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Volumn 40, Issue 5, 2012, Pages 2247-2257

Crucial elements that maintain the interactions between the regulatory TnaC peptide and the ribosome exit tunnel responsible for Trp inhibition of ribosome function

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; ASPARTIC ACID; CYTOSINE; GUANINE; NUCLEOTIDE; PEPTIDE; REGULATOR PROTEIN; RNA 23S; TNAC PEPTIDE; TRANSFER RNA; TRYPTOPHAN; UNCLASSIFIED DRUG; URIDINE;

EID: 84858411885     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkr1052     Document Type: Article
Times cited : (15)

References (45)
  • 1
    • 0022352611 scopus 로고
    • Evidence for transcription antitermination control of tryptophanase operon expression in Escherichia coli K-12
    • Stewart, V. and Yanofsky, C. (1985) Evidence for transcription antitermination control of tryptophanase operon expression in Escherichia coli K-12. J. Bacteriol., 164, 731-740.
    • (1985) J. Bacteriol. , vol.164 , pp. 731-740
    • Stewart, V.1    Yanofsky, C.2
  • 2
    • 0019825937 scopus 로고
    • Nucleotide sequence of the structural gene for tryptophanase of Escherichia coli K-12
    • Deeley, M. C. and Yanofsky, C. (1981) Nucleotide sequence of the structural gene for tryptophanase of Escherichia coli K-12. J. Bacteriol., 147, 787-796.
    • (1981) J. Bacteriol. , vol.147 , pp. 787-796
    • Deeley, M.C.1    Yanofsky, C.2
  • 3
    • 4644277087 scopus 로고    scopus 로고
    • Stationary-phase quorum-sensing signals affect autoinducer-2 and gene expression in Escherichia coli
    • Ren, D., Bedzyk, L. A., Ye, R. W., Thomas, S. M. and Wood, T. K. (2004) Stationary-phase quorum-sensing signals affect autoinducer-2 and gene expression in Escherichia coli. Appl. Environ. Microbiol., 70, 2038-2043.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 2038-2043
    • Ren, D.1    Bedzyk, L.A.2    Ye, R.W.3    Thomas, S.M.4    Wood, T.K.5
  • 4
    • 0019982963 scopus 로고
    • Transcription initiation at the tryptophanase promoter of Escherichia coli K-12
    • Deeley, M. C. and Yanofsky, C. (1982) Transcription initiation at the tryptophanase promoter of Escherichia coli K-12. J. Bacteriol., 151, 942-951.
    • (1982) J. Bacteriol. , vol.151 , pp. 942-951
    • Deeley, M.C.1    Yanofsky, C.2
  • 5
    • 0035910426 scopus 로고    scopus 로고
    • Reproducing tna operon regulation in vitro in an S-30 system. Tryptophan induction inhibits cleavage of TnaC peptidyl-tRNA
    • Gong, F. and Yanofsky, C. (2001) Reproducing tna operon regulation in vitro in an S-30 system. Tryptophan induction inhibits cleavage of TnaC peptidyl-tRNA. J. Biol. Chem., 276, 1974-1983.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1974-1983
    • Gong, F.1    Yanofsky, C.2
  • 6
    • 0035979174 scopus 로고    scopus 로고
    • The mechanism of tryptophan induction of tryptophanase operon expression: Tryptophan inhibits release factor-mediated cleavage of TnaC-peptidyl-tRNA(Pro)
    • Gong, F., Ito, K., Nakamura, Y. and Yanofsky, C. (2001) The mechanism of tryptophan induction of tryptophanase operon expression: tryptophan inhibits release factor-mediated cleavage of TnaC-peptidyl-tRNA(Pro). Proc. Natl Acad. Sci. USA, 98, 8997-9001.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 8997-9001
    • Gong, F.1    Ito, K.2    Nakamura, Y.3    Yanofsky, C.4
  • 7
    • 0033933221 scopus 로고    scopus 로고
    • Rho-dependent transcription termination in the tna operon of Escherichia coli: Roles of the boxA sequence and the rut site
    • Konan, K. V. and Yanofsky, C. (2000) Rho-dependent transcription termination in the tna operon of Escherichia coli: roles of the boxA sequence and the rut site. J. Bacteriol., 182, 3981-3988.
