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Volumn 80, Issue 1, 2011, Pages 54-67

Antibiotic-induced ribosomal assembly defects result from changes in the synthesis of ribosomal proteins

Author keywords

[No Author keywords available]

Indexed keywords

CHLORAMPHENICOL; ERYTHROMYCIN; PROTEIN PRECURSOR; RIBOSOME PROTEIN;

EID: 79953038837     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2011.07555.x     Document Type: Article
Times cited : (28)

References (73)
  • 1
    • 0014675220 scopus 로고
    • Synthesis and maturation of ribosomal RNA in Escherichia coli
    • Adesnik, M., and Levinthal, C. (1969) Synthesis and maturation of ribosomal RNA in Escherichia coli. J Mol Biol 46: 281-303.
    • (1969) J Mol Biol , vol.46 , pp. 281-303
    • Adesnik, M.1    Levinthal, C.2
  • 2
    • 0021347244 scopus 로고
    • Translational coupling of the trpB and trpA genes in the Escherichia coli tryptophan operon
    • Aksoy, S., Squires, C., and Squires, C. (1984) Translational coupling of the trpB and trpA genes in the Escherichia coli tryptophan operon. J Bacteriol 157: 363-367.
    • (1984) J Bacteriol , vol.157 , pp. 363-367
    • Aksoy, S.1    Squires, C.2    Squires, C.3
  • 3
    • 58449101336 scopus 로고    scopus 로고
    • Ribosome biogenesis is temperature-dependent and delayed in Escherichia coli lacking the chaperones DnaK or DnaJ
    • Al Refaii, A., and Alix, J. (2009) Ribosome biogenesis is temperature-dependent and delayed in Escherichia coli lacking the chaperones DnaK or DnaJ. Mol Microbiol 71: 748-762.
    • (2009) Mol Microbiol , vol.71 , pp. 748-762
    • Al Refaii, A.1    Alix, J.2
  • 5
    • 0000640710 scopus 로고
    • Modulation of chemical composition and other parameters of the cell by the growth rate
    • In Neinhardt, F., Ingraham, J.L., Low, K.B., Magasanik, B., Schaechter, M., and Umbarger, H.E. (eds). Washington, DC: American Society for Microbiology
    • Bremer, H., and Dennis, P.P. (1987) Modulation of chemical composition and other parameters of the cell by the growth rate. In Escherichia coli and Salmonella typhimurium Cellular and Molecular Biology. Neinhardt, F., Ingraham, J.L., Low, K.B., Magasanik, B., Schaechter, M., and Umbarger, H.E. (eds). Washington, DC: American Society for Microbiology, pp. 1527-1542.
    • (1987) Escherichia coli and Salmonella typhimurium Cellular and Molecular Biology , pp. 1527-1542
    • Bremer, H.1    Dennis, P.P.2
  • 6
    • 78049250815 scopus 로고    scopus 로고
    • Revisiting the structures of several antibiotics bound to the bacterial ribosome
    • Bulkley, D., Innis, C., Blaha, G., and Steitz, T. (2010) Revisiting the structures of several antibiotics bound to the bacterial ribosome. Proc Natl Acad Sci USA 107: 17158-17163.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 17158-17163
    • Bulkley, D.1    Innis, C.2    Blaha, G.3    Steitz, T.4
  • 7
    • 0024206339 scopus 로고
    • Translational regulation of the spc operon in Escherichia coli. Identification and structural analysis of the target site for S8 repressor protein
    • Cerretti, D., Mattheakis, L., Kearney, K., Vu, L., and Nomura, M. (1988) Translational regulation of the spc operon in Escherichia coli. Identification and structural analysis of the target site for S8 repressor protein. J Mol Biol 204: 309-329.
    • (1988) J Mol Biol , vol.204 , pp. 309-329
    • Cerretti, D.1    Mattheakis, L.2    Kearney, K.3    Vu, L.4    Nomura, M.5
  • 8
    • 0027374650 scopus 로고
    • Dissection of the his leader pause site by base substitution reveals a multipartite signal that includes a pause RNA hairpin
    • Chan, C., and Landick, R. (1993) Dissection of the his leader pause site by base substitution reveals a multipartite signal that includes a pause RNA hairpin. J Mol Biol 233: 25-42.
