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Volumn 45, Issue 51, 2006, Pages 15541-15551

Construction of modified ribosomes for incorporation of D-amino acids into proteins

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; ESCHERICHIA COLI; PROTEINS; RNA; SYNTHESIS (CHEMICAL);

EID: 33845940447     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060986a     Document Type: Article
Times cited : (87)

References (48)
  • 1
    • 0023054742 scopus 로고
    • Ribosome-catalyzed formation of an abnormal peptide analog
    • Roesser, J. R., Chorghade, M. S., and Hecht, S. M. (1986) Ribosome-catalyzed formation of an abnormal peptide analog, Biochemistry 25, 6361-6365.
    • (1986) Biochemistry , vol.25 , pp. 6361-6365
    • Roesser, J.R.1    Chorghade, M.S.2    Hecht, S.M.3
  • 2
    • 0025874005 scopus 로고
    • Site-specific incorporation of nonnatural residues during in vitro protein biosynthesis with semi-synthetic aminoacyl-tRNAs
    • Bain, J. D., Diala, E. S., Glabe, C. G., Wacker, D. A., Lyttle, M. H., Dix, T. A., and Chamberlin, A. R. (1991) Site-specific incorporation of nonnatural residues during in vitro protein biosynthesis with semi-synthetic aminoacyl-tRNAs, Biochemistry 30, 5411-5421.
    • (1991) Biochemistry , vol.30 , pp. 5411-5421
    • Bain, J.D.1    Diala, E.S.2    Glabe, C.G.3    Wacker, D.A.4    Lyttle, M.H.5    Dix, T.A.6    Chamberlin, A.R.7
  • 3
    • 0026082859 scopus 로고
    • Site-specific incorporation of nonnatural residues into peptides-Effect of residue structure on suppression and translation efficiencies
    • Bain, J. D., Wacker, D. A., Kuo, E. E., and Chamberlin, A. R. (1991) Site-specific incorporation of nonnatural residues into peptides-Effect of residue structure on suppression and translation efficiencies, Tetrahedron 47, 2389-2400.
    • (1991) Tetrahedron , vol.47 , pp. 2389-2400
    • Bain, J.D.1    Wacker, D.A.2    Kuo, E.E.3    Chamberlin, A.R.4
  • 4
    • 0026567563 scopus 로고
    • Site-specific incorporation of novel backbone structures into proteins
    • Ellman, J. A., Mendel, D., and Schultz, P. G. (1992) Site-specific incorporation of novel backbone structures into proteins, Science 255, 197-200.
    • (1992) Science , vol.255 , pp. 197-200
    • Ellman, J.A.1    Mendel, D.2    Schultz, P.G.3
  • 5
    • 0037668349 scopus 로고    scopus 로고
    • The puromycin route to assess stereo- and regiochemical constraints on peptide bond formation in eukaryotic ribosomes
    • Starck, S. R., Qi, X., Olsen, B. N., and Roberts, R. W. (2003) The puromycin route to assess stereo- and regiochemical constraints on peptide bond formation in eukaryotic ribosomes, J. Am. Chem. Soc. 125, 8090-8091.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 8090-8091
    • Starck, S.R.1    Qi, X.2    Olsen, B.N.3    Roberts, R.W.4
  • 6
    • 5644244186 scopus 로고    scopus 로고
    • Amino acid backbone specificity of the E. coli translation machiner
    • Tan, Z., Forster, A. C., Blacklow, S. C., and Cornish, V. W. (2004) Amino acid backbone specificity of the E. coli translation machiner, J. Am. Chem. Soc. 126, 12752-12753.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 12752-12753
    • Tan, Z.1    Forster, A.C.2    Blacklow, S.C.3    Cornish, V.W.4
  • 7
    • 0031006967 scopus 로고    scopus 로고
    • D-Amino acids in animal peptides
    • Kreil, G. (1997) D-Amino acids in animal peptides, Annu. Rev. Biochem. 66, 337-345.
