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Volumn 71, Issue 3, 2007, Pages 477-494

Ribosome biogenesis and the translation process in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; GUANOSINE TRIPHOSPHATASE; METAL ION; RIBOSOME PROTEIN; RIBOSOME RNA; RNA; RNA HELICASE;

EID: 34548728025     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/MMBR.00013-07     Document Type: Review
Times cited : (305)

References (221)
  • 1
    • 22544466402 scopus 로고    scopus 로고
    • Protein-independent folding pathway of the 16S rRNA 5′ domain
    • Adilakshimi, T., P. Ramaswamy, and S. A. Woodson. 2005. Protein-independent folding pathway of the 16S rRNA 5′ domain. J. Mol. Biol. 351: 508-519.
    • (2005) J. Mol. Biol , vol.351 , pp. 508-519
    • Adilakshimi, T.1    Ramaswamy, P.2    Woodson, S.A.3
  • 2
    • 0032967391 scopus 로고    scopus 로고
    • Conformational variability in Escherichia coli 70S ribosome as revealed by 3D cryo-electron tomography
    • Agrawal, R. K., R. K. Lata, and J. Frank. 1999. Conformational variability in Escherichia coli 70S ribosome as revealed by 3D cryo-electron tomography. Int. J. Biochem. Cell Biol. 31:243-254.
    • (1999) Int. J. Biochem. Cell Biol , vol.31 , pp. 243-254
    • Agrawal, R.K.1    Lata, R.K.2    Frank, J.3
  • 3
    • 0027362954 scopus 로고
    • Mutant DnaK chaperones cause ribosome assembly defects in Escherichia coli
    • Alix, J. H., and M. F. Guerin. 1993. Mutant DnaK chaperones cause ribosome assembly defects in Escherichia coli. Proc. Natl. Acad. Sci. USA 90:9725-9729.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9725-9729
    • Alix, J.H.1    Guerin, M.F.2
  • 4
    • 0018781772 scopus 로고
    • Properties of ribosomes and RNA synthesized by Escherichia coli grown in the presence of ethionine. V. Methylation dependence of the assembly of E. coli 50S ribosomal subunits
    • Alix, J. H., D. Hayes, and K. N. Nierhaus. 1979. Properties of ribosomes and RNA synthesized by Escherichia coli grown in the presence of ethionine. V. Methylation dependence of the assembly of E. coli 50S ribosomal subunits. J. Mol. Biol. 127:375-395.
    • (1979) J. Mol. Biol , vol.127 , pp. 375-395
    • Alix, J.H.1    Hayes, D.2    Nierhaus, K.N.3
  • 5
    • 0038382885 scopus 로고    scopus 로고
    • DnaK-facilitated ribosome assembly in Escherichia coli revisited
    • Alix, J. H., and K. N. Nierhaus. 2003. DnaK-facilitated ribosome assembly in Escherichia coli revisited. RNA 9:787-793.
    • (2003) RNA , vol.9 , pp. 787-793
    • Alix, J.H.1    Nierhaus, K.N.2
  • 6
    • 2542487488 scopus 로고    scopus 로고
    • Functional interaction between RNase III and the Escherichia coli ribosome
    • Allas, Ü., A. Liiv, and J. Remme. 2003. Functional interaction between RNase III and the Escherichia coli ribosome. BMC Mol. Biol. 4:8.
    • (2003) BMC Mol. Biol , vol.4 , pp. 8
    • Allas, U.1    Liiv, A.2    Remme, J.3
  • 7
    • 0033541674 scopus 로고    scopus 로고
    • Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry
    • Arnold, R. J., and J. P. Reilly. 1999. Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry. Anal. Biochem. 269:105-112.
    • (1999) Anal. Biochem , vol.269 , pp. 105-112
    • Arnold, R.J.1    Reilly, J.P.2
  • 8
    • 0346660000 scopus 로고
    • Secondary σ factor controls transcription of flagellar and chemotaxis genes in Escherichia coli
    • Arnosti, D. N., and M. J. Chamberlin. 1989. Secondary σ factor controls transcription of flagellar and chemotaxis genes in Escherichia coli. Proc. Natl. Acad. Sci. USA 86:830-934.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 830-934
    • Arnosti, D.N.1    Chamberlin, M.J.2
  • 11
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban, N., P. Nissen, J. Hansen, P. B. Moore, and T. A. Steitz. 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
  • 12
    • 1842506160 scopus 로고    scopus 로고
    • Regulation at complex bacterial promoters: How bacteria use different promoter organizations to produce different regulatory outcomes
    • Barnard, A., A. Wolfe, and S. J. W. Busby. 2004. Regulation at complex bacterial promoters: how bacteria use different promoter organizations to produce different regulatory outcomes. Curr. Opin. Microbiol. 7:102-108.
    • (2004) Curr. Opin. Microbiol , vol.7 , pp. 102-108
    • Barnard, A.1    Wolfe, A.2    Busby, S.J.W.3
  • 13
    • 33344476204 scopus 로고    scopus 로고
    • Identification and characterization of RsmE, the founding member of a new RNA base methyltransferase family
    • Basturea, G. N., K. E. Rudd, and M. P. Deutscher. 2006. Identification and characterization of RsmE, the founding member of a new RNA base methyltransferase family. RNA 12:426-434.
    • (2006) RNA , vol.12 , pp. 426-434
    • Basturea, G.N.1    Rudd, K.E.2    Deutscher, M.P.3
  • 14
    • 0345504147 scopus 로고    scopus 로고
    • Characterization of transient RNA-RNA interactions important for the facilitated structure formation of bacterial ribosomal 16S RNA
    • Besancon, W., and R. Wagner. 1999. Characterization of transient RNA-RNA interactions important for the facilitated structure formation of bacterial ribosomal 16S RNA. Nucleic Acids Res. 27:4353-4362.
    • (1999) Nucleic Acids Res , vol.27 , pp. 4353-4362
    • Besancon, W.1    Wagner, R.2
  • 16
    • 0017817813 scopus 로고
    • RNase III cleavage of Escherichia coli rRNA precursors: Fragment release and dependence on salt concentration
    • Birenbaum, M., D. Schlessinger, and S. Hashimoto. 1978. RNase III cleavage of Escherichia coli rRNA precursors: fragment release and dependence on salt concentration. Biochemistry 17:298-306.
    • (1978) Biochemistry , vol.17 , pp. 298-306
    • Birenbaum, M.1    Schlessinger, D.2    Hashimoto, S.3
  • 17
    • 0018901271 scopus 로고
    • The ribonuclease III site flanking 23S sequences in the 30S ribosomal precursor RNA of E. coli
    • Bram, R. J., R. A. Young, and J. A. Steitz. 1980. The ribonuclease III site flanking 23S sequences in the 30S ribosomal precursor RNA of E. coli. Cell 19:393-401.
    • (1980) Cell , vol.19 , pp. 393-401
    • Bram, R.J.1    Young, R.A.2    Steitz, J.A.3
  • 18
    • 0000640710 scopus 로고    scopus 로고
    • Modulation of chemical composition and other parameters of the cell by growth rate
    • F. C. Neidhardt ed, 2nd ed. ASM Press, Washington, DC
    • Bremer, H., and P. P. Dennis. 1996. Modulation of chemical composition and other parameters of the cell by growth rate, p. 1553-1569. In F. C. Neidhardt (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, DC.
    • (1996) Escherichia coli and Salmonella: Cellular and molecular biology , pp. 1553-1569
    • Bremer, H.1    Dennis, P.P.2
  • 19
    • 0031953140 scopus 로고    scopus 로고
    • Cell cycle arrest in Era GTPase mutants: A potential growth rate-regulated checkpoint in Escherichia coli
    • Britton, A. R., B. S. Powell, S. Dasgupta, Q. Sun, P. Margolin, J. R. Lupski, and D. L. Court. 1998. Cell cycle arrest in Era GTPase mutants: a potential growth rate-regulated checkpoint in Escherichia coli. Mol. Microbiol. 27: 739-750.
    • (1998) Mol. Microbiol , vol.27 , pp. 739-750
    • Britton, A.R.1    Powell, B.S.2    Dasgupta, S.3    Sun, Q.4    Margolin, P.5    Lupski, J.R.6    Court, D.L.7
  • 20
    • 0036303417 scopus 로고    scopus 로고
    • Crystal structure of the 30 S ribosomal subunit from Thermus thermophilus: Structure of the proteins and their interactions with 16S RNA
    • Brodersen, D. E., W. M. Clemons, A. P. Carter, B. T. Wimberly, and V. Ramakrishnan. 2002. Crystal structure of the 30 S ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16S RNA. J. Mol. Biol. 316:725-768.
    • (2002) J. Mol. Biol , vol.316 , pp. 725-768
    • Brodersen, D.E.1    Clemons, W.M.2    Carter, A.P.3    Wimberly, B.T.4    Ramakrishnan, V.5
  • 21
    • 0017152588 scopus 로고
    • The primary structure of protein L16 located at the peptidyltransferase center of Escherichia coli ribosomes
    • Brosius, J., and R. Chen. 1976. The primary structure of protein L16 located at the peptidyltransferase center of Escherichia coli ribosomes. FEBS Lett. 68:105-109.
    • (1976) FEBS Lett , vol.68 , pp. 105-109
    • Brosius, J.1    Chen, R.2
  • 22
    • 32044468906 scopus 로고    scopus 로고
    • Conserved P-loop GTPases of unknown function in bacteria: An emerging and vital ensemble in bacterial physiology
    • Brown, E. D. 2005. Conserved P-loop GTPases of unknown function in bacteria: an emerging and vital ensemble in bacterial physiology. Biochem. Cell Biol. 83:738-746.
    • (2005) Biochem. Cell Biol , vol.83 , pp. 738-746
    • Brown, E.D.1
  • 23
    • 0015955993 scopus 로고
    • Genetic analysis of cold-sensitive ribosome maturation mutants of Escherichia coli
    • Bryant, R. E., and P. S. Sypherd. 1974. Genetic analysis of cold-sensitive ribosome maturation mutants of Escherichia coli. J. Bacteriol. 117:1082-1092.
    • (1974) J. Bacteriol , vol.117 , pp. 1082-1092
    • Bryant, R.E.1    Sypherd, P.S.2
  • 25
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B., and A. L. Horwich. 1998. The Hsp70 and Hsp60 chaperone machines. Cell 92:351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 26
    • 0034811078 scopus 로고    scopus 로고
    • Characterization of mutations in the metY-nusA-infB operon that suppress the slow growth of a ΔrimM mutant
    • Bylund, G. O., J. M. Lövgren, and P. M. Wikström. 2001. Characterization of mutations in the metY-nusA-infB operon that suppress the slow growth of a ΔrimM mutant. J. Bacteriol. 183:6095-6106.
    • (2001) J. Bacteriol , vol.183 , pp. 6095-6106
    • Bylund, G.O.1    Lövgren, J.M.2    Wikström, P.M.3
  • 27
    • 0031973622 scopus 로고    scopus 로고
    • RimM and RbfA are essential for efficient processing of 16S rRNA in Escherichia coli
    • Bylund, G. O., L. C. Wipemo, L. A. C. Lundberg, and P. M. Wikström. 1998. RimM and RbfA are essential for efficient processing of 16S rRNA in Escherichia coli. J. Bacteriol. 180:73-82.
    • (1998) J. Bacteriol , vol.180 , pp. 73-82
    • Bylund, G.O.1    Wipemo, L.C.2    Lundberg, L.A.C.3    Wikström, P.M.4
  • 29
    • 0034909325 scopus 로고    scopus 로고
    • Evolution of a molecular switch: Universal bacterial GTPases regulate ribosome function
    • Caldon, C. E., P. Yoong, and P. E. March. 2001. Evolution of a molecular switch: universal bacterial GTPases regulate ribosome function. Mol. Microbiol. 41:289-297.