    • (2000) J. Bacteriol. , vol.182 , pp. 3981-3988
    • Konan, K.V.1    Yanofsky, C.2
  • 8
    • 47249162502 scopus 로고    scopus 로고
    • Conserved residues Asp16 and Pro24 of TnaC-tRNAPro participate in tryptophan induction of tna operon expression
    • Cruz-Vera, L. R. and Yanofsky, C. (2008) Conserved residues Asp16 and Pro24 of TnaC-tRNAPro participate in tryptophan induction of tna operon expression. J. Bacteriol., 190, 4791-4797.
    • (2008) J. Bacteriol. , vol.190 , pp. 4791-4797
    • Cruz-Vera, L.R.1    Yanofsky, C.2
  • 9
    • 77952589053 scopus 로고    scopus 로고
    • Recognition of the regulatory nascent chain TnaC by the ribosome
    • Trabuco, L. G., Harrison, C. B., Schreiner, E. and Schulten, K. (2010) Recognition of the regulatory nascent chain TnaC by the ribosome. Structure, 18, 627-637.
    • (2010) Structure , vol.18 , pp. 627-637
    • Trabuco, L.G.1    Harrison, C.B.2    Schreiner, E.3    Schulten, K.4
  • 10
    • 0025369085 scopus 로고
    • TRNA(Trp) translation of leader peptide codon 12 and other factors that regulate expression of the tryptophanase operon
    • Gollnick, P. and Yanofsky, C. (1990) tRNA(Trp) translation of leader peptide codon 12 and other factors that regulate expression of the tryptophanase operon. J. Bacteriol., 172, 3100-3107.
    • (1990) J. Bacteriol. , vol.172 , pp. 3100-3107
    • Gollnick, P.1    Yanofsky, C.2
  • 11
    • 0037072627 scopus 로고    scopus 로고
    • Instruction of translating ribosome by nascent peptide
    • Gong, F. and Yanofsky, C. (2002) Instruction of translating ribosome by nascent peptide. Science, 297, 1864-1867.
    • (2002) Science , vol.297 , pp. 1864-1867
    • Gong, F.1    Yanofsky, C.2
  • 13
    • 0037040411 scopus 로고    scopus 로고
    • The ribosomal exit tunnel functions as a discriminating gate
    • Nakatogawa, H. and Ito, K. (2002) The ribosomal exit tunnel functions as a discriminating gate. Cell, 108, 629-636.
    • (2002) Cell , vol.108 , pp. 629-636
    • Nakatogawa, H.1    Ito, K.2
  • 14
    • 70450222724 scopus 로고    scopus 로고
    • A ribosome-nascent chain sensor of membrane protein biogenesis in Bacillus subtilis
    • Chiba, S., Lamsa, A. and Pogliano, K. (2009) A ribosome-nascent chain sensor of membrane protein biogenesis in Bacillus subtilis. EMBO J., 28, 3461-3475.
    • (2009) EMBO J. , vol.28 , pp. 3461-3475
    • Chiba, S.1    Lamsa, A.2    Pogliano, K.3
  • 15
    • 43049089746 scopus 로고    scopus 로고
    • Molecular mechanism of drug-dependent ribosome stalling
    • Vazquez-Laslop, N., Thum, C. and Mankin, A. S. (2008) Molecular mechanism of drug-dependent ribosome stalling. Mol. Cell, 30, 190-202.
    • (2008) Mol. Cell , vol.30 , pp. 190-202
    • Vazquez-Laslop, N.1    Thum, C.2    Mankin, A.S.3
  • 16
    • 1642570293 scopus 로고    scopus 로고
    • A nascent polypeptide domain that can regulate translation elongation
    • Fang, P., Spevak, C. C., Wu, C. and Sachs, M. S. (2004) A nascent polypeptide domain that can regulate translation elongation. Proc. Natl Acad. Sci. USA, 101, 4059-4064.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 4059-4064
    • Fang, P.1    Spevak, C.C.2    Wu, C.3    Sachs, M.S.4
  • 17
    • 33845922611 scopus 로고    scopus 로고
    • Evolutionary changes in the fungal carbamoyl-phosphate synthetase small subunit gene and its associated upstream open reading frame
    • Hood, H. M., Spevak, C. C. and Sachs, M. S. (2007) Evolutionary changes in the fungal carbamoyl-phosphate synthetase small subunit gene and its associated upstream open reading frame. Fungal Genet. Biol., 44, 93-104.