    • (1997) Annu. Rev. Biochem , vol.66 , pp. 337-345
    • Kreil, G.1
  • 8
    • 0034529167 scopus 로고    scopus 로고
    • L to D amino acid isomerization in a peptide hormone is a late post-translational event occurring in specialized neurosecretory cells
    • Soyez, D., Toullec, J.-Y., Ollivaux, C., and Geraund, G. J. (2000) L to D amino acid isomerization in a peptide hormone is a late post-translational event occurring in specialized neurosecretory cells, J. Biol. Chem. 275, 37870-37875.
    • (2000) J. Biol. Chem , vol.275 , pp. 37870-37875
    • Soyez, D.1    Toullec, J.-Y.2    Ollivaux, C.3    Geraund, G.J.4
  • 9
    • 1542350231 scopus 로고    scopus 로고
    • The linear pentadecapeptide gramicidin is assembled by four multimodular nonribosomal peptide synthetases that comprise 16 modules with 56 catalytic domains
    • Kessler, N., Schuhmann, H., Morneweg, S., Linne, U., and Marahiel, M. A. (2004) The linear pentadecapeptide gramicidin is assembled by four multimodular nonribosomal peptide synthetases that comprise 16 modules with 56 catalytic domains, J. Biol. Chem. 279, 7413-7419,
    • (2004) J. Biol. Chem , vol.279 , pp. 7413-7419
    • Kessler, N.1    Schuhmann, H.2    Morneweg, S.3    Linne, U.4    Marahiel, M.A.5
  • 11
    • 0034693045 scopus 로고    scopus 로고
    • Metabolism of D-aminoacyl-tRNAs in Escherichia coli and Saccharomyces cerevisiae cells
    • Soutourina, J., Plateau, P., and Blanquet, S. (2000) Metabolism of D-aminoacyl-tRNAs in Escherichia coli and Saccharomyces cerevisiae cells, J. Biol. Chem. 275, 32535-32542.
    • (2000) J. Biol. Chem , vol.275 , pp. 32535-32542
    • Soutourina, J.1    Plateau, P.2    Blanquet, S.3
  • 12
    • 0019876111 scopus 로고
    • Donor site of ribosomal peptidyltransferase: Investigation of substrate specificity using 2′(3′)-O-(N-acylaminoacyl)dinucleoside phosphates as models of the 3′-terminus of N-acylaminoacyl transfer ribonucleic acid
    • Quiggle, K., Kumar, G., Ott, T. W., Ryu, E. K., and Chladek, S. (1981) Donor site of ribosomal peptidyltransferase: Investigation of substrate specificity using 2′(3′)-O-(N-acylaminoacyl)dinucleoside phosphates as models of the 3′-terminus of N-acylaminoacyl transfer ribonucleic acid, Biochemistry 20, 3480-3485.
    • (1981) Biochemistry , vol.20 , pp. 3480-3485
    • Quiggle, K.1    Kumar, G.2    Ott, T.W.3    Ryu, E.K.4    Chladek, S.5
  • 13
    • 0019873831 scopus 로고
    • Stereochemical control of ribosomal peptidyltransferase reaction. Role of amino acid side-chain orientation of acceptor substrate
    • Bhuta, A., Quiggle, K., Ott, T., Ringer, D., and Chladek, S. (1981) Stereochemical control of ribosomal peptidyltransferase reaction. Role of amino acid side-chain orientation of acceptor substrate, Biochemistry 20, 8-15.
    • (1981) Biochemistry , vol.20 , pp. 8-15
    • Bhuta, A.1    Quiggle, K.2    Ott, T.3    Ringer, D.4    Chladek, S.5
  • 14
    • 0019875775 scopus 로고
    • Discrimination between D- and L-tyrosyl transfer ribonucleic acids in peptide chain elongation
    • Yamane, T., Miller, D. L., and Hopfield, J. J. (1981) Discrimination between D- and L-tyrosyl transfer ribonucleic acids in peptide chain elongation, Biochemistry 20, 7059-7068.