    • (2001) Mol. Microbiol , vol.41 , pp. 289-297
    • Caldon, C.E.1    Yoong, P.2    March, P.E.3
  • 30
    • 0034699519 scopus 로고    scopus 로고
    • Functional insights from the structure of the ribosomal subunit and its interactions with antibiotics
    • Carter, A. P., W. M. Clemons, D. E. Brodersen, R. J. Morgan-Warren, B. T. Wimberly, and V. Ramakrishnan. 2000. Functional insights from the structure of the ribosomal subunit and its interactions with antibiotics. Nature 407:340-348.
    • (2000) Nature , vol.407 , pp. 340-348
    • Carter, A.P.1    Clemons, W.M.2    Brodersen, D.E.3    Morgan-Warren, R.J.4    Wimberly, B.T.5    Ramakrishnan, V.6
  • 32
    • 0032881809 scopus 로고    scopus 로고
    • X-ray crystal structures of 70S ribosome functional complexes
    • Cate, J. H., M. M. Yusupov, G. Z. Yusupova, T. N. Earnest, and H. F. Noller. 1999. X-ray crystal structures of 70S ribosome functional complexes. Science 285:2095-2104.
    • (1999) Science , vol.285 , pp. 2095-2104
    • Cate, J.H.1    Yusupov, M.M.2    Yusupova, G.Z.3    Earnest, T.N.4    Noller, H.F.5
  • 34
    • 2542557396 scopus 로고    scopus 로고
    • CsdA, a cold-shock RNA helicase from Escherichia coli, is involved in the biogenesis of the biogenesis of 50S ribosomal subunit
    • Charollais, J., M. Dreyfus, and I. Iost. 2004. CsdA, a cold-shock RNA helicase from Escherichia coli, is involved in the biogenesis of the biogenesis of 50S ribosomal subunit. Nucleic Acids Res. 323:2751-2759.
    • (2004) Nucleic Acids Res , vol.323 , pp. 2751-2759
    • Charollais, J.1    Dreyfus, M.2    Iost, I.3
  • 35
    • 0038120874 scopus 로고    scopus 로고
    • The DEAD-box RNA helicase SrmB is involved in the assembly of 50S ribosomal subunits in Escherichia coli
    • Charollais, J., D. Pflieger, J. Vinh, M. Dreyfus, and I. Iost. 2003. The DEAD-box RNA helicase SrmB is involved in the assembly of 50S ribosomal subunits in Escherichia coli. Mol. Microbiol. 48:1253-1265.
    • (2003) Mol. Microbiol , vol.48 , pp. 1253-1265
    • Charollais, J.1    Pflieger, D.2    Vinh, J.3    Dreyfus, M.4    Iost, I.5
  • 36
    • 0035075387 scopus 로고    scopus 로고
    • Revisiting the stringent response, ppGpp and starvation signaling
    • Chatterji, D., and A. K. Ojha. 2001. Revisiting the stringent response, ppGpp and starvation signaling. Curr. Opin. Microbiol. 4:160-165.
    • (2001) Curr. Opin. Microbiol , vol.4 , pp. 160-165
    • Chatterji, D.1    Ojha, A.K.2
  • 37
    • 0017598292 scopus 로고
    • Occurrence of methylated amino acids as N-termini of proteins from Escherichia coli ribosomes
    • Chen, R., J. Brosius, B. Wittmann-Liebold, and W. Schafer. 1977. Occurrence of methylated amino acids as N-termini of proteins from Escherichia coli ribosomes. J. Mol. Biol. 111:173-181.
    • (1977) J. Mol. Biol , vol.111 , pp. 173-181
    • Chen, R.1    Brosius, J.2    Wittmann-Liebold, B.3    Schafer, W.4
  • 38
    • 0038652098 scopus 로고    scopus 로고
    • Quality control of ribosomal RNA mediated by polynucleotide phosphorylase and RNase R
    • Cheng, Z.-F., and M. P. Deutscher. 2003. Quality control of ribosomal RNA mediated by polynucleotide phosphorylase and RNase R. Proc. Natl. Acad. Sci. USA 100:6388-6393.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6388-6393
    • Cheng, Z.-F.1    Deutscher, M.P.2
  • 39
    • 0023646046 scopus 로고
    • Feedback regulation of rRNA synthesis in Escherichia coli. Requirement for initiation factor IF2
    • Cole, J. R., C. L. Olsson, J. W. B. Hershey, M. Grunberg-Manago, and M. Nomura. 1987. Feedback regulation of rRNA synthesis in Escherichia coli. Requirement for initiation factor IF2. J. Mol. Biol. 198:383-392.
    • (1987) J. Mol. Biol , vol.198 , pp. 383-392
    • Cole, J.R.1    Olsson, C.L.2    Hershey, J.W.B.3    Grunberg-Manago, M.4    Nomura, M.5
  • 40
    • 0018286248 scopus 로고
    • Genetics of ribosomal protein methylation in Escherichia coli. III. Map position of two genes, prmA and prmB, governing methylation of proteins L11 and L3
    • Colson, C., J. Lhoest, and C. Urlings. 1979. Genetics of ribosomal protein methylation in Escherichia coli. III. Map position of two genes, prmA and prmB, governing methylation of proteins L11 and L3. Mol. Gen. Genet. 169:245-250.
    • (1979) Mol. Gen. Genet , vol.169 , pp. 245-250
    • Colson, C.1    Lhoest, J.2    Urlings, C.3
  • 41
    • 0027432869 scopus 로고
    • Depletion of functional ribosomal RNA operons in Escherichia coli causes increased expression of the remaining intact copies
    • Condon, C., S. French, C. Squires, and C. L. Squires. 1993. Depletion of functional ribosomal RNA operons in Escherichia coli causes increased expression of the remaining intact copies. EMBO J. 12:4305-4315.
    • (1993) EMBO J , vol.12 , pp. 4305-4315
    • Condon, C.1    French, S.2    Squires, C.3    Squires, C.L.4
  • 42
    • 0029048945 scopus 로고
    • rRNA operon multiplicity in Escherichia coli and the physiological implications of rrn inactivation
    • Condon, C., D. Liveris, C. Squires, I. Schwartz, and C. L. Squires. 1995. rRNA operon multiplicity in Escherichia coli and the physiological implications of rrn inactivation. J. Bacteriol. 177:4152-456.
    • (1995) J. Bacteriol , vol.177 , pp. 4152-4456
    • Condon, C.1    Liveris, D.2    Squires, C.3    Schwartz, I.4    Squires, C.L.5
  • 43
    • 0018571141 scopus 로고
    • In vivo transcriptionally coupled assembly of Escherichia coli ribosomal subunits
    • Cowgill de Navarez, C., and H. W. Schaup. 1979. In vivo transcriptionally coupled assembly of Escherichia coli ribosomal subunits. J. Mol. Biol. 134: 1-22.
    • (1979) J. Mol. Biol , vol.134 , pp. 1-22
    • Cowgill de Navarez, C.1    Schaup, H.W.2
  • 45
    • 0033057324 scopus 로고    scopus 로고
    • Efficient reconstitution of functional Escherichia coli 30S ribosomal subunits from a complete set of recombinant small subunit ribosomal proteins
    • Culver, G. M., and H. F. Noller. 1999. Efficient reconstitution of functional Escherichia coli 30S ribosomal subunits from a complete set of recombinant small subunit ribosomal proteins. RNA 5:832-843.
    • (1999) RNA , vol.5 , pp. 832-843
    • Culver, G.M.1    Noller, H.F.2
  • 46
    • 0018405372 scopus 로고
    • Ribosomal protein modification in Escherichia coli. I. A mutant lacking the N-terminal acetylation of protein S5 exhibits thermosensitivity
    • Cumberlidge, A. G., and K. Isono. 1979. Ribosomal protein modification in Escherichia coli. I. A mutant lacking the N-terminal acetylation of protein S5 exhibits thermosensitivity. J. Mol. Biol. 131:169-189.
    • (1979) J. Mol. Biol , vol.131 , pp. 169-189
    • Cumberlidge, A.G.1    Isono, K.2
  • 47
    • 1342346614 scopus 로고    scopus 로고
    • Studies of the interaction of Escherichia coli YjeQ with the ribosome in vitro
    • Daigle, D. M., and E. D. Brown. 2004. Studies of the interaction of Escherichia coli YjeQ with the ribosome in vitro. J. Bacteriol. 186:1381-1387.
    • (2004) J. Bacteriol , vol.186 , pp. 1381-1387
    • Daigle, D.M.1    Brown, E.D.2
  • 48
    • 0037127209 scopus 로고    scopus 로고
    • Structural basis for H-NS-mediated trapping of RNA polymerase in the open initiation complex at the rrn P1
    • Dame, R. T., C. Wyman, R. Wurm, R. Wagner, and N. Goosen. 2002. Structural basis for H-NS-mediated trapping of RNA polymerase in the open initiation complex at the rrn P1. J. Biol. Chem. 277:2146-2150.
    • (2002) J. Biol. Chem , vol.277 , pp. 2146-2150
    • Dame, R.T.1    Wyman, C.2    Wurm, R.3    Wagner, R.4    Goosen, N.5
  • 49
    • 0028906075 scopus 로고
    • Suppression of a cold-sensitive mutation in 16S rRNA by overexpression of a novel ribosome-binding factor, RbfA
    • Dammel, C. S., and H. F. Noller. 1995. Suppression of a cold-sensitive mutation in 16S rRNA by overexpression of a novel ribosome-binding factor, RbfA. Genes Dev. 9:626-637.
    • (1995) Genes Dev , vol.9 , pp. 626-637
    • Dammel, C.S.1    Noller, H.F.2
  • 50
    • 0032902763 scopus 로고    scopus 로고
    • Isoaspartate in ribosomal protein S11 of Escherichia coli
    • David, C., J. Keener, and D. W. Aswad. 1999. Isoaspartate in ribosomal protein S11 of Escherichia coli. J. Bacteriol. 181:2871-2877.
    • (1999) J. Bacteriol , vol.181 , pp. 2871-2877
    • David, C.1    Keener, J.2    Aswad, D.W.3
  • 51
    • 0036629250 scopus 로고    scopus 로고
    • rRNA modifications and ribosome function
    • Decatur, W. A., and M. J. Fournier. 2002. rRNA modifications and ribosome function. Trends Biochem. Sci. 27:344-351.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 344-351
    • Decatur, W.A.1    Fournier, M.J.2
  • 52
    • 34548788819 scopus 로고    scopus 로고
    • Delano, W. L. 2002. The PyMOL molecular graphics system. http://pymol.sourceforge.net/.
    • (2002)
    • Delano, W.L.1
  • 53
    • 0017033814 scopus 로고
    • Effects of chloramphenicol on the transcriptional activities of ribosomal RNA and ribosomal protein genes in Escherichia coli
    • Dennis, P. 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.P.1
  • 54
    • 10344265937 scopus 로고    scopus 로고
    • Control of rRNA synthesis in Escherichia coli: A systems biology approach
    • Dennis, P. P., M. Ehrenberg, and H. Bremer. 2004. Control of rRNA synthesis in Escherichia coli: a systems biology approach. Microbiol. Mol. Biol. Rev. 68:639-668.
    • (2004) Microbiol. Mol. Biol. Rev , vol.68 , pp. 639-668
    • Dennis, P.P.1    Ehrenberg, M.2    Bremer, H.3
  • 55
    • 33646128243 scopus 로고    scopus 로고
    • The adenosine dimethyltransferase KsgA recognizes a specific conformational state of the 30S ribosomal subunit
    • Desai, P. M., and J. P. Rife. 2006. The adenosine dimethyltransferase KsgA recognizes a specific conformational state of the 30S ribosomal subunit. Arch. Biochem. Biophys. 449:57-63.