    • (1993) J Mol Biol , vol.233 , pp. 25-42
    • Chan, C.1    Landick, R.2
  • 9
    • 0037316190 scopus 로고    scopus 로고
    • A microarray-based antibiotic screen identifies a regulatory role for supercoiling in the osmotic stress response of Escherichia coli
    • Cheung, K., Badarinarayana, V., Selinger, D., Janse, D., and Church, G. (2003) A microarray-based antibiotic screen identifies a regulatory role for supercoiling in the osmotic stress response of Escherichia coli. Genome Res 13: 206-215.
    • (2003) Genome Res , vol.13 , pp. 206-215
    • Cheung, K.1    Badarinarayana, V.2    Selinger, D.3    Janse, D.4    Church, G.5
  • 10
    • 0028963048 scopus 로고
    • Erythromycin inhibits the assembly of the large ribosomal subunit in growing Escherichia coli cells
    • Chittum, H., and Champney, W. (1995) Erythromycin inhibits the assembly of the large ribosomal subunit in growing Escherichia coli cells. Curr Microbiol 30: 273-279.
    • (1995) Curr Microbiol , vol.30 , pp. 273-279
    • Chittum, H.1    Champney, W.2
  • 11
    • 0028804889 scopus 로고
    • Control of rRNA transcription in Escherichia coli
    • Condon, C., Squires, C., and Squires, C. (1995) Control of rRNA transcription in Escherichia coli. Microbiol Rev 59: 623-645.
    • (1995) Microbiol Rev , vol.59 , pp. 623-645
    • Condon, C.1    Squires, C.2    Squires, C.3
  • 12
    • 0037319895 scopus 로고    scopus 로고
    • Assembly of the 30S ribosomal subunit
    • Culver, G. (2003) Assembly of the 30S ribosomal subunit. Biopolymers 68: 234-249.
    • (2003) Biopolymers , vol.68 , pp. 234-249
    • Culver, G.1
  • 13
    • 36949077276 scopus 로고
    • Effect of drugs upon components of bacterial cytoplasm
    • Dagley, S., and Sykes, J. (1959) Effect of drugs upon components of bacterial cytoplasm. Nature 183: 1608-1609.
    • (1959) Nature , vol.183 , pp. 1608-1609
    • Dagley, S.1    Sykes, J.2
  • 14
    • 0019484130 scopus 로고
    • Identification of ribosomal protein S7 as a repressor of translation within the str operon of E. coli
    • Dean, D., Yates, J., and Nomura, M. (1981) Identification of ribosomal protein S7 as a repressor of translation within the str operon of E. coli. Cell 24: 413-419.
    • (1981) Cell , vol.24 , pp. 413-419
    • Dean, D.1    Yates, J.2    Nomura, M.3
  • 15
    • 0017033814 scopus 로고
    • Effects of chloramphenicol on the transcriptional activities of ribosomal RNA and ribosomal protein genes in Escherichia coli
    • Dennis, P. (1976) Effects of chloramphenicol on the transcriptional activities of ribosomal RNA and ribosomal protein genes in Escherichia coli. J Mol Biol 108: 535-546.
    • (1976) J Mol Biol , vol.108 , pp. 535-546
    • Dennis, P.1
  • 16
    • 0025912716 scopus 로고
    • Lack of complete cooperativity of ribosome assembly in vitro and its possible relevance to in vivo ribosome assembly and the regulation of ribosomal gene expression
    • Dodd, J., Kolb, J., and Nomura, M. (1991) Lack of complete cooperativity of ribosome assembly in vitro and its possible relevance to in vivo ribosome assembly and the regulation of ribosomal gene expression. Biochimie 73: 757-767.
    • (1991) Biochimie , vol.73 , pp. 757-767
    • Dodd, J.1    Kolb, J.2    Nomura, M.3
  • 17
    • 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., Xiong, L., Mankin, A., and Cate, J. (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.1    Xiong, L.2    Mankin, A.3    Cate, J.4
  • 18
    • 0023726939 scopus 로고
    • Ribosomal protein L20 can replace the assembly-initiator protein L24 at low temperatures
    • Franceschi, F., and Nierhaus, K. (1988) Ribosomal protein L20 can replace the assembly-initiator protein L24 at low temperatures. Biochemistry 27: 7056-7059.
