메뉴 건너뛰기




Volumn 287, Issue 5, 2012, Pages 3175-3184

Substrate specificity of bacterial prolyl-tRNA synthetase editing domain is controlled by a tunable hydrophobic pocket

Author keywords

[No Author keywords available]

Indexed keywords

CONSERVED RESIDUES; COVALENT ATTACHMENT; EXPERIMENTAL APPROACHES; GENETIC INFORMATION; HIGH FIDELITY; HYDROPHOBIC POCKETS; IN-VIVO; MOLECULAR BASIS; SIDE-CHAINS; SITE-SPECIFIC; SUBSTRATE SPECIFICITY; SYNTHETASES;

EID: 84863011899     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.313619     Document Type: Article
Times cited : (21)

References (37)
  • 3
    • 3943088436 scopus 로고    scopus 로고
    • Incorporation of nonnatural amino acids into proteins
    • DOI 10.1146/annurev.biochem.73.012803.092429
    • Hendrickson, T. L., de Crécy-Lagard, V., and Schimmel, P. (2004) Incorporation of nonnatural amino acids into proteins. Annu. Rev. Biochem. 73, 147-176 (Pubitemid 39050366)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 147-176
    • Hendrickson, T.L.1    De Crecy-Lagard, V.2    Schimmel, P.3
  • 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
    • 42349103482 scopus 로고    scopus 로고
    • Fidelity mechanisms of the aminoacyl-tRNA synthetases
    • Köhrer, C., and RajBhandary, U. L., eds Springer-Verlag, Berlin
    • Mascarenhas, A. P., An, S., Rosen, A. E., Martinis, S. A., and Musier-Forsyth, K. (2008) Fidelity mechanisms of the aminoacyl-tRNA synthetases. Protein Engineering (Köhrer, C., and RajBhandary, U. L., eds) pp. 155-203, Springer-Verlag, Berlin
    • (2008) Protein Engineering , pp. 155-203
    • Mascarenhas, A.P.1    An, S.2    Rosen, A.E.3    Martinis, S.A.4    Musier-Forsyth, K.5
  • 7
    • 58149354143 scopus 로고    scopus 로고
    • Quality control by the ribosome following peptide bond formation
    • Zaher, H. S., and Green, R. (2009) Quality control by the ribosome following peptide bond formation. Nature 457, 161-166
    • (2009) Nature , vol.457 , pp. 161-166
    • Zaher, H.S.1    Green, R.2
  • 9
    • 10644277147 scopus 로고    scopus 로고
    • Post-transfer editing in vitro and in vivo by the β subunit of phenylalanyl-tRNA synthetase
    • DOI 10.1038/sj.emboj.7600474
    • Roy, H., Ling, J., Irnov, M., and Ibba, M. (2004) Post-transfer editing in vitro and in vivo by the β-subunit of phenylalanyl-tRNA synthetase. EMBO J. 23, 4639-4648 (Pubitemid 39657863)
    • (2004) EMBO Journal , vol.23 , Issue.23 , pp. 4639-4648
    • Roy, H.1    Ling, J.2    Irnov, M.3    Ibba, M.4
  • 11
    • 33749669848 scopus 로고    scopus 로고
    • Global Effects of Mistranslation from an Editing Defect in Mammalian Cells
    • DOI 10.1016/j.chembiol.2006.08.011, PII S107455210600305X
    • Nangle, L. A., Motta, C. M., and Schimmel, P. (2006) Global effects of mistranslation from an editing defect in mammalian cells. Chem. Biol. 13, 1091-1100 (Pubitemid 44557071)
    • (2006) Chemistry and Biology , vol.13 , Issue.10 , pp. 1091-1100
    • Nangle, L.A.1    Motta, C.M.2    Schimmel, P.3
  • 12
    • 5644229591 scopus 로고    scopus 로고
    • Pro by Haemophilus influenzae YbaK protein
    • DOI 10.1074/jbc.C400304200
    • An, S., and Musier-Forsyth, K. (2004) Trans-editing of Cys-tRNAPro by Haemophilus influenzae YbaK protein. J. Biol. Chem. 279, 42359-42362 (Pubitemid 39372116)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.41 , pp. 42359-42362