    • (2006) Arch. Biochem. Biophys , vol.449 , pp. 57-63
    • Desai, P.M.1    Rife, J.P.2
  • 56
    • 32644435694 scopus 로고    scopus 로고
    • Degradation of RNA in bacteria: Comparison of mRNA and stable RNA
    • Deutscher, M. P. 2006. Degradation of RNA in bacteria: comparison of mRNA and stable RNA. Nucleic Acids Res. 34:659-666.
    • (2006) Nucleic Acids Res , vol.34 , pp. 659-666
    • Deutscher, M.P.1
  • 57
    • 0024726281 scopus 로고
    • Identification of promoter mutants defective in growth-rate-dependent regulation of rRNA transcription in Escherichia coli
    • Dickson, R. R., T. Gaal, H. A. deBoer, P. L. deHaseth, and R. L. Gourse. 1989. Identification of promoter mutants defective in growth-rate-dependent regulation of rRNA transcription in Escherichia coli. J. Bacteriol. 171:4862-4870.
    • (1989) J. Bacteriol , vol.171 , pp. 4862-4870
    • Dickson, R.R.1    Gaal, T.2    deBoer, H.A.3    deHaseth, P.L.4    Gourse, R.L.5
  • 58
    • 19644362046 scopus 로고    scopus 로고
    • Escherichia coli DbpA is a 3′ to 5′ RNA helicase
    • Diges, C. M., and O. C. Uhlenbeck. 2005. Escherichia coli DbpA is a 3′ to 5′ RNA helicase. Biochemistry 44:7903-7911.
    • (2005) Biochemistry , vol.44 , pp. 7903-7911
    • Diges, C.M.1    Uhlenbeck, O.C.2
  • 59
    • 0035476705 scopus 로고    scopus 로고
    • Escherichia coli DbpA is an RNA helicase that requires hairpin 92 of 23S rRNA
    • Diges, C. M., and O. C. Uhlenbeck. 2001. Escherichia coli DbpA is an RNA helicase that requires hairpin 92 of 23S rRNA. EMBO J. 20:5503-5512.
    • (2001) EMBO J , vol.20 , pp. 5503-5512
    • Diges, C.M.1    Uhlenbeck, O.C.2
  • 60
    • 0347595319 scopus 로고    scopus 로고
    • Authentic precursors to ribosomal subunits accumulate in Escherichia coli in the absence of functional DnaK chaperone
    • El Hage, A., and J. H. Alix. 2004. Authentic precursors to ribosomal subunits accumulate in Escherichia coli in the absence of functional DnaK chaperone. Mol. Microbiol. 51:189-201.
    • (2004) Mol. Microbiol , vol.51 , pp. 189-201
    • El Hage, A.1    Alix, J.H.2
  • 61
    • 0035089326 scopus 로고    scopus 로고
    • The chaperonin GroEL and other heat-shock proteins, besides DnaK, participate in ribosome biogenesis in Escherichia coli
    • El Hage, A., M. Sbai, and J. H. Alix. 2001. The chaperonin GroEL and other heat-shock proteins, besides DnaK, participate in ribosome biogenesis in Escherichia coli. Mol. Gen. Genet. 264:796-808.
    • (2001) Mol. Gen. Genet , vol.264 , pp. 796-808
    • El Hage, A.1    Sbai, M.2    Alix, J.H.3
  • 62
    • 0029103356 scopus 로고
    • Transcription of the region encoding the ferric dicitrate-transport system in Escherichia coli: Similarity between promoters for fecA and for extracytoplasmic function sigma factors
    • Enz, S., V. Braun, and J. H. Crosa. 1995. Transcription of the region encoding the ferric dicitrate-transport system in Escherichia coli: similarity between promoters for fecA and for extracytoplasmic function sigma factors. Gene 163:13-18.
    • (1995) Gene , vol.163 , pp. 13-18
    • Enz, S.1    Braun, V.2    Crosa, J.H.3
  • 63
    • 4944246094 scopus 로고    scopus 로고
    • Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
    • Ferbitz, L., T. Maier, H. Patzelt, B. Bukau, E. Deuerling, and N. Ban. 2004. Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. Nature 431:590-596.
    • (2004) Nature , vol.431 , pp. 590-596
    • Ferbitz, L.1    Maier, T.2    Patzelt, H.3    Bukau, B.4    Deuerling, E.5    Ban, N.6
  • 64
    • 0030949960 scopus 로고    scopus 로고
    • Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner
    • Freistroffer, D. V., M. Y. Pavlov, J. MacDougall, R. H. Buckingham, and M. Ehrenberg. 1997. Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner. EMBO J. 16:4126-4133.
    • (1997) EMBO J , vol.16 , pp. 4126-4133
    • Freistroffer, D.V.1    Pavlov, M.Y.2    MacDougall, J.3    Buckingham, R.H.4    Ehrenberg, M.5
  • 65
    • 0028301073 scopus 로고
    • RNA helicases: Modulators of RNA structure
    • Fuller-Pace, F. V. 1994. RNA helicases: modulators of RNA structure. Trends Cell Biol. 4:271-274.
    • (1994) Trends Cell Biol , vol.4 , pp. 271-274
    • Fuller-Pace, F.V.1
  • 66
    • 0025102288 scopus 로고
    • Guanosine 3′-diphosphate 5′-diphosphate is not required for growth rate-dependent control of rRNA synthesis in Escherichia coli
    • Gaal, T., and R. L. Gourse. 1990. Guanosine 3′-diphosphate 5′-diphosphate is not required for growth rate-dependent control of rRNA synthesis in Escherichia coli. Proc. Natl. Acad. Sci. USA 87:5533-5537.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5533-5537
    • Gaal, T.1    Gourse, R.L.2
  • 67
  • 68
    • 0028019112 scopus 로고
    • Isolated P2 rRNA promoters of Escherichia coli are strong promoters that are subject to stringent control
    • Gafny, R., S. Cohen, N. Nachaliel, and G. Glaser. 1994. Isolated P2 rRNA promoters of Escherichia coli are strong promoters that are subject to stringent control. J. Mol. Biol. 243:152-156.
    • (1994) J. Mol. Biol , vol.243 , pp. 152-156
    • Gafny, R.1    Cohen, S.2    Nachaliel, N.3    Glaser, G.4
  • 69
    • 0029820872 scopus 로고    scopus 로고
    • rRNA transcription and growth rate-dependent regulation of ribosome synthesis in Escherichia coli
    • Gourse, R. L., T. Gaal, M. S. Bartlett, J. A. Appleman, and W. Ross. 1996. rRNA transcription and growth rate-dependent regulation of ribosome synthesis in Escherichia coli. Annu. Rev. Microbiol. 50:645-677.
    • (1996) Annu. Rev. Microbiol , vol.50 , pp. 645-677
    • Gourse, R.L.1    Gaal, T.2    Bartlett, M.S.3    Appleman, J.A.4    Ross, W.5
  • 70
    • 0038449534 scopus 로고    scopus 로고
    • Control of rRNA and ribosome synthesis
    • C. C. Lin and A. S. Lynch ed, coli. R. G. Landes Company, Austin, TX
    • Gourse, R. L., and W. Ross. 1996. Control of rRNA and ribosome synthesis, p. 521-545. In C. C. Lin and A. S. Lynch (ed.), Regulation of gene expression in Escherichia coli. R. G. Landes Company, Austin, TX.
    • (1996) Regulation of gene expression in Escherichia , pp. 521-545
    • Gourse, R.L.1    Ross, W.2
  • 71
    • 2942691919 scopus 로고    scopus 로고
    • Sequence-specific Rho-RNA interactions in transcription termination
    • Graham, J. E. 2004. Sequence-specific Rho-RNA interactions in transcription termination. Nucleic Acids Res. 32:3093-3100.
    • (2004) Nucleic Acids Res , vol.32 , pp. 3093-3100
    • Graham, J.E.1
  • 72
    • 0029903805 scopus 로고    scopus 로고
    • In vitro complementation analysis localizes 23S rRNA posttranscriptional modifications that are required for Escherichia coli 50S ribosomal subunit assembly and function
    • Green, R., and H. F. Noller. 1996. In vitro complementation analysis localizes 23S rRNA posttranscriptional modifications that are required for Escherichia coli 50S ribosomal subunit assembly and function. RNA 2:1011-1021.
    • (1996) RNA , vol.2 , pp. 1011-1021
    • Green, R.1    Noller, H.F.2
  • 73
    • 0002580155 scopus 로고    scopus 로고
    • Translation initiation in bacteria
    • R. A. Garrett, S. R. Douthwaite, A. Liljas, A. T. Matheson, P. B. Moore, and H. F. Noller ed, interactions. ASM Press, Washington, DC
    • Gualerzi, C. O., L. B. Brandi, E. Caserta, A. La Teana, R. Spurio, J. Tomsic, and C. L. Pon. 2000. Translation initiation in bacteria, p. 477-494. In R. A. Garrett, S. R. Douthwaite, A. Liljas, A. T. Matheson, P. B. Moore, and H. F. Noller (ed.), The ribosome: structure, function, antibiotics, and cellular interactions. ASM Press, Washington, DC.
    • (2000) The ribosome: Structure, function, antibiotics, and cellular , pp. 477-494
    • Gualerzi, C.O.1    Brandi, L.B.2    Caserta, E.3    La Teana, A.4    Spurio, R.5    Tomsic, J.6    Pon, C.L.7
  • 74
    • 34548732185 scopus 로고    scopus 로고
    • Gutell, R. R. 1996. Comparative sequence analysis and the structure of 16S and 23S rRNA, p. 111-128. In R. A. Zimmermann and A. E. Dahlberg (ed.), Ribosomal RNA. Structure, evolution, processing, and function in protein biosynthesis. CRC Press, New York, NY.
    • Gutell, R. R. 1996. Comparative sequence analysis and the structure of 16S and 23S rRNA, p. 111-128. In R. A. Zimmermann and A. E. Dahlberg (ed.), Ribosomal RNA. Structure, evolution, processing, and function in protein biosynthesis. CRC Press, New York, NY.
  • 75
    • 22244456758 scopus 로고    scopus 로고
    • The pseudouridine synthetase RluD is required for normal ribosome assembly and function in Escherichia coli
    • Gutgsell, N. S., M. P. Deutscher, and J. Ofengand. 2005. The pseudouridine synthetase RluD is required for normal ribosome assembly and function in Escherichia coli. RNA 11:1141-1152.
    • (2005) RNA , vol.11 , pp. 1141-1152
    • Gutgsell, N.S.1    Deutscher, M.P.2    Ofengand, J.3
  • 76
    • 33645779767 scopus 로고    scopus 로고
    • Hamacher, K., J. Trylska, and J. A. McCammon. 2006. Dependency map of proteins in the small ribosomal subunit. PLoS Comp. Biol. 2:e10.
    • Hamacher, K., J. Trylska, and J. A. McCammon. 2006. Dependency map of proteins in the small ribosomal subunit. PLoS Comp. Biol. 2:e10.
  • 78
    • 0017273722 scopus 로고
    • Processing of the 17-S Escherichia coli precursor RNA in the 27-S pre-ribosomal particle
    • Hayes, F., and M. Vasseur. 1976. Processing of the 17-S Escherichia coli precursor RNA in the 27-S pre-ribosomal particle. Eur. J. Biochem. 61: 433-442.
    • (1976) Eur. J. Biochem , vol.61 , pp. 433-442
    • Hayes, F.1    Vasseur, M.2
  • 79
    • 0016153699 scopus 로고
    • Assembly mapping of 30S ribosomal proteins from Escherichia coli
    • Held, W. A., B. Ballou, S. Mizushima, and M. Nomura. 1974. Assembly mapping of 30S ribosomal proteins from Escherichia coli. J. Biol. Chem. 249:3103-3111.