    • (1981) Biochemistry , vol.20 , pp. 7059-7068
    • Yamane, T.1    Miller, D.L.2    Hopfield, J.J.3
  • 16
    • 0024968835 scopus 로고
    • A general method for site-specific incorporation of unnatural amino acids into proteins
    • Noren, C. J., Anthony-Cahill, S. J., Griffith, M. C., and Schultz, P. G. (1989) A general method for site-specific incorporation of unnatural amino acids into proteins, Science 244, 182-188.
    • (1989) Science , vol.244 , pp. 182-188
    • Noren, C.J.1    Anthony-Cahill, S.J.2    Griffith, M.C.3    Schultz, P.G.4
  • 17
    • 0027375408 scopus 로고
    • Mutations at U2555, a tRNA-protected base in 23S rRNA, affect translational fidelity
    • O'Connor, M., and Dahlberg, A. E. (1993) Mutations at U2555, a tRNA-protected base in 23S rRNA, affect translational fidelity, Proc. Natl. Acad. Sci. U.S.A. 90, 9214-9218.
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 9214-9218
    • O'Connor, M.1    Dahlberg, A.E.2
  • 18
    • 0028298246 scopus 로고
    • Mutations in the peptidyl transferase region of E. coli 23S ribosomal-RNA affecting translational accuracy
    • Gregory, S. T., Lieberman, K. R., and Dahlberg, A. E. (1994) Mutations in the peptidyl transferase region of E. coli 23S ribosomal-RNA affecting translational accuracy, Nucleic Acid Res. 22, 279-284.
    • (1994) Nucleic Acid Res , vol.22 , pp. 279-284
    • Gregory, S.T.1    Lieberman, K.R.2    Dahlberg, A.E.3
  • 19
    • 0029026749 scopus 로고
    • Ribosome mutants with altered accuracy translate with reduced processivity
    • Dong, H., and Kurland, C. G. (1995) Ribosome mutants with altered accuracy translate with reduced processivity, J. Mol. Biol. 248, 551-561.
    • (1995) J. Mol. Biol , vol.248 , pp. 551-561
    • Dong, H.1    Kurland, C.G.2
  • 20
    • 0030859704 scopus 로고    scopus 로고
    • Conformational analysis of Escherichia coli 30S ribosomes containing the single-base mutations G530U, U1498G, G1401C, and C1501G and the double-base mutation G1401C/C1501G
    • Moine, H., Nurse, K., Ehresmann, B., Ehiesmanrt, C., and Ofengand, J. (1997) Conformational analysis of Escherichia coli 30S ribosomes containing the single-base mutations G530U, U1498G, G1401C, and C1501G and the double-base mutation G1401C/C1501G, Biochemistry 36, 13700-13709.
    • (1997) Biochemistry , vol.36 , pp. 13700-13709
    • Moine, H.1    Nurse, K.2    Ehresmann, B.3    Ehiesmanrt, C.4    Ofengand, J.5
  • 21
    • 0033555251 scopus 로고    scopus 로고
    • Characterization of in vitro and in vivo mutations in non-conserved nucleotides in the ribosomal RNA recognition domain for the ribotoxins ricin and sarcin and the translation elongation factors
    • Macbeth, M. R., and Wool, I. G. (1999) Characterization of in vitro and in vivo mutations in non-conserved nucleotides in the ribosomal RNA recognition domain for the ribotoxins ricin and sarcin and the translation elongation factors, J. Mol. Biol. 285, 567-580.
    • (1999) J. Mol. Biol , vol.285 , pp. 567-580
    • Macbeth, M.R.1    Wool, I.G.2
  • 22
    • 0033582599 scopus 로고    scopus 로고
    • Sites of interaction of streptogramin A and B antibiotics in the peptidyl transferase loop of 23S rRNA and the synergism of their inhibitory mechanisms
    • Porse, B. T., and Garrett, R. A. (1999) Sites of interaction of streptogramin A and B antibiotics in the peptidyl transferase loop of 23S rRNA and the synergism of their inhibitory mechanisms, J. Mol. Biol. 286, 375-387.