    • An, S.1    Musier-Forsyth, K.2
  • 13
    • 27144460984 scopus 로고    scopus 로고
    • Pro editing by Haemophilus influenzae YbaK via a novel synthetase•YbaK•tRNA ternary complex
    • DOI 10.1074/jbc.M507550200
    • An, S., and Musier-Forsyth, K. (2005) Cys-tRNA(Pro) editing by Haemophilus influenzae YbaK via a novel synthetase•YbaK•tRNA ternary complex. J. Biol. Chem. 280, 34465-34472 (Pubitemid 41504575)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.41 , pp. 34465-34472
    • An, S.1    Musier-Forsyth, K.2
  • 14
    • 21844462827 scopus 로고    scopus 로고
    • Cys deacylase
    • DOI 10.1074/jbc.M502174200
    • Ruan, B., and Söll, D. (2005) The bacterial YbaK protein is a Cys-tRNAPro and Cys-tRNA Cys deacylase. J. Biol. Chem. 280, 25887-25891 (Pubitemid 40962300)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.27 , pp. 25887-25891
    • Ruan, B.1    Soll, D.2
  • 16
    • 80052402915 scopus 로고    scopus 로고
    • Substrate-mediated fidelity mechanism ensures accurate decoding of proline codons
    • So, B. R., An, S., Kumar, S., Das, M., Turner, D. A., Hadad, C. M., and Musier-Forsyth, K. (2011) Substrate-mediated fidelity mechanism ensures accurate decoding of proline codons. J. Biol. Chem. 286, 31810-31820
    • (2011) J. Biol. Chem. , vol.286 , pp. 31810-31820
    • So, B.R.1    An, S.2    Kumar, S.3    Das, M.4    Turner, D.A.5    Hadad, C.M.6    Musier-Forsyth, K.7
  • 21
    • 33947716119 scopus 로고    scopus 로고
    • Software news and update a semiempirical free energy force field with charge-based desolvation
    • DOI 10.1002/jcc.20634
    • Huey, R., Morris, G. M., Olson, A. J., and Goodsell, D. S. (2007) A semiempirical free energy force field with charge-based desolvation. J. Comput. Chem. 28, 1145-1152 (Pubitemid 46506716)
    • (2007) Journal of Computational Chemistry , vol.28 , Issue.6 , pp. 1145-1152
    • Huey, R.1    Morris, G.M.2    Olson, A.J.3    Goodsell, D.S.4
  • 22
    • 0037018949 scopus 로고    scopus 로고
    • Functional role of the prokaryotic proline-tRNA synthetase insertion domain in amino acid editing
    • DOI 10.1021/bi012178j
    • Wong, F. C., Beuning, P. J., Nagan, M., Shiba, K., and Musier-Forsyth, K. (2002) Functional role of the prokaryotic proline-tRNA synthetase insertion domain in amino acid editing. Biochemistry 41, 7108-7115 (Pubitemid 34575684)
    • (2002) Biochemistry , vol.41 , Issue.22 , pp. 7108-7115
    • Wong, F.-C.1    Beuning, P.J.2    Nagan, M.3    Shiba, K.4    Musier-Forsyth, K.5
  • 23
    • 0037415734 scopus 로고    scopus 로고
    • Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability
    • DOI 10.1093/emboj/cdg065
    • Beebe, K., Ribas De Pouplana, L., and Schimmel, P. (2003) Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability. EMBO J. 22, 668-675 (Pubitemid 36193611)
    • (2003) EMBO Journal , vol.22 , Issue.3 , pp. 668-675
    • Beebe, K.1    De Pouplana, L.R.2    Schimmel, P.3
  • 24
    • 0037036357 scopus 로고    scopus 로고
    • Plasticity of recognition of the 3′-end of mischarged tRNA by class I aminoacyl-tRNA synthetases
    • DOI 10.1074/jbc.M202023200