    • (1974) J. Biol. Chem , vol.249 , pp. 3103-3111
    • Held, W.A.1    Ballou, B.2    Mizushima, S.3    Nomura, M.4
  • 80
    • 0034067840 scopus 로고    scopus 로고
    • Transcription termination control in bacteria
    • Henkin, T. M. 2000. Transcription termination control in bacteria. Curr. Opin. Microbiol. 3:149-153.
    • (2000) Curr. Opin. Microbiol , vol.3 , pp. 149-153
    • Henkin, T.M.1
  • 82
    • 0027258590 scopus 로고
    • Characterization of RNA and DNA synthesis in Escherichia coli strains devoid of ppGpp
    • Hernandez, V. J., and H. Bremer. 1993. Characterization of RNA and DNA synthesis in Escherichia coli strains devoid of ppGpp. J. Biol. Chem. 268: 10851-10862.
    • (1993) J. Biol. Chem , vol.268 , pp. 10851-10862
    • Hernandez, V.J.1    Bremer, H.2
  • 83
    • 0023664556 scopus 로고
    • Incorporation of six additional proteins to complete the assembly map of the 50S subunit from Escherichia coli ribosomes
    • Herold, M., and K. N. Nierhaus. 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.N.2
  • 84
    • 0029163563 scopus 로고
    • RNA chaperones and the RNA folding problem
    • Herschlag, D. 1995. RNA chaperones and the RNA folding problem. J. Biol. Chem. 270:20871-20874.
    • (1995) J. Biol. Chem , vol.270 , pp. 20871-20874
    • Herschlag, D.1
  • 85
    • 26844454546 scopus 로고    scopus 로고
    • The seven E. coli ribosomal RNA operon upstream regulatory regions differ in structure and transcription factor binding efficiencies
    • Hillebrand, A., R. Wurm, A. Menzel, and R. Wagner. 2005. The seven E. coli ribosomal RNA operon upstream regulatory regions differ in structure and transcription factor binding efficiencies. Biol. Chem. 366:523-534.
    • (2005) Biol. Chem , vol.366 , pp. 523-534
    • Hillebrand, A.1    Wurm, R.2    Menzel, A.3    Wagner, R.4
  • 87
    • 0035688744 scopus 로고    scopus 로고
    • Contributions of UP elements and the transcription factor FIS to expression from the seven rrn P1 promoters in Escherichia coli
    • Hirvonen, C. A., W. Ross, C. E. Wozniak, E. Marasco, J. R. Anthony, S. E. Ayar, V. H. Newburn, and R. L. Gourse. 2001. Contributions of UP elements and the transcription factor FIS to expression from the seven rrn P1 promoters in Escherichia coli. J. Bacteriol. 183:6305-6314.
    • (2001) J. Bacteriol , vol.183 , pp. 6305-6314
    • Hirvonen, C.A.1    Ross, W.2    Wozniak, C.E.3    Marasco, E.4    Anthony, J.R.5    Ayar, S.E.6    Newburn, V.H.7    Gourse, R.L.8
  • 88
    • 27644536231 scopus 로고    scopus 로고
    • Analysis of conformational changes in 16S rRNA during the course of 30S subunit assembly
    • Holmes, K. L., and G. M. Culver. 2005. Analysis of conformational changes in 16S rRNA during the course of 30S subunit assembly. J. Mol. Biol. 354:340-357.
    • (2005) J. Mol. Biol , vol.354 , pp. 340-357
    • Holmes, K.L.1    Culver, G.M.2
  • 89
    • 0742322957 scopus 로고    scopus 로고
    • Mapping structural differences between 30S ribosomal subunit assembly intermediates
    • Holmes, K. L., and G. M. Culver. 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.L.1    Culver, G.M.2
  • 90
    • 33748486487 scopus 로고    scopus 로고
    • The tandem GTPase, Der, is essential for the biogenesis of 50S ribosomal subunits in Escherichia coli
    • Hwang, J., and M. Inouye. 2006. The tandem GTPase, Der, is essential for the biogenesis of 50S ribosomal subunits in Escherichia coli. Mol. Microbiol. 61:1660-1672.
    • (2006) Mol. Microbiol , vol.61 , pp. 1660-1672
    • Hwang, J.1    Inouye, M.2
  • 91
    • 0038016743 scopus 로고    scopus 로고
    • Suppression of defective ribosome assembly in a rbfA deletion mutant by overexpression of Era, an essential GTPase in Escherichia coli
    • Inoue, K., J. Alsina, J. Chen, and M. Inouye. 2003. Suppression of defective ribosome assembly in a rbfA deletion mutant by overexpression of Era, an essential GTPase in Escherichia coli. Mol. Microbiol. 48:1005-1016.
    • (2003) Mol. Microbiol , vol.48 , pp. 1005-1016
    • Inoue, K.1    Alsina, J.2    Chen, J.3    Inouye, M.4
  • 92
    • 0033765113 scopus 로고    scopus 로고
    • Functional modulation of Escherichia coli RNA polymerase
    • Ishihama, A. 2000. Functional modulation of Escherichia coli RNA polymerase. Annu. Rev. Microbiol. 54:499-518.
    • (2000) Annu. Rev. Microbiol , vol.54 , pp. 499-518
    • Ishihama, A.1
  • 93
    • 0018870981 scopus 로고
    • Ribosomal protein modification in Escherichia coli. II. Studies of a mutant lacking the N-terminal acetylation of protein S18
    • Isono, I., and K. Isono. 1980. Ribosomal protein modification in Escherichia coli. II. Studies of a mutant lacking the N-terminal acetylation of protein S18. Mol. Gen. Genet. 177:645-651.
    • (1980) Mol. Gen. Genet , vol.177 , pp. 645-651
    • Isono, I.1    Isono, K.2
  • 94
    • 34548730541 scopus 로고    scopus 로고
    • Jemiolo, D. K. 1996. Processing of prokaryotic ribosomal RNA, p. 453-468. In R. A. Zimmermann and A. E. Dahlberg (ed.), Ribosomal RNA. Structure, evolution, processing, and function in protein synthesis. CRC Press, New York, NY.
    • Jemiolo, D. K. 1996. Processing of prokaryotic ribosomal RNA, p. 453-468. In R. A. Zimmermann and A. E. Dahlberg (ed.), Ribosomal RNA. Structure, evolution, processing, and function in protein synthesis. CRC Press, New York, NY.
  • 96
    • 34247605075 scopus 로고    scopus 로고
    • Identification of novel Escherichia coli ribosome-associated proteins using isobaric tags and multidimensional protein identification techniques
    • Jiang, M., S. M. Sullivan, A. K. Walker, J. R. Strahler, P. C. Andrews, and J. R. Maddock. 2007. Identification of novel Escherichia coli ribosome-associated proteins using isobaric tags and multidimensional protein identification techniques. J. Bacteriol. 189:3434-3444.
    • (2007) J. Bacteriol , vol.189 , pp. 3434-3444
    • Jiang, M.1    Sullivan, S.M.2    Walker, A.K.3    Strahler, J.R.4    Andrews, P.C.5    Maddock, J.R.6
  • 97
    • 0017159367 scopus 로고
    • A lethal mutation which affects the maturation of ribosomes
    • Johnson, S. C., N. Watson, and D. Apirion. 1976. A lethal mutation which affects the maturation of ribosomes. Mol. Gen. Genet. 147:29-37.
    • (1976) Mol. Gen. Genet , vol.147 , pp. 29-37
    • Johnson, S.C.1    Watson, N.2    Apirion, D.3
  • 98
    • 0030043216 scopus 로고    scopus 로고
    • Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli
    • Jones, P. G., M. Mitta, Y. Kim, W. Jiang, and M. Inouye. 1996. Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli. Proc. Natl. Acad. Sci. USA 93:76-80.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 76-80
    • Jones, P.G.1    Mitta, M.2    Kim, Y.3    Jiang, W.4    Inouye, M.5
  • 99
    • 0028840061 scopus 로고
    • Stringent control and growth-rate-dependent control have nonidentical promoter sequence requirements
    • Josaitis, C. A., T. Gaal, and R. L. Gourse. 1995. Stringent control and growth-rate-dependent control have nonidentical promoter sequence requirements. Proc. Natl. Acad. Sci. USA 92:1117-1121.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1117-1121
    • Josaitis, C.A.1    Gaal, T.2    Gourse, R.L.3
  • 100
    • 2342553864 scopus 로고    scopus 로고
    • Temperature sensitivity caused by mutant release factor 1 is suppressed by mutations that affect 16S rRNA maturation
    • Kaczanowska, M., and M. Ryden-Aulin. 2004. Temperature sensitivity caused by mutant release factor 1 is suppressed by mutations that affect 16S rRNA maturation. J. Bacteriol. 186:3046-3055.
    • (2004) J. Bacteriol , vol.186 , pp. 3046-3055
    • Kaczanowska, M.1    Ryden-Aulin, M.2
  • 101
    • 13444259766 scopus 로고    scopus 로고
    • The YrdC protein - a putative ribosome maturation factor
    • Kaczanowska, M., and M. Rydén-Aulin. 2005. The YrdC protein - a putative ribosome maturation factor. Biochim. Biophys. Acta 1727:87-96.
    • (2005) Biochim. Biophys. Acta , vol.1727 , pp. 87-96
    • Kaczanowska, M.1    Rydén-Aulin, M.2
  • 102
    • 0024674214 scopus 로고
    • Characterization of the gene rimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 in Escherichia coli K12
    • Kang, W.-K., T. Icho, S. Isono, M. Kitakawa, and I. Isono. 1989. Characterization of the gene rimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 in Escherichia coli K12. Mol. Gen. Genet. 217:281-288.
    • (1989) Mol. Gen. Genet , vol.217 , pp. 281-288
    • Kang, W.-K.1    Icho, T.2    Isono, S.3    Kitakawa, M.4    Isono, I.5
  • 103
    • 0016656665 scopus 로고
    • The fate of ribosomes in Escherichia coli starved for a carbon source
    • Kaplan, R., and D. Apirion. 1975. The fate of ribosomes in Escherichia coli starved for a carbon source. J. Biol. Chem. 250:1854-1863.
    • (1975) J. Biol. Chem , vol.250 , pp. 1854-1863
    • Kaplan, R.1    Apirion, D.2
  • 104
    • 0033063428 scopus 로고    scopus 로고
    • Novel roles for classical factors at the interface between translation termination and initiation
    • Karimi, R., M. Y. Pavlov, R. H. Buckingham, and M. Ehrenberg. 1999. Novel roles for classical factors at the interface between translation termination and initiation. Mol. Cell 3:601-609.
    • (1999) Mol. Cell , vol.3 , pp. 601-609
    • Karimi, R.1    Pavlov, M.Y.2    Buckingham, R.H.3    Ehrenberg, M.4
  • 106
    • 0346850831 scopus 로고    scopus 로고
    • Release of ribosome-bound ribosome recycling factor by elongation factor G
    • Kiel, M. C., V. S. Raj, H. Kaji, and A. Kaji. 2003. Release of ribosome-bound ribosome recycling factor by elongation factor G. J. Biol. Chem. 278:48041-48050.
    • (2003) J. Biol. Chem , vol.278 , pp. 48041-48050
    • Kiel, M.C.1    Raj, V.S.2    Kaji, H.3    Kaji, A.4
  • 107
    • 0021100156 scopus 로고
    • S1 nuclease mapping analysis of ribosomal RNA processing in wild type and processing deficient Escherichia coli
    • King, C. K., and D. Schlessinger. 1983. S1 nuclease mapping analysis of ribosomal RNA processing in wild type and processing deficient Escherichia coli. J. Biol. Chem. 258:12034-12042.
    • (1983) J. Biol. Chem , vol.258 , pp. 12034-12042
    • King, C.K.1    Schlessinger, D.2
  • 108
    • 0022981322 scopus 로고
    • Nucleolytic processing of ribonucleic acid transcripts in procaryotes
    • King, T. C., R. Sirdeshmukh, and D. Schlessinger. 1986. Nucleolytic processing of ribonucleic acid transcripts in procaryotes. Microbiol. Rev. 50: 428-451.