    • (1988) Biochemistry , vol.27 , pp. 7056-7059
    • Franceschi, F.1    Nierhaus, K.2
  • 19
    • 0025051302 scopus 로고
    • Ribosomal proteins L15 and L16 are mere late assembly proteins of the large ribosomal subunit. Analysis of an Escherichia coli mutant lacking L15
    • Franceschi, F., and Nierhaus, K. (1990) Ribosomal proteins L15 and L16 are mere late assembly proteins of the large ribosomal subunit. Analysis of an Escherichia coli mutant lacking L15. J Biol Chem 265: 16676-16682.
    • (1990) J Biol Chem , vol.265 , pp. 16676-16682
    • Franceschi, F.1    Nierhaus, K.2
  • 20
    • 0028932215 scopus 로고
    • The umpA gene of Escherichia coli encodes phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (lgt) and regulates thymidylate synthase levels through translational coupling
    • Gan, K., Sankaran, K., Williams, M., Aldea, M., Rudd, K., Kushner, S., etal. (1995) The umpA gene of Escherichia coli encodes phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (lgt) and regulates thymidylate synthase levels through translational coupling. J Bacteriol 177: 1879-1882.
    • (1995) J Bacteriol , vol.177 , pp. 1879-1882
    • Gan, K.1    Sankaran, K.2    Williams, M.3    Aldea, M.4    Rudd, K.5    Kushner, S.6
  • 21
    • 0024349775 scopus 로고
    • Independent and coupled translational initiation of atp genes in Escherichia coli: experiments using chromosomal and plasmid-borne lacZ fusions
    • Gerstel, B., and McCarthy, J. (1989) Independent and coupled translational initiation of atp genes in Escherichia coli: experiments using chromosomal and plasmid-borne lacZ fusions. Mol Microbiol 3: 851-859.
    • (1989) Mol Microbiol , vol.3 , pp. 851-859
    • Gerstel, B.1    McCarthy, J.2
  • 22
    • 0024095523 scopus 로고
    • Translational coupling between the ilvD and ilvA genes of Escherichia coli
    • Harms, E., Higgins, E., Chen, J., and Umbarger, H. (1988) Translational coupling between the ilvD and ilvA genes of Escherichia coli. J Bacteriol 170: 4798-4807.
    • (1988) J Bacteriol , vol.170 , pp. 4798-4807
    • Harms, E.1    Higgins, E.2    Chen, J.3    Umbarger, H.4
  • 23
    • 0016153699 scopus 로고
    • Assembly mapping of 30S ribosomal proteins from Escherichia coli. Further studies
    • Held, W., Ballou, B., Mizushima, S., and Nomura, M. (1974) Assembly mapping of 30S ribosomal proteins from Escherichia coli. Further studies. J Biol Chem 249: 3103-3111.
    • (1974) J Biol Chem , vol.249 , pp. 3103-3111
    • Held, W.1    Ballou, B.2    Mizushima, S.3    Nomura, M.4
  • 24
    • 0025896985 scopus 로고
    • Translational coupling varying in efficiency between different pairs of genes in the central region of the atp operon of Escherichia coli
    • Hellmuth, K., Rex, G., Surin, B., Zinck, R., and McCarthy, J. (1991) Translational coupling varying in efficiency between different pairs of genes in the central region of the atp operon of Escherichia coli. Mol Microbiol 5: 813-824.
    • (1991) Mol Microbiol , vol.5 , pp. 813-824
    • Hellmuth, K.1    Rex, G.2    Surin, B.3    Zinck, R.4    McCarthy, J.5
  • 25
    • 0023664556 scopus 로고
    • Incorporation of six additional proteins to complete the assembly map of the 50S subunit from Escherichia coli ribosomes
    • Herold, M., and Nierhaus, K. (1987) Incorporation of six additional proteins to complete the assembly map of the 50S subunit from Escherichia coli ribosomes. J Biol Chem 262: 8826-8833.
    • (1987) J Biol Chem , vol.262 , pp. 8826-8833
    • Herold, M.1    Nierhaus, K.2
  • 26
    • 0742322957 scopus 로고    scopus 로고
    • Mapping structural differences between 30S ribosomal subunit assembly intermediates
    • Holmes, K., and Culver, G. (2004) Mapping structural differences between 30S ribosomal subunit assembly intermediates. Nat Struct Mol Biol 11: 179-186.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 179-186
    • Holmes, K.1    Culver, G.2
  • 27
    • 59749098664 scopus 로고
    • Incomplete ribosomes produced in chloramphenicol- and puromycin-inhibited Escherichia coli
    • Hosokawa, K., and Nomura, M. (1965) Incomplete ribosomes produced in chloramphenicol- and puromycin-inhibited Escherichia coli. J Mol Biol 12: 225-241.