    • Nordin, B. E., and Schimmel, P. (2002) Plasticity of recognition of the 3′-end of mischarged tRNA by class I aminoacyl-tRNA synthetases. J. Biol. Chem. 277, 20510-20517 (Pubitemid 34967350)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.23 , pp. 20510-20517
    • Nordin, B.E.1    Schimmel, P.2
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 0016437581 scopus 로고
    • Active site titration and aminoacyl adenylate binding stoichiometry of aminoacyl-tRNA synthetases
    • Fersht, A. R., Ashford, J. S., Bruton, C. J., Jakes, R., Koch, G. L., and Hartley, B. S. (1975) Active site titration and aminoacyl adenylate binding stoichiometry of aminoacyl-tRNA synthetases. Biochemistry 14, 1-4
    • (1975) Biochemistry , vol.14 , pp. 1-4
    • Fersht, A.R.1    Ashford, J.S.2    Bruton, C.J.3    Jakes, R.4    Koch, G.L.5    Hartley, B.S.6
  • 29
    • 33749503497 scopus 로고    scopus 로고
    • Structures of Two Bacterial Prolyl-tRNA Synthetases with and without a cis-Editing Domain
    • DOI 10.1016/j.str.2006.08.007, PII S0969212606003558
    • Crepin, T., Yaremchuk, A., Tukalo, M., and Cusack, S. (2006) Structures of two bacterial prolyl-tRNA synthetases with and without a cis-editing domain. Structure 14, 1511-1525 (Pubitemid 44515073)
    • (2006) Structure , vol.14 , Issue.10 , pp. 1511-1525
    • Crepin, T.1    Yaremchuk, A.2    Tukalo, M.3    Cusack, S.4
  • 30
    • 0034237733 scopus 로고    scopus 로고
    • Crystal structure of YbaK protein from Haemophilus influenzae (HI1434) at 1.8 Å resolution: Functional implications
    • DOI 10.1002/(SICI)1097-0134(20000701)40:1<86::AID-PROT100>3.0.CO;2- Y
    • Zhang, H., Huang, K., Li, Z., Banerjei, L., Fisher, K. E., Grishin, N. V., Eisenstein, E., and Herzberg, O. (2000) Crystal structure of YbaK protein from Haemophilus influenzae (HI1434) at 1.8 Å resolution: functional implications. Proteins 40, 86-97 (Pubitemid 30368584)
    • (2000) Proteins: Structure, Function and Genetics , vol.40 , Issue.1 , pp. 86-97
    • Zhang, H.1    Huang, K.2    Li, Z.3    Banerjei, L.4    Fisher, K.E.5    Grishin, N.V.6    Eisenstein, E.7    Herzberg, O.8
  • 31
    • 0035747672 scopus 로고    scopus 로고
    • Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM
    • DOI 10.1002/prot.1168
    • Bates, P. A., Kelley, L. A., MacCallum, R. M., and Sternberg, M. J. (2001) Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM. Proteins Suppl. 5, 39-46 (Pubitemid 34113166)
    • (2001) Proteins: Structure, Function and Genetics , vol.45 , Issue.SUPPL. 5 , pp. 39-46
    • Bates, P.A.1    Kelley, L.A.2    MacCallum, R.M.3    Sternberg, M.J.E.4
  • 32
    • 0032562707 scopus 로고    scopus 로고
    • Sieves in sequence
    • Fersht, A. R. (1998) Sieves in sequence. Science 280, 541
    • (1998) Science , vol.280 , pp. 541
    • Fersht, A.R.1
  • 34
    • 0034703763 scopus 로고    scopus 로고
    • Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNA(Val) and valyl-tRNA synthetase
    • Fukai, S., Nureki, O., Sekine, S., Shimada, A., Tao, J., Vassylyev, D. G., and Yokoyama, S. (2000) Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNA(Val) and valyl-tRNA synthetase. Cell 103, 793-803
    • (2000) Cell , vol.103 , pp. 793-803
    • Fukai, S.1    Nureki, O.2    Sekine, S.3    Shimada, A.4    Tao, J.5    Vassylyev, D.G.6    Yokoyama, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.