    • (2007) Fungal Genet. Biol. , vol.44 , pp. 93-104
    • Hood, H.M.1    Spevak, C.C.2    Sachs, M.S.3
  • 18
    • 78650354576 scopus 로고    scopus 로고
    • Sequence requirements for ribosome stalling by the arginine attenuator peptide
    • Spevak, C. C., Ivanov, I. P. and Sachs, M. S. (2010) Sequence requirements for ribosome stalling by the arginine attenuator peptide. J. Biol. Chem., 285, 40933-40942.
    • (2010) J. Biol. Chem. , vol.285 , pp. 40933-40942
    • Spevak, C.C.1    Ivanov, I.P.2    Sachs, M.S.3
  • 19
    • 23044445236 scopus 로고    scopus 로고
    • Features of ribosome-peptidyl-tRNA interactions essential for tryptophan induction of tna operon expression
    • Cruz-Vera, L. R., Rajagopal, S., Squires, C. and Yanofsky, C. (2005) Features of ribosome-peptidyl-tRNA interactions essential for tryptophan induction of tna operon expression. Mol. Cell, 19, 333-343.
    • (2005) Mol. Cell , vol.19 , pp. 333-343
    • Cruz-Vera, L.R.1    Rajagopal, S.2    Squires, C.3    Yanofsky, C.4
  • 22
    • 66149135994 scopus 로고    scopus 로고
    • 23S rRNA nucleotides in the peptidyl transferase center are essential for tryptophanase operon induction
    • Yang, R., Cruz-Vera, L. R. and Yanofsky, C. (2009) 23S rRNA nucleotides in the peptidyl transferase center are essential for tryptophanase operon induction. J. Bacteriol., 191, 3445-3450.
    • (2009) J. Bacteriol. , vol.191 , pp. 3445-3450
    • Yang, R.1    Cruz-Vera, L.R.2    Yanofsky, C.3
  • 23
    • 0037072619 scopus 로고    scopus 로고
    • Biochemistry. Sense and sensitivity-controlling the ribosome
    • Sachs, M. S. and Geballe, A. P. (2002) Biochemistry. Sense and sensitivity-controlling the ribosome. Science, 297, 1820-1821.
    • (2002) Science , vol.297 , pp. 1820-1821
    • Sachs, M.S.1    Geballe, A.P.2
  • 24
    • 77956884449 scopus 로고    scopus 로고
    • The key function of a conserved and modified rRNA residue in the ribosomal response to the nascent peptide
    • Vazquez-Laslop, N., Ramu, H., Klepacki, D., Kannan, K. and Mankin, A. S. (2010) The key function of a conserved and modified rRNA residue in the ribosomal response to the nascent peptide. EMBO J., 29, 3108-3117.
    • (2010) EMBO J. , vol.29 , pp. 3108-3117
    • Vazquez-Laslop, N.1    Ramu, H.2    Klepacki, D.3    Kannan, K.4    Mankin, A.S.5
  • 25
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2. 4 Aresolution
    • 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 Aresolution. 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
  • 26
    • 78049302075 scopus 로고    scopus 로고
    • Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action
    • Dunkle, J. A., Xiong, L., Mankin, A. S. and Cate, J. H. (2010) Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action. Proc. Natl Acad. Sci. USA, 107, 17152-17157.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 17152-17157
    • Dunkle, J.A.1    Xiong, L.2    Mankin, A.S.3    Cate, J.H.4
  • 27
    • 64749115067 scopus 로고    scopus 로고
    • The plasticity of a translation arrest motif yields insights into nascent polypeptide recognition inside the ribosome tunnel
    • Yap, M. N. and Bernstein, H. D. (2009) The plasticity of a translation arrest motif yields insights into nascent polypeptide recognition inside the ribosome tunnel. Mol. Cell, 34, 201-211.
    • (2009) Mol. Cell , vol.34 , pp. 201-211
    • Yap, M.N.1    Bernstein, H.D.2
  • 29
    • 0027234622 scopus 로고
    • Translational inhibition mediated by a short upstream open reading frame in the human cytomegalovirus gpUL4 (gp48) transcript
    • Degnin, C. R., Schleiss, M. R., Cao, J. and Geballe, A. P. (1993) Translational inhibition mediated by a short upstream open reading frame in the human cytomegalovirus gpUL4 (gp48) transcript. J. Virol., 67, 5514-5521.