    • (1999) J. Mol. Biol , vol.286 , pp. 375-387
    • Porse, B.T.1    Garrett, R.A.2
  • 23
    • 0033515041 scopus 로고    scopus 로고
    • An Escherichia coli strain with all chromosomal rRNA operons inactivated: Complete exchange of rRNA genes between bacteria
    • Asai, T., Zaporojets, D., Squires, C., and Squires, C. L. (1999) An Escherichia coli strain with all chromosomal rRNA operons inactivated: Complete exchange of rRNA genes between bacteria, Proc. Natl. Acad. Sci. U.S.A. 96, 1971-1976.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 1971-1976
    • Asai, T.1    Zaporojets, D.2    Squires, C.3    Squires, C.L.4
  • 24
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban, N., Nissen, P., Hansen, J., Moore, P. B., and Steitz, T. A. (2000) The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution, Science 289, 905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 25
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • Nissen, P., Hansen, J., Ban, N., Moore, P. B., and Steitz, T. A. (2000) The structural basis of ribosome activity in peptide bond synthesis, Science 289, 920-930.
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 26
    • 0024114860 scopus 로고
    • The importance of highly conserved nucleotides in the binding region of chloramphenicol at the peptidyl transfer center of E. coli 23S ribosomal-RNA
    • Vester, B., and Garrett, R. A. (1988) The importance of highly conserved nucleotides in the binding region of chloramphenicol at the peptidyl transfer center of E. coli 23S ribosomal-RNA, EMBO J. 7, 3577-3587.
    • (1988) EMBO J , vol.7 , pp. 3577-3587
    • Vester, B.1    Garrett, R.A.2
  • 27
    • 0032584065 scopus 로고    scopus 로고
    • 23S rRNA positions essential for tRNA binding in ribosomal functional sites
    • Bocchetta, M., Xion, L., Mankin, A. S. (1998) 23S rRNA positions essential for tRNA binding in ribosomal functional sites, Proc. Natl. Acad. Sci. U.S.A. 95, 3525-3530.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 3525-3530
    • Bocchetta, M.1    Xion, L.2    Mankin, A.S.3
  • 28
    • 0029898625 scopus 로고    scopus 로고
    • The influence of base identity and base pairing on the function of the α-sarcin loop of 23S rRNA
    • O'Connor, M., and Dahlberg, A. E. (1996) The influence of base identity and base pairing on the function of the α-sarcin loop of 23S rRNA, Nucleic Acid Res. 24, 2701-2705.
    • (1996) Nucleic Acid Res , vol.24 , pp. 2701-2705
    • O'Connor, M.1    Dahlberg, A.E.2
  • 30
    • 0035253420 scopus 로고    scopus 로고
    • Mutagenesis of the peptidyltransferase center of 23S rRNA: The invariant U2449 is dispensable
    • O'Connor, M., Lee, W.-C. M., Mankad, A., Squires, C. L., and Dahlberg, A. E. (2001) Mutagenesis of the peptidyltransferase center of 23S rRNA: The invariant U2449 is dispensable, Nucleic Acids Res. 29, 710-715.
    • (2001) Nucleic Acids Res , vol.29 , pp. 710-715
    • O'Connor, M.1    Lee, W.-C.M.2    Mankad, A.3    Squires, C.L.4    Dahlberg, A.E.5
  • 31
    • 0035942753 scopus 로고    scopus 로고
    • Ribosomal peptidyl transferase can withstand mutations at the putative catalytic nucleotide
    • Polacek, N., Gaynor, M., Yassin, A., and Mankin, A. S. (2001) Ribosomal peptidyl transferase can withstand mutations at the putative catalytic nucleotide, Nature 411, 498-501.