    • (1965) J Mol Biol , vol.12 , pp. 225-241
    • Hosokawa, K.1    Nomura, M.2
  • 29
    • 34548728025 scopus 로고    scopus 로고
    • Ribosome biogenesis and the translation process in Escherichia coli
    • Kaczanowska, M., and Ryden-Aulin, M. (2007) Ribosome biogenesis and the translation process in Escherichia coli. Microbiol Mol Biol Rev 71: 477-494.
    • (2007) Microbiol Mol Biol Rev , vol.71 , pp. 477-494
    • Kaczanowska, M.1    Ryden-Aulin, M.2
  • 30
    • 0016607629 scopus 로고
    • Intermediates and time kinetics of the in vivo assembly of Escherichia coli ribosomes
    • Lindahl, L. (1975) Intermediates and time kinetics of the in vivo assembly of Escherichia coli ribosomes. J Mol Biol 92: 15-37.
    • (1975) J Mol Biol , vol.92 , pp. 15-37
    • Lindahl, L.1
  • 31
    • 0024401949 scopus 로고
    • Translational coupling in the threonine operon of Escherichia coli K-12
    • Little, S., Hyde, S., Campbell, C., Lilley, R., and Robinson, M. (1989) Translational coupling in the threonine operon of Escherichia coli K-12. J Bacteriol 171: 3518-3522.
    • (1989) J Bacteriol , vol.171 , pp. 3518-3522
    • Little, S.1    Hyde, S.2    Campbell, C.3    Lilley, R.4    Robinson, M.5
  • 32
    • 0029982204 scopus 로고    scopus 로고
    • Ribosome regulation by the nascent peptide
    • Lovett, P., and Rogers, E. (1996) Ribosome regulation by the nascent peptide. Microbiol Rev 60: 366-385.
    • (1996) Microbiol Rev , vol.60 , pp. 366-385
    • Lovett, P.1    Rogers, E.2
  • 33
    • 11144238888 scopus 로고    scopus 로고
    • Kinetics of macrolide action: the josamycin and erythromycin cases
    • Lovmar, M., Tenson, T., and Ehrenberg, M. (2004) Kinetics of macrolide action: the josamycin and erythromycin cases. J Biol Chem 279: 53506-53515.
    • (2004) J Biol Chem , vol.279 , pp. 53506-53515
    • Lovmar, M.1    Tenson, T.2    Ehrenberg, M.3
  • 34
    • 0029035632 scopus 로고
    • Characterization of three genes in the dam-containing operon of Escherichia coli
    • Lyngstadaas, A., Lbner-Olesen, A., and Boye, E. (1995) Characterization of three genes in the dam-containing operon of Escherichia coli. Mol Gen Genet 247: 546-554.
    • (1995) Mol Gen Genet , vol.247 , pp. 546-554
    • Lyngstadaas, A.1    Lbner-Olesen, A.2    Boye, E.3
  • 35
    • 0024094562 scopus 로고
    • Feedback regulation of the spc operon in Escherichia coli: translational coupling and mRNA processing
    • Mattheakis, L., and Nomura, M. (1988) Feedback regulation of the spc operon in Escherichia coli: translational coupling and mRNA processing. J Bacteriol 170: 4484-4492.
    • (1988) J Bacteriol , vol.170 , pp. 4484-4492
    • Mattheakis, L.1    Nomura, M.2
  • 36
    • 0024509153 scopus 로고
    • Retroregulation of the synthesis of ribosomal proteins L14 and L24 by feedback repressor S8 in Escherichia coli
    • Mattheakis, L., Vu, L., Sor, F., and Nomura, M. (1989) Retroregulation of the synthesis of ribosomal proteins L14 and L24 by feedback repressor S8 in Escherichia coli. Proc Natl Acad Sci USA 86: 448-452.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 448-452
    • Mattheakis, L.1    Vu, L.2    Sor, F.3    Nomura, M.4
  • 37
    • 2442702832 scopus 로고    scopus 로고
    • The structure of a ribosomal protein S8/spc operon mRNA complex
    • Merianos, H., Wang, J., and Moore, P. (2004) The structure of a ribosomal protein S8/spc operon mRNA complex. RNA 10: 954-964.