    • (1993) J. Virol. , vol.67 , pp. 5514-5521
    • Degnin, C.R.1    Schleiss, M.R.2    Cao, J.3    Geballe, A.P.4
  • 30
    • 79955022180 scopus 로고    scopus 로고
    • Recruitment of a species-specific translational arrest module to monitor different cellular processes
    • Chiba, S., Kanamori, T., Ueda, T., Akiyama, Y., Pogliano, K. and Ito, K. (2011) Recruitment of a species-specific translational arrest module to monitor different cellular processes. Proc. Natl Acad. Sci. USA, 108, 6073-6078.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 6073-6078
    • Chiba, S.1    Kanamori, T.2    Ueda, T.3    Akiyama, Y.4    Pogliano, K.5    Ito, K.6
  • 31
    • 79954997529 scopus 로고    scopus 로고
    • Picky nascent peptides do not talk to foreign ribosomes
    • Vazquez-Laslop, N. and Mankin, A. S. (2011) Picky nascent peptides do not talk to foreign ribosomes. Proc. Natl Acad. Sci. USA, 108, 5931-5932.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 5931-5932
    • Vazquez-Laslop, N.1    Mankin, A.S.2
  • 32
    • 0033014076 scopus 로고    scopus 로고
    • Erythromycin resistance mutations in ribosomal proteins L22 and L4 perturb the higher order structure of 23 S ribosomal RNA
    • Gregory, S. T. and Dahlberg, A. E. (1999) Erythromycin resistance mutations in ribosomal proteins L22 and L4 perturb the higher order structure of 23 S ribosomal RNA. J. Mol. Biol., 289, 827-834.
    • (1999) J. Mol. Biol. , vol.289 , pp. 827-834
    • Gregory, S.T.1    Dahlberg, A.E.2
  • 33
    • 0035162904 scopus 로고    scopus 로고
    • Binding site of macrolide antibiotics on the ribosome: New resistance mutation identifies a specific interaction of ketolides with rRNA
    • Garza-Ramos, G., Xiong, L., Zhong, P. and Mankin, A. (2001) Binding site of macrolide antibiotics on the ribosome: new resistance mutation identifies a specific interaction of ketolides with rRNA. J. Bacteriol., 183, 6898-6907.
    • (2001) J. Bacteriol. , vol.183 , pp. 6898-6907
    • Garza-Ramos, G.1    Xiong, L.2    Zhong, P.3    Mankin, A.4
  • 34
    • 0031912037 scopus 로고    scopus 로고
    • Identification of the rrmA gene encoding the 23S rRNA m1G745 methyltransferase in Escherichia coli and characterization of an m1G745-deficient mutant
    • Gustafsson, C. and Persson, B. C. (1998) Identification of the rrmA gene encoding the 23S rRNA m1G745 methyltransferase in Escherichia coli and characterization of an m1G745-deficient mutant. J. Bacteriol., 180, 359-365.
    • (1998) J. Bacteriol. , vol.180 , pp. 359-365
    • Gustafsson, C.1    Persson, B.C.2
  • 35
    • 33644851066 scopus 로고    scopus 로고
    • Changes produced by bound tryptophan in the ribosome peptidyl transferase center in response to TnaC, a nascent leader peptide
    • Cruz-Vera, L. R., Gong, M. and Yanofsky, C. (2006) Changes produced by bound tryptophan in the ribosome peptidyl transferase center in response to TnaC, a nascent leader peptide. Proc. Natl Acad. Sci. USA, 103, 3598-3603.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 3598-3603
    • Cruz-Vera, L.R.1    Gong, M.2    Yanofsky, C.3
  • 36
    • 34247868068 scopus 로고    scopus 로고
    • Ribosomal features essential for tna operon induction: Tryptophan binding at the peptidyl transferase center
    • Cruz-Vera, L. R., New, A., Squires, C. and Yanofsky, C. (2007) Ribosomal features essential for tna operon induction: tryptophan binding at the peptidyl transferase center. J. Bacteriol., 189, 3140-3146.