    • (2001) Nature , vol.411 , pp. 498-501
    • Polacek, N.1    Gaynor, M.2    Yassin, A.3    Mankin, A.S.4
  • 32
    • 0038547955 scopus 로고    scopus 로고
    • Enhanced D-amino acid incorporation into protein by modified ribosomes
    • Dedkova, L. M., Fahmi, N. E., Golovine, S. Y., and Hecht, S. M. (2003) Enhanced D-amino acid incorporation into protein by modified ribosomes, J. Am. Chem. Soc. 125, 6616-6617.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 6616-6617
    • Dedkova, L.M.1    Fahmi, N.E.2    Golovine, S.Y.3    Hecht, S.M.4
  • 33
    • 0033529240 scopus 로고    scopus 로고
    • Effects of release factor 1 on in vitro protein translation and the elaboration of proteins containing unnatural amino acids
    • Short, G. F., III, Golovine, S. Y., and Hecht, S. M. (1999) Effects of release factor 1 on in vitro protein translation and the elaboration of proteins containing unnatural amino acids, Biochemistry 38, 8808-8819.
    • (1999) Biochemistry , vol.38 , pp. 8808-8819
    • Short III, G.F.1    Golovine, S.Y.2    Hecht, S.M.3
  • 35
    • 0030669531 scopus 로고    scopus 로고
    • Structurally modified firefly luciferase. Effects of amino acid substitution at position 286
    • Arslan, T., Mamaev, S. V., Mamaeva, N. V., and Hecht, S. M. (1997) Structurally modified firefly luciferase. Effects of amino acid substitution at position 286, J. Am. Chem. Soc. 119, 10877-10887.
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 10877-10887
    • Arslan, T.1    Mamaev, S.V.2    Mamaeva, N.V.3    Hecht, S.M.4
  • 36
    • 0016709592 scopus 로고
    • Purification and properties of Escherichia coli dihydrofolate reductase
    • Baccanari, D., Phillips, A., Smith, S., Sinski, D., and Burchall, J. (1975) Purification and properties of Escherichia coli dihydrofolate reductase, Biochemistry 14, 5267-5270.
    • (1975) Biochemistry , vol.14 , pp. 5267-5270
    • Baccanari, D.1    Phillips, A.2    Smith, S.3    Sinski, D.4    Burchall, J.5
  • 37
    • 0029617892 scopus 로고
    • The involvement of two distinct regions of 23S ribosomal RNA in tRNA selection
    • O'Connor, M., and Dahlberg, A. E. (1995) The involvement of two distinct regions of 23S ribosomal RNA in tRNA selection, J. Mol. Biol. 254, 838-847.
    • (1995) J. Mol. Biol , vol.254 , pp. 838-847
    • O'Connor, M.1    Dahlberg, A.E.2
  • 38
    • 12644274577 scopus 로고    scopus 로고
    • Mutational analysis of two highly conserved UGG sequences of 23S rRNA from E. coli
    • Spahn, C. M. T., Remme, J., Schafer, M. A., and Nierhaus, K. H. (1996) Mutational analysis of two highly conserved UGG sequences of 23S rRNA from E. coli, J. Biol. Chem. 271, 32849-32856.
    • (1996) J. Biol. Chem , vol.271 , pp. 32849-32856
    • Spahn, C.M.T.1    Remme, J.2    Schafer, M.A.3    Nierhaus, K.H.4
  • 39
    • 33845945458 scopus 로고
    • L-Amino acid oxidase (snake venom)
    • Wellner, D. (1971) L-Amino acid oxidase (snake venom), Methods Enzymol. 17, 597-600.
    • (1971) Methods Enzymol , vol.17 , pp. 597-600
    • Wellner, D.1
  • 40
    • 0023472472 scopus 로고
    • Tricine sodium dodecyl sulfate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 kDa to 100 kDa
    • Schagger, H., and VonJagow, G. (1987) Tricine sodium dodecyl sulfate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 kDa to 100 kDa, Anal. Biochem. 166, 368-372.