    • (2004) RNA , vol.10 , pp. 954-964
    • Merianos, H.1    Wang, J.2    Moore, P.3
  • 38
    • 0014219393 scopus 로고
    • Ribosome-catalysed reaction of puromycin with a formylmethionine-containing oligonucleotide
    • Monro, R., and Marcker, K. (1967) Ribosome-catalysed reaction of puromycin with a formylmethionine-containing oligonucleotide. J Mol Biol 25: 347-350.
    • (1967) J Mol Biol , vol.25 , pp. 347-350
    • Monro, R.1    Marcker, K.2
  • 39
    • 78049406997 scopus 로고    scopus 로고
    • Visualizing ribosome biogenesis: parallel assembly pathways for the 30S subunit
    • Mulder, A., Yoshioka, C., Beck, A., Bunner, A., Milligan, R., Potter, C., etal. (2010) Visualizing ribosome biogenesis: parallel assembly pathways for the 30S subunit. Science 330: 673-677.
    • (2010) Science , vol.330 , pp. 673-677
    • Mulder, A.1    Yoshioka, C.2    Beck, A.3    Bunner, A.4    Milligan, R.5    Potter, C.6
  • 40
    • 0025912715 scopus 로고
    • The assembly of prokaryotic ribosomes
    • Nierhaus, K. (1991) The assembly of prokaryotic ribosomes. Biochimie 73: 739-755.
    • (1991) Biochimie , vol.73 , pp. 739-755
    • Nierhaus, K.1
  • 41
    • 59749101203 scopus 로고
    • Biosynthesis of ribosomes: fate of chloraphenicol particles and of pulse-labeled RNA in Escherichia coli
    • Nomura, M., and Hosokawa, K. (1965) Biosynthesis of ribosomes: fate of chloraphenicol particles and of pulse-labeled RNA in Escherichia coli. J Mol Biol 12: 242-265.
    • (1965) J Mol Biol , vol.12 , pp. 242-265
    • Nomura, M.1    Hosokawa, K.2
  • 42
    • 0021155247 scopus 로고
    • Regulation of the synthesis of ribosomes and ribosomal components
    • Nomura, M., Gourse, R., and Baughman, G. (1984) Regulation of the synthesis of ribosomes and ribosomal components. Annu Rev Biochem 53: 75-117.
    • (1984) Annu Rev Biochem , vol.53 , pp. 75-117
    • Nomura, M.1    Gourse, R.2    Baughman, G.3
  • 43
    • 0008146940 scopus 로고
    • Initiator proteins for the assembly of the 50S subunit from Escherichia coli ribosomes
    • Nowotny, V., and Nierhaus, K. (1982) Initiator proteins for the assembly of the 50S subunit from Escherichia coli ribosomes. Proc Natl Acad Sci USA 79: 7238-7242.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 7238-7242
    • Nowotny, V.1    Nierhaus, K.2
  • 44
    • 0023688660 scopus 로고
    • Assembly of the 30S subunit from Escherichia coli ribosomes occurs via two assembly domains which are initiated by S4 and S7
    • Nowotny, V., and Nierhaus, K. (1988) Assembly of the 30S subunit from Escherichia coli ribosomes occurs via two assembly domains which are initiated by S4 and S7. Biochemistry 27: 7051-7055.
    • (1988) Biochemistry , vol.27 , pp. 7051-7055
    • Nowotny, V.1    Nierhaus, K.2
  • 45
    • 29244448703 scopus 로고    scopus 로고
    • Parts per million mass accuracy on an Orbitrap mass spectrometer via lock mass injection into a C-trap
    • Olsen, J., de Godoy, L., Li, G., Macek, B., Mortensen, P., Pesch, R., etal. (2005) Parts per million mass accuracy on an Orbitrap mass spectrometer via lock mass injection into a C-trap. Mol Cell Proteomics 4: 2010-2021.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 2010-2021
    • Olsen, J.1    de Godoy, L.2    Li, G.3    Macek, B.4    Mortensen, P.5    Pesch, R.6
  • 46
    • 47249094203 scopus 로고    scopus 로고
    • Ribosome assembly in Escherichia coli strains lacking the RNA helicase DeaD/CsdA or DbpA
    • Peil, L., Virumäe, K., and Remme, J. (2008) Ribosome assembly in Escherichia coli strains lacking the RNA helicase DeaD/CsdA or DbpA. FEBS J 275: 3772-3782.