    • (1986) Microbiol. Rev , vol.50 , pp. 428-451
    • King, T.C.1    Sirdeshmukh, R.2    Schlessinger, D.3
  • 109
    • 0021347298 scopus 로고
    • RNase III cleavage is obligate for maturation but not for function of Escherichia coli pre-23S rRNA
    • King, T. C., R. Sirdeshmukh, and D. Schlessinger. 1984. RNase III cleavage is obligate for maturation but not for function of Escherichia coli pre-23S rRNA. Proc. Natl. Acad. Sci. USA 81:185-188.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 185-188
    • King, T.C.1    Sirdeshmukh, R.2    Schlessinger, D.3
  • 110
    • 0037439231 scopus 로고    scopus 로고
    • Termination of translation: Interplay of mRNA, rRNAs and release factors?
    • Kisselev, L., M. Ehrenberg, and L. Y. Frolova. 2003. Termination of translation: interplay of mRNA, rRNAs and release factors? EMBO J. 22:175-182.
    • (2003) EMBO J , vol.22 , pp. 175-182
    • Kisselev, L.1    Ehrenberg, M.2    Frolova, L.Y.3
  • 111
    • 1542378898 scopus 로고    scopus 로고
    • Visualization of release factor 3 on the ribosome during termination of protein synthesis
    • Klaholtz, B. P., A. G. Myasnikov, and M. van Heel. 2004. Visualization of release factor 3 on the ribosome during termination of protein synthesis. Nature 427:862-865.
    • (2004) Nature , vol.427 , pp. 862-865
    • Klaholtz, B.P.1    Myasnikov, A.G.2    van Heel, M.3
  • 112
    • 4344569647 scopus 로고    scopus 로고
    • The contribution of metal ions to the structural stability of the large ribosomal subunit
    • Klein, D. J., P. B. Moore, and J. A. Steitz. 2004. The contribution of metal ions to the structural stability of the large ribosomal subunit. RNA 10:1366-1379.
    • (2004) RNA , vol.10 , pp. 1366-1379
    • Klein, D.J.1    Moore, P.B.2    Steitz, J.A.3
  • 113
    • 33846649581 scopus 로고    scopus 로고
    • Importance of the 5S rRNA-binding ribosomal proteins for cell viability and translation Escherichia coli
    • Korepanov, A., G. M. Gongadze, M. B. Graber, D. L. Court, and M. Bubunenko. 2007. Importance of the 5S rRNA-binding ribosomal proteins for cell viability and translation Escherichia coli. J. Mol. Biol. 366:1199-1208.
    • (2007) J. Mol. Biol , vol.366 , pp. 1199-1208
    • Korepanov, A.1    Gongadze, G.M.2    Graber, M.B.3    Court, D.L.4    Bubunenko, M.5
  • 114
    • 33748582906 scopus 로고    scopus 로고
    • Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements
    • Korostelev, A., S. Trakhanov, M. Laurberg, and H. F. Noller. 2006. Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements. Cell 126:1-13.
    • (2006) Cell , vol.126 , pp. 1-13
    • Korostelev, A.1    Trakhanov, S.2    Laurberg, M.3    Noller, H.F.4
  • 115
    • 0030017693 scopus 로고    scopus 로고
    • β-Methylthio-aspartic acid: Identification of a novel posttranslational modification in ribosomal protein S12 from Escherichia coli
    • Kowalak, J. A., and K. A. Walsh. 1996. β-Methylthio-aspartic acid: identification of a novel posttranslational modification in ribosomal protein S12 from Escherichia coli. Protein Sci. 5:1625-1632.
    • (1996) Protein Sci , vol.5 , pp. 1625-1632
    • Kowalak, J.A.1    Walsh, K.A.2
  • 116
    • 0029819597 scopus 로고    scopus 로고
    • Transcriptional pausing of RNA polymerase in the presence of guanosine tetraphosphate depends on the promoter and gene sequence
    • Krohn, M., and R. Wagner. 1996. Transcriptional pausing of RNA polymerase in the presence of guanosine tetraphosphate depends on the promoter and gene sequence. J. Bacteriol. 271:23884-23894.
    • (1996) J. Bacteriol , vol.271 , pp. 23884-23894
    • Krohn, M.1    Wagner, R.2
  • 117
    • 0023216779 scopus 로고
    • In vitro synthesis of 16S ribosomal RNA containing single base changes and assembly into a functional 30S ribosome
    • Krzyzosiak, W., R. Denman, K. Nurse, W. Hellmann, M. Boublik, C. W. Gehrke, P. F. Agris, and J. Ofengand. 1987. In vitro synthesis of 16S ribosomal RNA containing single base changes and assembly into a functional 30S ribosome. Biochemistry 26:2353-2364.
    • (1987) Biochemistry , vol.26 , pp. 2353-2364
    • Krzyzosiak, W.1    Denman, R.2    Nurse, K.3    Hellmann, W.4    Boublik, M.5    Gehrke, C.W.6    Agris, P.F.7    Ofengand, J.8
  • 119
    • 33750290824 scopus 로고    scopus 로고
    • 2G methyltransferases. I. The ycbY gene encodes a methyltransferase specific for G2445 of the 23S rRNA
    • 2G methyltransferases. I. The ycbY gene encodes a methyltransferase specific for G2445 of the 23S rRNA. J. Mol. Biol. 364:20-25.
    • (2006) J. Mol. Biol , vol.364 , pp. 20-25
    • Lesnyak, D.V.1    Sergiev, P.V.2    Bogdanov, A.A.3    Dontsova, O.A.4
  • 120
    • 0027305857 scopus 로고
    • Coupling of rRNA transcription and ribosomal assembly in vivo
    • Lewicki, B. T. U., T. Margus, J. Remme, and K. N. Nierhaus. 1993. Coupling of rRNA transcription and ribosomal assembly in vivo. J. Mol. Biol. 231:581-593.
    • (1993) J. Mol. Biol , vol.231 , pp. 581-593
    • Lewicki, B.T.U.1    Margus, T.2    Remme, J.3    Nierhaus, K.N.4
  • 121
    • 0019834067 scopus 로고
    • Cold-sensitive ribosome assembly in an Escherichia coli mutant lacking a single methyl group in ribosomal protein L3
    • Lhoest, J., and C. Colson. 1981. Cold-sensitive ribosome assembly in an Escherichia coli mutant lacking a single methyl group in ribosomal protein L3. Eur. J. Biochem. 121:33-37.
    • (1981) Eur. J. Biochem , vol.121 , pp. 33-37
    • Lhoest, J.1    Colson, C.2
  • 122
    • 0029151159 scopus 로고
    • The tRNA processing enzyme RNase T is essential for maturation of 5S RNA
    • Li, Z., and M. P. Deutscher. 1995. The tRNA processing enzyme RNase T is essential for maturation of 5S RNA. Proc. Natl. Acad. Sci. USA 92:6883-6886.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6883-6886
    • Li, Z.1    Deutscher, M.P.2
  • 123
    • 0032951885 scopus 로고    scopus 로고
    • Maturation of 23S ribosomal RNA requires the exoribonuclease RNase T
    • Li, Z., S. Pandit, and M. P. Deutscher. 1999. Maturation of 23S ribosomal RNA requires the exoribonuclease RNase T. RNA 5:139-146.
    • (1999) RNA , vol.5 , pp. 139-146
    • Li, Z.1    Pandit, S.2    Deutscher, M.P.3
  • 124
    • 0032514754 scopus 로고    scopus 로고
    • Polyadenylation of stable RNA precursors in vivo
    • Li, Z., S. Pandit, and M. P. Deutscher. 1998. Polyadenylation of stable RNA precursors in vivo. Proc. Natl. Acad. Sci. USA 95:12158-12162.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12158-12162
    • Li, Z.1    Pandit, S.2    Deutscher, M.P.3
  • 125
    • 0033577789 scopus 로고    scopus 로고
    • RNase G (CafA protein) and RNase E are both required for the 5′ maturation of 16S ribosomal RNA
    • Li, Z., S. Pandit, and M. P. Deutscher. 1999. RNase G (CafA protein) and RNase E are both required for the 5′ maturation of 16S ribosomal RNA. EMBO J. 18:2878-2885.
    • (1999) EMBO J , vol.18 , pp. 2878-2885
    • Li, Z.1    Pandit, S.2    Deutscher, M.P.3
  • 126
    • 0034075255 scopus 로고    scopus 로고
    • mRNA composition and control of bacterial gene expression
    • Liang, S. T., Y. C. Xu, P. Dennis, and H. Bremer. 2000. mRNA composition and control of bacterial gene expression. J. Bacteriol. 182:3037-3044.
    • (2000) J. Bacteriol , vol.182 , pp. 3037-3044
    • Liang, S.T.1    Xu, Y.C.2    Dennis, P.3    Bremer, H.4
  • 127
    • 4444244605 scopus 로고    scopus 로고
    • Importance of transient structures during post-transcriptional refolding of the pre-23S rRNA and ribosomal large subunit assembly
    • Liiv, A., and J. Remme. 2004. Importance of transient structures during post-transcriptional refolding of the pre-23S rRNA and ribosomal large subunit assembly. J. Mol. Biol. 342:725-741.
    • (2004) J. Mol. Biol , vol.342 , pp. 725-741
    • Liiv, A.1    Remme, J.2
  • 128
    • 0016607629 scopus 로고
    • Intermediates and time kinetics of the in vitro assembly of Escherichia coli ribosomes
    • Lindahl, L. 1975. Intermediates and time kinetics of the in vitro assembly of Escherichia coli ribosomes. J. Mol. Biol. 92:15-37.
    • (1975) J. Mol. Biol , vol.92 , pp. 15-37
    • Lindahl, L.1
  • 129
    • 0037188887 scopus 로고    scopus 로고
    • RNA chaperones exist and DEAD box proteins get a life
    • Lorsch, J. R. 2002. RNA chaperones exist and DEAD box proteins get a life. Cell 109:797-800.
    • (2002) Cell , vol.109 , pp. 797-800
    • Lorsch, J.R.1
  • 130
    • 0031705811 scopus 로고    scopus 로고
    • The gene for 16S rRNA methyltransferase (ksgA) functions as a multicopy suppressor for a cold-sensitive mutant of Era, an essential RAS-like GTP-binding protein in Escherichia coli
    • Lu, Q., and M. Inouye. 1998. The gene for 16S rRNA methyltransferase (ksgA) functions as a multicopy suppressor for a cold-sensitive mutant of Era, an essential RAS-like GTP-binding protein in Escherichia coli. J. Bacteriol. 180:5243-5246.
    • (1998) J. Bacteriol , vol.180 , pp. 5243-5246
    • Lu, Q.1    Inouye, M.2
  • 131
    • 0034666279 scopus 로고    scopus 로고
    • Competition among seven Escherichia coli a subunits: Relative binding affinities to the core RNA polymerase
    • Maeda, H., N. Fujita, and A. Ishihama. 2000. Competition among seven Escherichia coli a subunits: relative binding affinities to the core RNA polymerase. Nucleic Acids Res. 28:3497-3503.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3497-3503
    • Maeda, H.1    Fujita, N.2    Ishihama, A.3
  • 132
  • 133
    • 23044444048 scopus 로고    scopus 로고
    • Recent developments in factor-facilitated ribosome assembly
    • Maki, J. A., and G. M. Culver. 2005. Recent developments in factor-facilitated ribosome assembly. Methods 36:313-320.
    • (2005) Methods , vol.36 , pp. 313-320
    • Maki, J.A.1    Culver, G.M.2
  • 134
    • 0036342369 scopus 로고    scopus 로고
    • The DnaK chaperone system facilitates 30S ribosomal subunit assembly
    • Maki, J. A., D. J. Schnobrich, and G. M. Culver. 2002. The DnaK chaperone system facilitates 30S ribosomal subunit assembly. Mol. Cell 10:129-138.