    • (1987) Anal. Biochem , vol.166 , pp. 368-372
    • Schagger, H.1    VonJagow, G.2
  • 41
    • 11944269377 scopus 로고
    • Probing the synthetic capabilities of a center of biochemical catalysis
    • Hecht, S. M. (1992) Probing the synthetic capabilities of a center of biochemical catalysis, Acc. Chem. Res. 25, 545-552.
    • (1992) Acc. Chem. Res , vol.25 , pp. 545-552
    • Hecht, S.M.1
  • 42
    • 0037167581 scopus 로고    scopus 로고
    • Site-specific incorporation of (aminooxy)acetic acid into protein
    • Eisenhauer, B. M., and Hecht, S. M. (2002) Site-specific incorporation of (aminooxy)acetic acid into protein, Biochemistry 41, 11472-1478.
    • (2002) Biochemistry , vol.41 , pp. 11472-11478
    • Eisenhauer, B.M.1    Hecht, S.M.2
  • 43
    • 0032495762 scopus 로고    scopus 로고
    • Ribosome-mediated incorporation of hydrazinophenylalanine into modified peptide and protein analogues
    • Killian, J. A., van Cleve, M. D., Shayo, Y. P., and Hecht, S. M. (1998) Ribosome-mediated incorporation of hydrazinophenylalanine into modified peptide and protein analogues, J. Am. Chem. Soc. 120, 3032-3042.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 3032-3042
    • Killian, J.A.1    van Cleve, M.D.2    Shayo, Y.P.3    Hecht, S.M.4
  • 44
    • 0018891591 scopus 로고
    • Evolutionary relationship between Halobacterium cutirubrum and eukaryotes determined by use of aminoacyl-tRNA synthetases as phylogenetic probes
    • Kwok, Y., and Wong, J. T. (1980) Evolutionary relationship between Halobacterium cutirubrum and eukaryotes determined by use of aminoacyl-tRNA synthetases as phylogenetic probes, Can. J. Biochem. 58, 213-218.
    • (1980) Can. J. Biochem , vol.58 , pp. 213-218
    • Kwok, Y.1    Wong, J.T.2
  • 45
    • 0025270551 scopus 로고
    • + ternary complex. Substrate binding and a model for the transition state
    • + ternary complex. Substrate binding and a model for the transition state, Biochemistry 29, 3263-3277.
    • (1990) Biochemistry , vol.29 , pp. 3263-3277
    • Bystroff, C.1    Oatley, S.J.2    Kraut, J.3
  • 46
    • 0024512066 scopus 로고
    • Hydrophobic interactions via mutants of Escherichia coli dihydrofolate reductase: Separation of binding and catalysis
    • Murphy, D. J., and Benkovic, S. J. (1989) Hydrophobic interactions via mutants of Escherichia coli dihydrofolate reductase: Separation of binding and catalysis, Biochemistry 28, 3025-3031.
    • (1989) Biochemistry , vol.28 , pp. 3025-3031
    • Murphy, D.J.1    Benkovic, S.J.2
  • 47
    • 0032480765 scopus 로고    scopus 로고
    • Site-directed mutagenesis of histidine 245 in firefly luciferase: A proposed model of the active site
    • Branchini, B. B., Magyar, R. A., Murtiashaw, M. H., Anderson, S. A., and Zimmer, M. (1998) Site-directed mutagenesis of histidine 245 in firefly luciferase: A proposed model of the active site, Biochemistry 37, 15311-15319.
    • (1998) Biochemistry , vol.37 , pp. 15311-15319
    • Branchini, B.B.1    Magyar, R.A.2    Murtiashaw, M.H.3    Anderson, S.A.4    Zimmer, M.5
  • 48
    • 0029583854 scopus 로고
    • UGA suppression by a mutant RNA of the large ribosomal subunit
    • Jemiolo, D. K., Pagel, F. T., Murgola, E. J. (1995) UGA suppression by a mutant RNA of the large ribosomal subunit, Proc. Natl. Acad. Sci. U.S.A. 92, 12309-12313.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 12309-12313
    • Jemiolo, D.K.1    Pagel, F.T.2    Murgola, E.J.3


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