    • (2008) FEBS J , vol.275 , pp. 3772-3782
    • Peil, L.1    Virumäe, K.2    Remme, J.3
  • 47
    • 0029081148 scopus 로고
    • Lipid biosynthetic genes and a ribosomal protein gene are cotranscribed
    • Podkovyrov, S., and Larson, T. (1995) Lipid biosynthetic genes and a ribosomal protein gene are cotranscribed. FEBS Lett 368: 429-431.
    • (1995) FEBS Lett , vol.368 , pp. 429-431
    • Podkovyrov, S.1    Larson, T.2
  • 49
    • 60349100340 scopus 로고    scopus 로고
    • Programmed drug-dependent ribosome stalling
    • Ramu, H., Mankin, A., and Vazquez-Laslop, N. (2009) Programmed drug-dependent ribosome stalling. Mol Microbiol 71: 811-824.
    • (2009) Mol Microbiol , vol.71 , pp. 811-824
    • Ramu, H.1    Mankin, A.2    Vazquez-Laslop, N.3
  • 50
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • Rappsilber, J., Mann, M., and Ishihama, Y. (2007) Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat Protoc 2: 1896-1906.
    • (2007) Nat Protoc , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 51
    • 0028306907 scopus 로고
    • The mechanism of translational coupling in Escherichia coli. Higher order structure in the atpHA mRNA acts as a conformational switch regulating the access of de novo initiating ribosomes
    • Rex, G., Surin, B., Besse, G., Schneppe, B., and McCarthy, J. (1994) The mechanism of translational coupling in Escherichia coli. Higher order structure in the atpHA mRNA acts as a conformational switch regulating the access of de novo initiating ribosomes. J Biol Chem 269: 18118-18127.
    • (1994) J Biol Chem , vol.269 , pp. 18118-18127
    • Rex, G.1    Surin, B.2    Besse, G.3    Schneppe, B.4    McCarthy, J.5
  • 53
    • 0035950132 scopus 로고    scopus 로고
    • Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria
    • Schlünzen, F., Zarivach, R., Harms, J., Bashan, A., Tocilj, A., Albrecht, R., etal. (2001) Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria. Nature 413: 814-821.
    • (2001) Nature , vol.413 , pp. 814-821
    • Schlünzen, F.1    Zarivach, R.2    Harms, J.3    Bashan, A.4    Tocilj, A.5    Albrecht, R.6
  • 54
    • 0020371936 scopus 로고
    • Translational coupling at an intercistronic boundary of the Escherichia coli galactose operon
    • Schümperli, D., McKenney, K., Sobieski, D., and Rosenberg, M. (1982) Translational coupling at an intercistronic boundary of the Escherichia coli galactose operon. Cell 30: 865-871.
    • (1982) Cell , vol.30 , pp. 865-871
    • Schümperli, D.1    McKenney, K.2    Sobieski, D.3    Rosenberg, M.4
  • 55
    • 59449085150 scopus 로고    scopus 로고
    • Global analysis of cellular protein translation by pulsed SILAC
    • Schwanhauser, B., Gossen, M., Dittmar, G., and Selbach, M. (2009) Global analysis of cellular protein translation by pulsed SILAC. Proteomics 9: 205-209.
    • (2009) Proteomics , vol.9 , pp. 205-209
    • Schwanhauser, B.1    Gossen, M.2    Dittmar, G.3    Selbach, M.4
  • 56
    • 77957291981 scopus 로고    scopus 로고
    • Subribosomal particle analysis reveals the stages of bacterial ribosome assembly at which rRNA nucleotides are modified
    • Siibak, T., and Remme, J. (2010) Subribosomal particle analysis reveals the stages of bacterial ribosome assembly at which rRNA nucleotides are modified. RNA 16: 2023-2032.