    • (2002) Mol. Cell , vol.10 , pp. 129-138
    • Maki, J.A.1    Schnobrich, D.J.2    Culver, G.M.3
  • 135
    • 0345305432 scopus 로고    scopus 로고
    • Demonstration of the role of the DnaK chaperone system in assembly of 30S ribosomal subunits using a purified in vitro system
    • Maki, J. A., D. R. Southworth, and G. M. Culver. 2003. Demonstration of the role of the DnaK chaperone system in assembly of 30S ribosomal subunits using a purified in vitro system. RNA 9:1418-1421.
    • (2003) RNA , vol.9 , pp. 1418-1421
    • Maki, J.A.1    Southworth, D.R.2    Culver, G.M.3
  • 136
    • 0345730808 scopus 로고    scopus 로고
    • Growth phase-dependent regulation and stringent control of fis are conserved processes in enteric bacteria and involve a single promoter (fis P) in Escherichia coli
    • Mallik, P., T. S. Pratt, M. B. Beach, M. D. Bradley, J. Undamatla, and R. Osuna. 2004. Growth phase-dependent regulation and stringent control of fis are conserved processes in enteric bacteria and involve a single promoter (fis P) in Escherichia coli. J. Bacteriol. 186:122-135.
    • (2004) J. Bacteriol , vol.186 , pp. 122-135
    • Mallik, P.1    Pratt, T.S.2    Beach, M.B.3    Bradley, M.D.4    Undamatla, J.5    Osuna, R.6
  • 137
    • 0030784254 scopus 로고    scopus 로고
    • rRNA maturation as a "quality" control step in ribosomal subunit assembly in Dictyostelium discoideum
    • Mangiarotti, G., S. Chiaberge, and S. Bulfone. 1997. rRNA maturation as a "quality" control step in ribosomal subunit assembly in Dictyostelium discoideum. J. Biol. Chem. 272:27818-27822.
    • (1997) J. Biol. Chem , vol.272 , pp. 27818-27822
    • Mangiarotti, G.1    Chiaberge, S.2    Bulfone, S.3
  • 138
    • 0016440668 scopus 로고
    • Role of precursor 16S RNA in assembly of E. coli 30S ribosome
    • Mangiarotti, G., E. Turco, C. Perlo, and F. Altruda. 1975. Role of precursor 16S RNA in assembly of E. coli 30S ribosome. Nature 253:569-570.
    • (1975) Nature , vol.253 , pp. 569-570
    • Mangiarotti, G.1    Turco, E.2    Perlo, C.3    Altruda, F.4
  • 139
  • 140
    • 25644436944 scopus 로고    scopus 로고
    • Translation initiation: Structures, mechanisms and evolution
    • Marintchev, A., and G. Wagner. 2004. Translation initiation: structures, mechanisms and evolution. Q. Rev. Biophys. 37:197-284.
    • (2004) Q. Rev. Biophys , vol.37 , pp. 197-284
    • Marintchev, A.1    Wagner, G.2
  • 141
    • 2442595013 scopus 로고    scopus 로고
    • Specific recognition of rpsO mRNA and 16S rRNA by Escherichia coli ribosomal protein S15 relies on both mimicry and site differentiation
    • Mathy, N., O. Pellegrini, A. Serganov, D. J. Patel, C. Ehresmann, and C. Portier. 2004. Specific recognition of rpsO mRNA and 16S rRNA by Escherichia coli ribosomal protein S15 relies on both mimicry and site differentiation. Mol. Microbiol. 52:661-675.
    • (2004) Mol. Microbiol , vol.52 , pp. 661-675
    • Mathy, N.1    Pellegrini, O.2    Serganov, A.3    Patel, D.J.4    Ehresmann, C.5    Portier, C.6
  • 142
    • 0034067634 scopus 로고    scopus 로고
    • Era GTPase of Escherichia coli: Binding to 16S rRNA and modulation of GTPase activity by RNA and carbohydrates
    • Meier, T. I., R. B. Peery, K. A. McAllister, and G. Zhao. 2000. Era GTPase of Escherichia coli: binding to 16S rRNA and modulation of GTPase activity by RNA and carbohydrates. Microbiology 146:1071-1083.
    • (2000) Microbiology , vol.146 , pp. 1071-1083
    • Meier, T.I.1    Peery, R.B.2    McAllister, K.A.3    Zhao, G.4
  • 144
    • 0033457296 scopus 로고    scopus 로고
    • Analysis of the function of Escherichia coli poly(A) polymerase I in RNA metabolism
    • Mohanty, B. K., and S. R. Kushner. 1999. Analysis of the function of Escherichia coli poly(A) polymerase I in RNA metabolism. Mol. Microbiol. 34:1094-1108.
    • (1999) Mol. Microbiol , vol.34 , pp. 1094-1108
    • Mohanty, B.K.1    Kushner, S.R.2
  • 145
    • 0031801743 scopus 로고    scopus 로고
    • Information processing by RNA polymerase: Recognition of regulatory signals during RNA chain elongation
    • Mooney, R. A., I. Artsimovitch, and R. Landick. 1998. Information processing by RNA polymerase: recognition of regulatory signals during RNA chain elongation. J. Bacteriol. 180:3265-3275.
    • (1998) J. Bacteriol , vol.180 , pp. 3265-3275
    • Mooney, R.A.1    Artsimovitch, I.2    Landick, R.3
  • 146
    • 0033578860 scopus 로고    scopus 로고
    • RNA polymerase unveiled
    • Mooney, R. A., and R. Landick. 1999. RNA polymerase unveiled. Cell 98:687-690.
    • (1999) Cell , vol.98 , pp. 687-690
    • Mooney, R.A.1    Landick, R.2
  • 147
    • 0043268903 scopus 로고    scopus 로고
    • The structural basis of large ribosomal subunit function
    • Moore, P. B., and T. A. Steitz. 2003. The structural basis of large ribosomal subunit function. Annu. Rev. Biochem. 72:813-850.
    • (2003) Annu. Rev. Biochem , vol.72 , pp. 813-850
    • Moore, P.B.1    Steitz, T.A.2
  • 148
    • 0022450979 scopus 로고
    • Antitermination mechanisms in rRNA operons of Escherichia coli
    • Morgan, E. A. 1986. Antitermination mechanisms in rRNA operons of Escherichia coli. J. Bacteriol. 168:1-5.
    • (1986) J. Bacteriol , vol.168 , pp. 1-5
    • Morgan, E.A.1
  • 150
    • 0015243809 scopus 로고
    • Structure and function of bacterial ribosomes. XII. Accumulation of 21S particles by some cold-sensitive mutants of Escherichia coli
    • Nashimoto, H., W. A. Held, E. Kaltschmidt, and M. Nomura. 1971. Structure and function of bacterial ribosomes. XII. Accumulation of 21S particles by some cold-sensitive mutants of Escherichia coli. J. Mol. Biol. 62:121-138.
    • (1971) J. Mol. Biol , vol.62 , pp. 121-138
    • Nashimoto, H.1    Held, W.A.2    Kaltschmidt, E.3    Nomura, M.4
  • 151
    • 0014877018 scopus 로고
    • Structure and function of bacterial ribosomes. XI. Dependence of 50S ribosomal assembly on simultaneous assembly of 30S subunits
    • Nashimoto, H., and M. Nomura. 1970. Structure and function of bacterial ribosomes. XI. Dependence of 50S ribosomal assembly on simultaneous assembly of 30S subunits. Proc. Natl. Acad. Sci. USA 67:1440-1447.
    • (1970) Proc. Natl. Acad. Sci. USA , vol.67 , pp. 1440-1447
    • Nashimoto, H.1    Nomura, M.2
  • 152
    • 0015924780 scopus 로고
    • Ribosomal proteins. XLIII. In vivo assembly of Escherichia coli ribosomal proteins
    • Nierhaus, K. H., K. Bordasch, and H. E. Homann. 1973. Ribosomal proteins. XLIII. In vivo assembly of Escherichia coli ribosomal proteins J. Mol. Biol. 74:587-597.
    • (1973) J. Mol. Biol , vol.74 , pp. 587-597
    • Nierhaus, K.H.1    Bordasch, K.2    Homann, H.E.3
  • 153
    • 84955073832 scopus 로고    scopus 로고
    • Ribosome assembly: Assembly of the prokaryotic ribosome
    • K. N. Nierhaus and D. N. Wilson ed, Wiley-VCh, Einheim, Germany
    • Nierhaus, K. N. 2004. Ribosome assembly: assembly of the prokaryotic ribosome, p. 85-105. In K. N. Nierhaus and D. N. Wilson (ed.), Protein synthesis and ribosome structure. Wiley-VCh, Einheim, Germany.
    • (2004) Protein synthesis and ribosome structure , pp. 85-105
    • Nierhaus, K.N.1
  • 154
    • 0024220027 scopus 로고
    • An eIF-4A-like protein is a suppressor of an Escherichia coli mutant defective in 50S ribosomal subunit assembly
    • Nishi, K., F. Morel-Deville, J. W. B. Hershey, T. Leighton, and J. Schnier. 1988. An eIF-4A-like protein is a suppressor of an Escherichia coli mutant defective in 50S ribosomal subunit assembly. Nature 336:496-498.
    • (1988) Nature , vol.336 , pp. 496-498
    • Nishi, K.1    Morel-Deville, F.2    Hershey, J.W.B.3    Leighton, T.4    Schnier, J.5
  • 155
    • 34248349446 scopus 로고    scopus 로고
    • Mutations in rsmG, encoding a 16S rRNA methyltransferase, result in low-level streptomycin resistance and antibiotic overproduction in Streptomyces coelicolor A3(2)
    • Nishimura, K., T. Hosaka, S. Tokuyama, S. Okamoto, and K. Ochi. 2007. Mutations in rsmG, encoding a 16S rRNA methyltransferase, result in low-level streptomycin resistance and antibiotic overproduction in Streptomyces coelicolor A3(2). J. Bacteriol. 189:3876-3883.
    • (2007) J. Bacteriol , vol.189 , pp. 3876-3883
    • Nishimura, K.1    Hosaka, T.2    Tokuyama, S.3    Okamoto, S.4    Ochi, K.5
  • 156
    • 0027453160 scopus 로고
    • Recognition of boxA antiterminator RNA by the E coli antitermination factors NusB and ribosomal protein S10
    • Nodwell, J. R., and J. Greenblatt. 1993. Recognition of boxA antiterminator RNA by the E coli antitermination factors NusB and ribosomal protein S10. Cell 72:261-268.
    • (1993) Cell , vol.72 , pp. 261-268
    • Nodwell, J.R.1    Greenblatt, J.2
  • 158
    • 0032749381 scopus 로고    scopus 로고
    • Regulation of ribosome biosynthesis in Escherichia coli and Saccharomyces cerevisiae: Diversity and common principles
    • Nomura, M. 1999. Regulation of ribosome biosynthesis in Escherichia coli and Saccharomyces cerevisiae: diversity and common principles. J. Bacteriol. 181:6857-6864.
    • (1999) J. Bacteriol , vol.181 , pp. 6857-6864
    • Nomura, M.1
  • 159
    • 34548754197 scopus 로고    scopus 로고
    • Ofengand, J., and M. del Campo. 29 December 2004, posting date. Chapter 4.6.1, Modified nucleosides of Escherichia coli ribosomal RNA. In G. R. Björk (ed.), EcoSal - Escherichia coli and Salmonella: cellular and molecular biology. ASM Press, Washington, DC. http://www.ecosal.org.
    • Ofengand, J., and M. del Campo. 29 December 2004, posting date. Chapter 4.6.1, Modified nucleosides of Escherichia coli ribosomal RNA. In G. R. Björk (ed.), EcoSal - Escherichia coli and Salmonella: cellular and molecular biology. ASM Press, Washington, DC. http://www.ecosal.org.
