeu
    • Li, Y., Wang, E. and Wang, Y. (1998) Overproduction and purification of Escherichia coli tRNALeu. Sci. China, C, Life Sci., 41, 225-231.
    • (1998) Sci. China C, Life Sci. , vol.41 , pp. 225-231
    • Li, Y.1    Wang, E.2    Wang, Y.3
  • 29
    • 0033551417 scopus 로고    scopus 로고
    • Discrimination of tRNALeu isoacceptors by the insertion mutant of Escherichia coli leucyl-tRNA synthetase
    • Li, T., Li, Y., Guo, N., Wang, E. and Wang, Y. (1999) Discrimination of tRNALeu isoacceptors by the insertion mutant of Escherichia coli leucyl-tRNA synthetase. Biochemistry, 38, 9084-9088.
    • (1999) Biochemistry , vol.38 , pp. 9084-9088
    • Li, T.1    Li, Y.2    Guo, N.3    Wang, E.4    Wang, Y.5
  • 30
    • 0034832844 scopus 로고    scopus 로고
    • This is the end: Processing, editing and repair at the tRNA 30-terminus
    • Schurer, H., Schiffer, S., Marchfelder, A. and Morl, M. (2001) This is the end: processing, editing and repair at the tRNA 30-terminus. Biol. Chem., 382, 1147-1156.
    • (2001) Biol. Chem. , vol.382 , pp. 1147-1156
    • Schurer, H.1    Schiffer, S.2    Marchfelder, A.3    Morl, M.4
  • 31
    • 0028100461 scopus 로고
    • Role of the CCA terminal sequence of tRNA(Val) in aminoacylation with valyl-tRNA synthetase
    • Tamura, K., Nameki, N., Hasegawa, T., Shimizu, M. and Himeno, H. (1994) Role of the CCA terminal sequence of tRNA(Val) in aminoacylation with valyl-tRNA synthetase. J. Biol. Chem., 269, 22173-22177.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22173-22177
    • Tamura, K.1    Nameki, N.2    Hasegawa, T.3    Shimizu, M.4    Himeno, H.5
  • 32
    • 0028033045 scopus 로고
    • Functional transfer RNAs with modifications in the 30-CCA end: Differential effects on aminoacylation and polypeptide synthesis
    • Liu, M. and Horowitz, J. (1994) Functional transfer RNAs with modifications in the 30-CCA end: differential effects on aminoacylation and polypeptide synthesis. Proc. Natl Acad. Sci. USA, 91, 10389-10393.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10389-10393
    • Liu, M.1    Horowitz, J.2
  • 33
    • 0033609807 scopus 로고    scopus 로고
    • Yeast aspartyl-tRNA synthetase residues interacting with tRNA(Asp) identity bases connectively contribute to tRNA(Asp) binding in the ground and transition-state complex and discriminate against non-cognate tRNAs
    • Eriani, G. and Gangloff, J. (1999) Yeast aspartyl-tRNA synthetase residues interacting with tRNA(Asp) identity bases connectively contribute to tRNA(Asp) binding in the ground and transition-state complex and discriminate against non-cognate tRNAs. J. Mol. Biol., 291, 761-773.
    • (1999) J. Mol. Biol. , vol.291 , pp. 761-773
    • Eriani, G.1    Gangloff, J.2
  • 34
    • 0036606137 scopus 로고    scopus 로고
    • Transfer RNA determinants for translational editing by Escherichia coli valyl-tRNA synthetase
    • Tardif, K.D. and Horowitz, J. (2002) Transfer RNA determinants for translational editing by Escherichia coli valyl-tRNA synthetase. Nucleic Acids Res., 30, 2538-2545.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2538-2545
    • Tardif, K.D.1    Horowitz, J.2
  • 35
    • 43749101170 scopus 로고    scopus 로고
    • Transfer RNA modulates the editing mechanism used by class II prolyl-tRNA synthetase
    • Splan, K.E., Ignatov, M.E. and Musier-Forsyth, K. (2008) Transfer RNA modulates the editing mechanism used by class II prolyl-tRNA synthetase. J. Biol. Chem., 283, 7128-7134.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7128-7134
    • Splan, K.E.1    Ignatov, M.E.2    Musier-Forsyth, K.3
  • 36
    • 35348920149 scopus 로고    scopus 로고
    • Hydrolysis of non-cognate aminoacyl-adenylates by a class II aminoacyl-tRNA synthetase lacking an editing domain
    • Gruic-Sovulj, I., Rokov-Plavec, J. and Weygand-Durasevic, I. (2007) Hydrolysis of non-cognate aminoacyl-adenylates by a class II aminoacyl-tRNA synthetase lacking an editing domain. FEBS Lett., 581, 5110-5114.
    • (2007) FEBS Lett. , vol.581 , pp. 5110-5114
    • Gruic-Sovulj, I.1    Rokov-Plavec, J.2    Weygand-Durasevic, I.3
  • 37
    • 77954943220 scopus 로고    scopus 로고
    • Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase
    • Minajigi, A. and Francklyn, C.S. (2010) Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase. J. Biol. Chem., 285, 23810-23817.
    • (2010) J. Biol. Chem. , vol.285 , pp. 23810-23817
    • Minajigi, A.1    Francklyn, C.S.2
  • 38
    • 77954908008 scopus 로고    scopus 로고
    • Partitioning of tRNA-dependent editing between pre- and post-transfer pathways in class i aminoacyl-tRNA synthetases
    • Dulic, M., Cvetesic, N., Perona, J.J. and Gruic-Sovulj, I. (2010) Partitioning of tRNA-dependent editing between pre- and post-transfer pathways in class I aminoacyl-tRNA synthetases. J. Biol. Chem., 285, 23799-23809.
    • (2010) J. Biol. Chem. , vol.285 , pp. 23799-23809
    • Dulic, M.1    Cvetesic, N.2    Perona, J.J.3    Gruic-Sovulj, I.4
  • 39
    • 0033928672 scopus 로고    scopus 로고
    • Unusual synthesis by the Escherichia coli CCA-adding enzyme
    • Hou, Y.M. (2000) Unusual synthesis by the Escherichia coli CCA-adding enzyme. RNA, 6, 1031-1043.
    • (2000) RNA , vol.6 , pp. 1031-1043
    • Hou, Y.M.1
  • 40
    • 33846062140 scopus 로고    scopus 로고
    • Reengineering CCA-adding enzymes to function as (U, G)- or dCdCdA-adding enzymes or poly(C, A) and poly(U, G) polymerases
    • Cho, H.D., Verlinde, C.L. and Weiner, A.M. (2007) Reengineering CCA-adding enzymes to function as (U, G)- or dCdCdA-adding enzymes or poly(C, A) and poly(U, G) polymerases. Proc. Natl Acad. Sci. USA, 104, 54-59.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 54-59
    • Cho, H.D.1    Verlinde, C.L.2    Weiner, A.M.3
  • 41
    • 0035834385 scopus 로고    scopus 로고
    • Collaboration between CCand A-adding enzymes to build and repair the 30-terminal CCA of tRNA in Aquifex aeolicus
    • Tomita, K. and Weiner, A.M. (2001) Collaboration between CCand A-adding enzymes to build and repair the 30-terminal CCA of tRNA in Aquifex aeolicus. Science, 294, 1334-1336.
    • (2001) Science , vol.294 , pp. 1334-1336
    • Tomita, K.1    Weiner, A.M.2


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