    • (2010) RNA , vol.16 , pp. 2023-2032
    • Siibak, T.1    Remme, J.2
  • 57
    • 59749083182 scopus 로고    scopus 로고
    • Erythromycin- and chloramphenicol-induced ribosomal assembly defects are secondary effects of protein synthesis inhibition
    • Siibak, T., Peil, L., Xiong, L., Mankin, A., Remme, J., and Tenson, T. (2009) Erythromycin- and chloramphenicol-induced ribosomal assembly defects are secondary effects of protein synthesis inhibition. Antimicrob Agents Chemother 53: 563-571.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 563-571
    • Siibak, T.1    Peil, L.2    Xiong, L.3    Mankin, A.4    Remme, J.5    Tenson, T.6
  • 58
    • 46049106143 scopus 로고    scopus 로고
    • Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli
    • Sperandeo, P., Lau, F., Carpentieri, A., De Castro, C., Molinaro, A., Deho, G., etal. (2008) Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli. J Bacteriol 190: 4460-4469.
    • (2008) J Bacteriol , vol.190 , pp. 4460-4469
    • Sperandeo, P.1    Lau, F.2    Carpentieri, A.3    De Castro, C.4    Molinaro, A.5    Deho, G.6
  • 59
    • 77954185197 scopus 로고    scopus 로고
    • Interplay between the ribosomal tunnel, nascent chain, and macrolides influences drug inhibition
    • Starosta, A., Karpenko, V., Shishkina, A., Mikolajka, A., Sumbatyan, N., Schluenzen, F., etal. (2010) Interplay between the ribosomal tunnel, nascent chain, and macrolides influences drug inhibition. Chem Biol 17: 504-514.
    • (2010) Chem Biol , vol.17 , pp. 504-514
    • Starosta, A.1    Karpenko, V.2    Shishkina, A.3    Mikolajka, A.4    Sumbatyan, N.5    Schluenzen, F.6
  • 60
    • 77957754593 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of ribosome assembly and turnover in vivo
    • Sykes, M., Shajani, Z., Sperling, E., Beck, A., and Williamson, J. (2010) Quantitative proteomic analysis of ribosome assembly and turnover in vivo. J Mol Biol 403: 331-345.
    • (2010) J Mol Biol , vol.403 , pp. 331-345
    • Sykes, M.1    Shajani, Z.2    Sperling, E.3    Beck, A.4    Williamson, J.5
  • 61
    • 28444479853 scopus 로고    scopus 로고
    • An assembly landscape for the 30S ribosomal subunit
    • Talkington, M., Siuzdak, G., and Williamson, J. (2005) An assembly landscape for the 30S ribosomal subunit. Nature 438: 628-632.
    • (2005) Nature , vol.438 , pp. 628-632
    • Talkington, M.1    Siuzdak, G.2    Williamson, J.3
  • 62
    • 0037040406 scopus 로고    scopus 로고
    • Regulatory nascent peptides in the ribosomal tunnel
    • Tenson, T., and Ehrenberg, M. (2002) Regulatory nascent peptides in the ribosomal tunnel. Cell 108: 591-594.
    • (2002) Cell , vol.108 , pp. 591-594
    • Tenson, T.1    Ehrenberg, M.2
  • 63
    • 0038690158 scopus 로고    scopus 로고
    • The mechanism of action of macrolides, lincosamides and streptogramin B reveals the nascent peptide exit path in the ribosome
    • Tenson, T., Lovmar, M., and Ehrenberg, M. (2003) The mechanism of action of macrolides, lincosamides and streptogramin B reveals the nascent peptide exit path in the ribosome. J Mol Biol 330: 1005-1014.
    • (2003) J Mol Biol , vol.330 , pp. 1005-1014
    • Tenson, T.1    Lovmar, M.2    Ehrenberg, M.3
  • 64
    • 0014760541 scopus 로고
    • Peptide chain termination. VII. The ribosomal and release factor requirements for peptide release
    • Tompkins, R., Scolnick, E., and Caskey, C. (1970) Peptide chain termination. VII. The ribosomal and release factor requirements for peptide release. Proc Natl Acad Sci USA 65: 702-708.
    • (1970) Proc Natl Acad Sci USA , vol.65 , pp. 702-708
    • Tompkins, R.1    Scolnick, E.2    Caskey, C.3
  • 65
    • 0035005634 scopus 로고    scopus 로고
    • Erythromycin inhibition of 50S ribosomal subunit formation in Escherichia coli cells
    • Usary, J., and Champney, W. (2001) Erythromycin inhibition of 50S ribosomal subunit formation in Escherichia coli cells. Mol Microbiol 40: 951-962.