    • (2007) J. Bacteriol. , vol.189 , pp. 3140-3146
    • Cruz-Vera, L.R.1    New, A.2    Squires, C.3    Yanofsky, C.4
  • 37
    • 0019513663 scopus 로고
    • Gene organization and primary structure of a ribosomal RNA operon from Escherichia coli
    • Brosius, J., Dull, T. J., Sleeter, D. D. and Noller, H. F. (1981) Gene organization and primary structure of a ribosomal RNA operon from Escherichia coli. J. Mol. Biol., 148, 107-127.
    • (1981) J. Mol. Biol. , vol.148 , pp. 107-127
    • Brosius, J.1    Dull, T.J.2    Sleeter, D.D.3    Noller, H.F.4
  • 38
    • 2542470615 scopus 로고    scopus 로고
    • The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release
    • Youngman, E. M., Brunelle, J. L., Kochaniak, A. B. and Green, R. (2004) The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release. Cell, 117, 589-599.
    • (2004) Cell , vol.117 , pp. 589-599
    • Youngman, E.M.1    Brunelle, J.L.2    Kochaniak, A.B.3    Green, R.4
  • 39
    • 33744988346 scopus 로고    scopus 로고
    • Fast, easy and efficient: Site-specific insertion of transgenes into enterobacterial chromosomes using Tn7 without need for selection of the insertion event
    • McKenzie, G. J. and Craig, N. L. (2006) Fast, easy and efficient: site-specific insertion of transgenes into enterobacterial chromosomes using Tn7 without need for selection of the insertion event. BMC Microbiol., 6, 39.
    • (2006) BMC Microbiol. , vol.6 , pp. 39
    • McKenzie, G.J.1    Craig, N.L.2
  • 41
    • 0024334898 scopus 로고
    • Interaction of tRNA with 23S rRNA in the ribosomal A, P, and e sites
    • Moazed, D. and Noller, H. F. (1989) Interaction of tRNA with 23S rRNA in the ribosomal A, P, and E sites. Cell, 57, 585-597.
    • (1989) Cell , vol.57 , pp. 585-597
    • Moazed, D.1    Noller, H.F.2
  • 42
    • 0026006958 scopus 로고
    • Physiological studies of tryptophan transport and tryptophanase operon induction in Escherichia coli
    • Yanofsky, C., Horn, V. and Gollnick, P. (1991) Physiological studies of tryptophan transport and tryptophanase operon induction in Escherichia coli. J. Bacteriol., 173, 6009-6017.
    • (1991) J. Bacteriol. , vol.173 , pp. 6009-6017
    • Yanofsky, C.1    Horn, V.2    Gollnick, P.3
  • 43
    • 79953106751 scopus 로고    scopus 로고
    • The ribosomal tunnel as a functional environment for nascent polypeptide folding and translational stalling
    • Wilson, D. N. and Beckmann, R. (2011) The ribosomal tunnel as a functional environment for nascent polypeptide folding and translational stalling. Curr. Opin. Struct. Biol., 21, 274-282.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 274-282
    • Wilson, D.N.1    Beckmann, R.2
  • 44
    • 0037439087 scopus 로고    scopus 로고
    • Structure of 23S rRNA hairpin 35 and its interaction with the tylosin-resistance methyltransferase RlmAII
    • Lebars, I., Yoshizawa, S., Stenholm, A. R., Guittet, E., Douthwaite, S. and Fourmy, D. (2003) Structure of 23S rRNA hairpin 35 and its interaction with the tylosin-resistance methyltransferase RlmAII. EMBO J., 22, 183-192.
    • (2003) EMBO J. , vol.22 , pp. 183-192
    • Lebars, I.1    Yoshizawa, S.2    Stenholm, A.R.3    Guittet, E.4    Douthwaite, S.5    Fourmy, D.6
  • 45
    • 0345687915 scopus 로고    scopus 로고
    • Products transcribed from rearranged rrn genes of Escherichia coli can assemble to form functional ribosomes
    • Zaporojets, D., French, S. and Squires, C. L. (2003) Products transcribed from rearranged rrn genes of Escherichia coli can assemble to form functional ribosomes. J. Bacteriol., 185, 6921-6927.
    • (2003) J. Bacteriol. , vol.185 , pp. 6921-6927
    • Zaporojets, D.1    French, S.2    Squires, C.L.3


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