  • 160
    • 18844413446 scopus 로고    scopus 로고
    • Structural insights into translational fidelity
    • Ogle, J. M., and V. Ramakrishnan. 2005. Structural insights into translational fidelity. Annu. Rev. Biochem. 74:129-177.
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 129-177
    • Ogle, J.M.1    Ramakrishnan, V.2
  • 161
    • 0018288493 scopus 로고
    • Analysis of rpsD mutations in Escherichia coli. II: Physiology of some representative mutants
    • Olsson, M. O. 1979. Analysis of rpsD mutations in Escherichia coli. II: Physiology of some representative mutants. Mol. Gen. Genet. 169:259-269.
    • (1979) Mol. Gen. Genet , vol.169 , pp. 259-269
    • Olsson, M.O.1
  • 162
    • 3242875113 scopus 로고    scopus 로고
    • Activation of transcription initiation from a stable RNA promoter by a FIS protein-mediated DNA structural transmission mechanism
    • Opel, M. L., K. A. Aeling, W. M. Holmes, R. C. Johnson, C. J. Benham, and G. W. Hatfield. 2004. Activation of transcription initiation from a stable RNA promoter by a FIS protein-mediated DNA structural transmission mechanism. Mol. Microbiol. 53:665-674.
    • (2004) Mol. Microbiol , vol.53 , pp. 665-674
    • Opel, M.L.1    Aeling, K.A.2    Holmes, W.M.3    Johnson, R.C.4    Benham, C.J.5    Hatfield, G.W.6
  • 164
    • 0042665928 scopus 로고    scopus 로고
    • RNase G of Escherichia coli exhibits only limited functional overlap with its essential homologue, RNase E
    • Ow, M. C., T. Perwez, and S. R. Kushner. 2003. RNase G of Escherichia coli exhibits only limited functional overlap with its essential homologue, RNase E. Mol. Microbiol. 49:607-622.
    • (2003) Mol. Microbiol , vol.49 , pp. 607-622
    • Ow, M.C.1    Perwez, T.2    Kushner, S.R.3
  • 165
    • 0032535207 scopus 로고    scopus 로고
    • Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the A site of the E. coli ribosome
    • Pape, T., W. Wintermeyer, and M. V. Rodnina. 1998. Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the A site of the E. coli ribosome. EMBO J. 17:7490-7497.
    • (1998) EMBO J , vol.17 , pp. 7490-7497
    • Pape, T.1    Wintermeyer, W.2    Rodnina, M.V.3
  • 166
    • 0017656504 scopus 로고
    • A new ribosomal mutation which affects the two ribosomal subunits in Escherichia coli
    • Pardo, D., and R. Rosset. 1977. A new ribosomal mutation which affects the two ribosomal subunits in Escherichia coli. Mol. Gen. Genet. 153:199-204.
    • (1977) Mol. Gen. Genet , vol.153 , pp. 199-204
    • Pardo, D.1    Rosset, R.2
  • 167
    • 0018290567 scopus 로고
    • Assembly of ribosomal subunits affected in a ribosomal mutant of E coli having an altered L22 protein
    • Pardo, D., C. Vola, and R. Rosset. 1979. Assembly of ribosomal subunits affected in a ribosomal mutant of E coli having an altered L22 protein. Mol. Gen. Genet. 174:53-58.
    • (1979) Mol. Gen. Genet , vol.174 , pp. 53-58
    • Pardo, D.1    Vola, C.2    Rosset, R.3
  • 168
    • 0028957034 scopus 로고
    • The Escherichia coli ribosomal RNA leader nut region interacts specifically with mature 16S RNA
    • Pardon, B., and R. Wagner. 1995. The Escherichia coli ribosomal RNA leader nut region interacts specifically with mature 16S RNA. Nucleic Acids Res. 23:932-941.
    • (1995) Nucleic Acids Res , vol.23 , pp. 932-941
    • Pardon, B.1    Wagner, R.2
  • 169
    • 0036296779 scopus 로고    scopus 로고
    • Alteration of stringent response of the Escherichia coli mpB promoter by mutations in the -35 region
    • Park, W. J., Y. Jung, S. J. Lee, D. J. Jin, and Y. Lee. 2002. Alteration of stringent response of the Escherichia coli mpB promoter by mutations in the -35 region. Biochem. Biophys. Res. Commun. 290:1183- 1187.
    • (2002) Biochem. Biophys. Res. Commun , vol.290 , pp. 1183-1187
    • Park, W.J.1    Jung, Y.2    Lee, S.J.3    Jin, D.J.4    Lee, Y.5
  • 170
    • 4043069926 scopus 로고    scopus 로고
    • DksA: A critical component of the transcription machinery that potentiates the regulation of rRNA promoters by ppGpp and the initiating NTP
    • Paul, B. J., M. M. Barker, D. A. Schneider, C. Webb, J. W. Foster, and R. L. Gourse. 2004. DksA: a critical component of the transcription machinery that potentiates the regulation of rRNA promoters by ppGpp and the initiating NTP. Cell 118:311-322.
    • (2004) Cell , vol.118 , pp. 311-322
    • Paul, B.J.1    Barker, M.M.2    Schneider, D.A.3    Webb, C.4    Foster, J.W.5    Gourse, R.L.6
  • 172
    • 4043108470 scopus 로고    scopus 로고
    • Regulation through the secondary channel - structural framework for ppGpp-DksA synergism during transcription
    • Perederina, A., V. Svetlov, M. N. Vassylyeva, T. H. Tahirov, S. Yokoyama, I. Artsimovitch, and D. M. Vassylyev. 2004. Regulation through the secondary channel - structural framework for ppGpp-DksA synergism during transcription. Cell 118:297-309.
    • (2004) Cell , vol.118 , pp. 297-309
    • Perederina, A.1    Svetlov, V.2    Vassylyeva, M.N.3    Tahirov, T.H.4    Yokoyama, S.5    Artsimovitch, I.6    Vassylyev, D.M.7
  • 173
    • 0027171312 scopus 로고
    • Dynamics of in vitro assembly of 16S rRNA into 30S ribosomal subunits
    • Powers, T., G. Daubresse, and H. F. Noller. 1993. Dynamics of in vitro assembly of 16S rRNA into 30S ribosomal subunits. J. Mol. Biol. 232:362-374.
    • (1993) J. Mol. Biol , vol.232 , pp. 362-374
    • Powers, T.1    Daubresse, G.2    Noller, H.F.3
  • 174
    • 0016710043 scopus 로고
    • Growth-dependent regulation in production and utilization of acetylated ribosomal protein L7
    • Ramagopal, S., and A. R. Subramanian. 1975. Growth-dependent regulation in production and utilization of acetylated ribosomal protein L7. J. Mol. Biol. 94:633-641.
    • (1975) J. Mol. Biol , vol.94 , pp. 633-641
    • Ramagopal, S.1    Subramanian, A.R.2
  • 175
    • 0037154986 scopus 로고    scopus 로고
    • Ribosome structure and the mechanism of translation
    • Ramakrishnan, V. 2002. Ribosome structure and the mechanism of translation. Cell 108:557-572.
    • (2002) Cell , vol.108 , pp. 557-572
    • Ramakrishnan, V.1
  • 176
    • 0037073063 scopus 로고    scopus 로고
    • Rho-dependent termination and ATPases in transcript termination. BBA Gene Struct. Expr
    • Richardson, J. P. 2002. Rho-dependent termination and ATPases in transcript termination. BBA Gene Struct. Expr. 1577:251-260.
    • (2002) , vol.1577 , pp. 251-260
    • Richardson, J.P.1
  • 177
    • 0000882465 scopus 로고    scopus 로고
    • Control of RNA chain elongation and termination
    • F. C. Neidhardt ed, biology. ASM Press, Washington, DC
    • Richardson, J. P., and J. Greenblatt. 1996. Control of RNA chain elongation and termination, p. 822-848. In F. C. Neidhardt (ed.), Escherichia coli and Salmonella: cellular and molecular biology. ASM Press, Washington, DC.
    • (1996) Escherichia coli and Salmonella: Cellular and molecular , pp. 822-848
    • Richardson, J.P.1    Greenblatt, J.2
  • 178
    • 0031028688 scopus 로고    scopus 로고
    • Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
    • Rodnina, M. V., A. Savelsbergh, V. I. Katunin, and W. Wintermeyer. 1997. Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome. Nature 385:37-41.
    • (1997) Nature , vol.385 , pp. 37-41
    • Rodnina, M.V.1    Savelsbergh, A.2    Katunin, V.I.3    Wintermeyer, W.4
  • 179
    • 0036606484 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli glucose-inhibited division protein B (GidB) reveals a methyltransferase fold
    • Romanowski, M. J., J. B. Bonanno, and S. K. Burley. 2002. Crystal structure of the Escherichia coli glucose-inhibited division protein B (GidB) reveals a methyltransferase fold. Proteins Struct. Funct. Genet. 47:563-567.
    • (2002) Proteins Struct. Funct. Genet , vol.47 , pp. 563-567
    • Romanowski, M.J.1    Bonanno, J.B.2    Burley, S.K.3
  • 180
    • 0031691355 scopus 로고    scopus 로고
    • Escherichia coli promoters with UP elements of different strengths: Modular structure of bacterial promoters
    • Ross, W., S. E. Aiyar, J. Salomon, and R. L. Gourse. 1998. Escherichia coli promoters with UP elements of different strengths: modular structure of bacterial promoters. J. Bacteriol. 180:5375-5383.
    • (1998) J. Bacteriol , vol.180 , pp. 5375-5383
    • Ross, W.1    Aiyar, S.E.2    Salomon, J.3    Gourse, R.L.4
  • 181
    • 0025163439 scopus 로고    scopus 로고
    • Ross, W., J. F. Thompson, J. T. Newlands, and R. L. Gourse. 1990. E. coli Fis protein activates ribosomal RNA transcription in vitro and in vivo. EMBO J. 9:3733-3742.
    • Ross, W., J. F. Thompson, J. T. Newlands, and R. L. Gourse. 1990. E. coli Fis protein activates ribosomal RNA transcription in vitro and in vivo. EMBO J. 9:3733-3742.
  • 182
    • 0020731515 scopus 로고
    • Maturation of 5S rRNA: Ribonuclease E cleavages and their dependence on precursor sequences
    • Roy, M. K., B. Singh, B. K. Ray, and D. Apirion. 1983. Maturation of 5S rRNA: ribonuclease E cleavages and their dependence on precursor sequences. Eur. J. Biochem. 131:119-127.
    • (1983) Eur. J. Biochem , vol.131 , pp. 119-127
    • Roy, M.K.1    Singh, B.2    Ray, B.K.3    Apirion, D.4
  • 183
    • 0027483417 scopus 로고
    • Ribosome activity and modification of 16S RNA are influenced by deletion of ribosomal protein S20
    • Rydén-Aulin, M., S. Zhang, P. Kylsten, and L. A. Isaksson. 1993. Ribosome activity and modification of 16S RNA are influenced by deletion of ribosomal protein S20. Mol. Microbiol. 7:983-992.
    • (1993) Mol. Microbiol , vol.7 , pp. 983-992
    • Rydén-Aulin, M.1    Zhang, S.2    Kylsten, P.3    Isaksson, L.A.4
  • 185
    • 0033554653 scopus 로고    scopus 로고
    • Era, an essential Esch erichia coli small G-protein, binds to the 30S ribosomal subunit
    • Sayed, A., S.-I. Matsuyama, and M. Inouye. 1999. Era, an essential Esch erichia coli small G-protein, binds to the 30S ribosomal subunit. Biochem. Biophys. Res. Commun. 264:51-54.