    • (2001) Mol Microbiol , vol.40 , pp. 951-962
    • Usary, J.1    Champney, W.2
  • 66
    • 0023684123 scopus 로고
    • Non-autogenous control of ribosomal protein synthesis from the trmD operon in Escherichia coli
    • Wikström, P., Byström, A., and Björk, G. (1988) Non-autogenous control of ribosomal protein synthesis from the trmD operon in Escherichia coli. J Mol Biol 203: 141-152.
    • (1988) J Mol Biol , vol.203 , pp. 141-152
    • Wikström, P.1    Byström, A.2    Björk, G.3
  • 67
    • 70450233600 scopus 로고    scopus 로고
    • The A-Z of bacterial translation inhibitors
    • Wilson, D. (2009) The A-Z of bacterial translation inhibitors. Crit Rev Biochem Mol Biol 44: 393-433.
    • (2009) Crit Rev Biochem Mol Biol , vol.44 , pp. 393-433
    • Wilson, D.1
  • 68
    • 0025339204 scopus 로고
    • Co-overproduction and localization of the Escherichia coli motility proteins motA and motB
    • Wilson, M., and Macnab, R. (1990) Co-overproduction and localization of the Escherichia coli motility proteins motA and motB. J Bacteriol 172: 3932-3939.
    • (1990) J Bacteriol , vol.172 , pp. 3932-3939
    • Wilson, M.1    Macnab, R.2
  • 69
    • 0018897011 scopus 로고
    • In vitro expression of Escherichia coli ribosomal protein genes: autogenous inhibition of translation
    • Yates, J., Arfsten, A., and Nomura, M. (1980) In vitro expression of Escherichia coli ribosomal protein genes: autogenous inhibition of translation. Proc Natl Acad Sci USA 77: 1837-1841.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1837-1841
    • Yates, J.1    Arfsten, A.2    Nomura, M.3
  • 70
    • 0019813824 scopus 로고
    • E. coli ribosomal protein L10 inhibits translation of L10 and L7/L12 mRNAs by acting at a single site
    • Yates, J., Dean, D., Strycharz, W., and Nomura, M. (1981) E. coli ribosomal protein L10 inhibits translation of L10 and L7/L12 mRNAs by acting at a single site. Nature 294: 190-192.
    • (1981) Nature , vol.294 , pp. 190-192
    • Yates, J.1    Dean, D.2    Strycharz, W.3    Nomura, M.4
  • 71
    • 0028251157 scopus 로고
    • Diverse mechanisms for regulating ribosomal protein synthesis in Escherichia coli
    • Zengel, J., and Lindahl, L. (1994) Diverse mechanisms for regulating ribosomal protein synthesis in Escherichia coli. Prog Nucleic Acid Res Mol Biol 47: 331-370.
    • (1994) Prog Nucleic Acid Res Mol Biol , vol.47 , pp. 331-370
    • Zengel, J.1    Lindahl, L.2
  • 72
    • 0031801906 scopus 로고    scopus 로고
    • Transcriptional analysis of essential genes of the Escherichia coli fatty acid biosynthesis gene cluster by functional replacement with the analogous Salmonella typhimurium gene cluster
    • Zhang, Y., and Cronan, J.J. (1998) Transcriptional analysis of essential genes of the Escherichia coli fatty acid biosynthesis gene cluster by functional replacement with the analogous Salmonella typhimurium gene cluster. J Bacteriol 180: 3295-3303.
    • (1998) J Bacteriol , vol.180 , pp. 3295-3303
    • Zhang, Y.1    Cronan, J.J.2
  • 73
    • 77950344767 scopus 로고    scopus 로고
    • Promoter and regulon analysis of nitrogen assimilation factor, sigma54, reveal alternative strategy for E. coli MG1655 flagellar biosynthesis
    • Zhao, K., Liu, M., and Burgess, R. (2010) Promoter and regulon analysis of nitrogen assimilation factor, sigma54, reveal alternative strategy for E. coli MG1655 flagellar biosynthesis. Nucleic Acids Res 38: 1273-1283.
    • (2010) Nucleic Acids Res , vol.38 , pp. 1273-1283
    • Zhao, K.1    Liu, M.2    Burgess, R.3


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