    • (1999) Biochem. Biophys. Res. Commun , vol.264 , pp. 51-54
    • Sayed, A.1    Matsuyama, S.-I.2    Inouye, M.3
  • 186
    • 0035881120 scopus 로고    scopus 로고
    • Effects of base change mutations within an Escherichia coli ribosomal RNA leader region on rRNA maturation and ribosome formation
    • Schaferkordt, J., and R. Wagner. 2001. Effects of base change mutations within an Escherichia coli ribosomal RNA leader region on rRNA maturation and ribosome formation. Nucleic Acids Res. 29:3394-3403.
    • (2001) Nucleic Acids Res , vol.29 , pp. 3394-3403
    • Schaferkordt, J.1    Wagner, R.2
  • 187
    • 0002429755 scopus 로고
    • Ribosome formation in Escherichia coli
    • M. Nomura ed, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Schlessinger, D. 1974. Ribosome formation in Escherichia coli, p. 393-416. In M. Nomura (ed.), Ribosomes. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1974) Ribosomes , pp. 393-416
    • Schlessinger, D.1
  • 189
    • 27644491082 scopus 로고    scopus 로고
    • Schuwirth, B. S., M. A. Borovinskaya, C. W. Hau, W. Zhang, A. Vila-Sanjurjo, J. M. Holton, and J. H. D. Cate. 2005. Structures of the bacterial ribosome at 3.5 Å resolution. Science 310:827-834.
    • Schuwirth, B. S., M. A. Borovinskaya, C. W. Hau, W. Zhang, A. Vila-Sanjurjo, J. M. Holton, and J. H. D. Cate. 2005. Structures of the bacterial ribosome at 3.5 Å resolution. Science 310:827-834.
  • 191
    • 0020503681 scopus 로고
    • Shape and compactness of the isolated ribosomal 16S RNA and its complexes with ribosomal proteins
    • Serdyuk, I. N., S. C. Agalarov, S. E. Sedelnikova, and A. S. Spirin. 1983. Shape and compactness of the isolated ribosomal 16S RNA and its complexes with ribosomal proteins. J. Mol. Biol. 169:409-425.
    • (1983) J. Mol. Biol , vol.169 , pp. 409-425
    • Serdyuk, I.N.1    Agalarov, S.C.2    Sedelnikova, S.E.3    Spirin, A.S.4
  • 192
    • 33750378312 scopus 로고    scopus 로고
    • 2G methyltransferases. II. The ygjO gene encodes a methyltransferase specific for G1835 of the 23S rRNA
    • 2G methyltransferases. II. The ygjO gene encodes a methyltransferase specific for G1835 of the 23S rRNA. J. Mol. Biol. 364:26-31.
    • (2006) J. Mol. Biol , vol.364 , pp. 26-31
    • Sergiev, P.V.1    Lesnyak, D.V.2    Bogdanov, A.A.3    Dontsova, O.A.4
  • 194
    • 0016154301 scopus 로고
    • The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribosome binding sites
    • Shine, J., and L. Dalgarno. 1974. The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc. Natl. Acad. Sci. USA 71:1342-1346.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 1342-1346
    • Shine, J.1    Dalgarno, L.2
  • 195
    • 0023767492 scopus 로고
    • Coregulation of processing and translation: Mature 5′ termini of Escherichia coli 23S ribosomal RNA form in polysomes
    • Srivastava, A. K., and D. Schlessinger. 1988. Coregulation of processing and translation: mature 5′ termini of Escherichia coli 23S ribosomal RNA form in polysomes. Proc. Natl. Acad. Sci. USA 85:7144-7148.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7144-7148
    • Srivastava, A.K.1    Schlessinger, D.2
  • 196
    • 0024374064 scopus 로고
    • Escherichia coli 16S rRNA 3′-end formation requires a distal transfer RNA sequence at a proper distance
    • Srivastava, A. K., and D. Schlessinger. 1989. Escherichia coli 16S rRNA 3′-end formation requires a distal transfer RNA sequence at a proper distance. EMBO J. 8:3159-3166.
    • (1989) EMBO J , vol.8 , pp. 3159-3166
    • Srivastava, A.K.1    Schlessinger, D.2
  • 197
    • 0025153770 scopus 로고
    • Mechanism and regulation of bacterial ribosomal RNA
    • Srivastava, A. K., and D. Schlessinger. 1990. Mechanism and regulation of bacterial ribosomal RNA. Annu. Rev. Microbiol. 44:105-129.
    • (1990) Annu. Rev. Microbiol , vol.44 , pp. 105-129
    • Srivastava, A.K.1    Schlessinger, D.2
  • 198
    • 0037453294 scopus 로고    scopus 로고
    • A structural model for the assembly of the 30S subunit of the ribosome
    • Stagg, S. M., J. A. Mears, and S. C. Harvey. 2003. A structural model for the assembly of the 30S subunit of the ribosome. J. Mol. Biol. 328:49-61.
    • (2003) J. Mol. Biol , vol.328 , pp. 49-61
    • Stagg, S.M.1    Mears, J.A.2    Harvey, S.C.3
  • 200
    • 28444479853 scopus 로고    scopus 로고
    • An assembly landscape for the 30S ribosomal subunit
    • Talkington, M. W. T., G. Siuzdak, and J. R. Williamson. 2005. An assembly landscape for the 30S ribosomal subunit. Nature 438:628-632.
    • (2005) Nature , vol.438 , pp. 628-632
    • Talkington, M.W.T.1    Siuzdak, G.2    Williamson, J.R.3
  • 201
    • 0036237999 scopus 로고    scopus 로고
    • Overexpression of two different GTPases rescues a null mutation in a heat-induced tRNA methyltransferase
    • Tan, J., U. Jakob, and J. C. A. Bardwell. 2002. Overexpression of two different GTPases rescues a null mutation in a heat-induced tRNA methyltransferase. J. Bacteriol. 184:2692-2698.
    • (2002) J. Bacteriol , vol.184 , pp. 2692-2698
    • Tan, J.1    Jakob, U.2    Bardwell, J.C.A.3
  • 202
    • 0034491066 scopus 로고    scopus 로고
    • The structure of the yrdC gene product from Escherichia coli reveals a new fold and suggests a role in RNA binding
    • Teplova, M., V. Tereshko, R. Sanishvili, A. Joachimiak, T. Bushueva, W. F. Anderson, and M. Egli. 2000. The structure of the yrdC gene product from Escherichia coli reveals a new fold and suggests a role in RNA binding. Protein Sci. 9:2557-2566.
    • (2000) Protein Sci , vol.9 , pp. 2557-2566
    • Teplova, M.1    Tereshko, V.2    Sanishvili, R.3    Joachimiak, A.4    Bushueva, T.5    Anderson, W.F.6    Egli, M.7
  • 204
    • 0025733344 scopus 로고
    • deaD, a new Escherichia coli gene encoding a presumed ATP-dependent RNA helicase, can suppress a mutation in rpsB, the gene encoding ribosomal protein S2
    • Toone, W. M., K. E. Rudd, and J. D. Friesen. 1991. deaD, a new Escherichia coli gene encoding a presumed ATP-dependent RNA helicase, can suppress a mutation in rpsB, the gene encoding ribosomal protein S2. J. Bacteriol. 173:3291-3302.
    • (1991) J. Bacteriol , vol.173 , pp. 3291-3302
    • Toone, W.M.1    Rudd, K.E.2    Friesen, J.D.3
  • 205
    • 0035898536 scopus 로고    scopus 로고
    • Ribosomal protein S4 is a transcription factor with properties remarkably similar to NusA, a protein involved in both non-ribosomal and ribosomal RNA antitermination
    • Torres, M., C. Condon, J. M. Balada, C. Squires, and C. L. Squires. 2001. Ribosomal protein S4 is a transcription factor with properties remarkably similar to NusA, a protein involved in both non-ribosomal and ribosomal RNA antitermination. EMBO J. 20:3811-3820.
    • (2001) EMBO J , vol.20 , pp. 3811-3820
    • Torres, M.1    Condon, C.2    Balada, J.M.3    Squires, C.4    Squires, C.L.5
  • 206
    • 0029166388 scopus 로고
    • Effects of the antiterminator BoxA on transcription elongation kinetics and ppGpp inhibition of transcription elongation in Escherichia coli
    • Vogel, U., and K. F. Jensen. 1995. Effects of the antiterminator BoxA on transcription elongation kinetics and ppGpp inhibition of transcription elongation in Escherichia coli. J. Biol. Chem. 270:18335-18340.
    • (1995) J. Biol. Chem , vol.270 , pp. 18335-18340
    • Vogel, U.1    Jensen, K.F.2
  • 207
    • 0032584643 scopus 로고    scopus 로고
    • An integrated model of the transcription complex in elongation, termination, and editing
    • von Hippel, P. H. 1998. An integrated model of the transcription complex in elongation, termination, and editing. Science 281:660-665.
    • (1998) Science , vol.281 , pp. 660-665
    • von Hippel, P.H.1
  • 211
    • 0030916948 scopus 로고    scopus 로고
    • Protein-facilitated RNA folding
    • Weeks, K. M. 1997. Protein-facilitated RNA folding. Curr. Opin. Struct. Biol. 7:336-342.
    • (1997) Curr. Opin. Struct. Biol , vol.7 , pp. 336-342
    • Weeks, K.M.1
  • 212
    • 0023684123 scopus 로고
    • Non-autogenous control of ribosomal protein synthesis from the trmD operon in Escherichia coli
    • Wikstrom, P. M., A. S. Ihström, and G. R. Björk. 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
    • Wikstrom, P.M.1    Ihström, A.S.2    Björk, G.R.3
  • 213
    • 0037321039 scopus 로고    scopus 로고
    • After the ribosome structure: How are the subunits assembled?
    • Williamson, J. R. 2003. After the ribosome structure: how are the subunits assembled? RNA 9:165-167.
    • (2003) RNA , vol.9 , pp. 165-167
    • Williamson, J.R.1
  • 216
    • 0034043484 scopus 로고    scopus 로고
    • Recent insights on RNA folding mechanisms from catalytic RNA
    • Woodson, S. A. 2000. Recent insights on RNA folding mechanisms from catalytic RNA. Cell Mol. Life Sci. 57:796-808.
    • (2000) Cell Mol. Life Sci , vol.57 , pp. 796-808
    • Woodson, S.A.1
  • 218
    • 0023646048 scopus 로고
    • Feedback regulation of rRNA synthesis. A mutational alteration in the anti-Shine-Dalgarno region of the 16S rRNA gene abolishes regulation
    • Yamagishi, M., H. A. de Boer, and M. Nomura. 1987. Feedback regulation of rRNA synthesis. A mutational alteration in the anti-Shine-Dalgarno region of the 16S rRNA gene abolishes regulation. J. Mol. Biol. 198:547-550.
    • (1987) J. Mol. Biol , vol.198 , pp. 547-550
    • Yamagishi, M.1    de Boer, H.A.2    Nomura, M.3
  • 219
    • 0023212383 scopus 로고
    • A tunnel in the large ribosomal subunit revealed by three-dimensional image reconstruction
    • Yonath, A., K. R. Leonard, and H. G. Wittmann. 1987. A tunnel in the large ribosomal subunit revealed by three-dimensional image reconstruction. Science 236:813-816.
    • (1987) Science , vol.236 , pp. 813-816
    • Yonath, A.1    Leonard, K.R.2    Wittmann, H.G.3
  • 220
    • 0003463151 scopus 로고
    • Complementary sequences 1,700 nucleotides apart from a ribonuclease III cleavage site in Escherichia coli ribosomal precursor RNA
    • Young, R. A., and J. A. Steitz. 1978. Complementary sequences 1,700 nucleotides apart from a ribonuclease III cleavage site in Escherichia coli ribosomal precursor RNA. Proc. Natl. Acad. Sci. USA 75:3593-3597.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3593-3597
    • Young, R.A.1    Steitz, J.A.2


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