메뉴 건너뛰기




Volumn 42, Issue 3, 2007, Pages 187-219

The weird and wonderful world of bacterial ribosome regulation

Author keywords

Assembly; Biogenesis; Protein synthesis; Ribosome; RNA; Translation regulation

Indexed keywords

AMINOGLYCOSIDE ANTIBIOTIC AGENT; BACTERIAL RNA; CHLORAMPHENICOL; ELONGATION FACTOR; GENTAMICIN; GUANOSINE TRIPHOSPHATASE; HEAT SHOCK PROTEIN; KASUGAMYCIN; NEOMYCIN; PAROMOMYCIN; RAS PROTEIN; RIBOSOME PROTEIN; RIBOSOME RNA; RNA 16S; RNA 23S; RNA 5S; STREPTOMYCIN; TETRACYCLINE; TRANSFER RNA;

EID: 34250377197     PISSN: 10409238     EISSN: 15497798     Source Type: Journal    
DOI: 10.1080/10409230701360843     Document Type: Review
Times cited : (170)

References (248)
  • 1
    • 0033607228 scopus 로고    scopus 로고
    • A protein residing at the subunit interface of the bacterial ribosome
    • Agafonov, D.E., Kolb, V.A., Nazimov, I.V., and Spirin, A.S. 1999. A protein residing at the subunit interface of the bacterial ribosome. Proc Natl Acad Sci USA 96:12345-12349.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 12345-12349
    • Agafonov, D.E.1    Kolb, V.A.2    Nazimov, I.V.3    Spirin, A.S.4
  • 2
    • 0034981052 scopus 로고    scopus 로고
    • Ribosome-associated protein that inhibits translation at the aminoacyl-tRNA binding stage
    • Agafonov, D.E., Kolb, V.A., and Spirin, A.S. 2001. Ribosome-associated protein that inhibits translation at the aminoacyl-tRNA binding stage. EMBO Rep 2:399-402.
    • (2001) EMBO Rep , vol.2 , pp. 399-402
    • Agafonov, D.E.1    Kolb, V.A.2    Spirin, A.S.3
  • 3
    • 2942709696 scopus 로고    scopus 로고
    • The ribosome-associated inhibitor A reduces translation errors
    • Agafonov, D.E. and Spirin, A.S. 2004. The ribosome-associated inhibitor A reduces translation errors. Biochem Biophys Res Commun 320:354-358.
    • (2004) Biochem Biophys Res Commun , vol.320 , pp. 354-358
    • Agafonov, D.E.1    Spirin, A.S.2
  • 4
    • 0027362954 scopus 로고
    • Mutant DnaK chaperones cause ribosome assembly defects in Escherichia coli
    • Alix, J.H. and Guerin, M.F. 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
  • 5
    • 0038382885 scopus 로고    scopus 로고
    • DnaK-facilitated ribosome assembly in Escherichia coli revisited
    • Alix, J.H. and Nierhaus, K.H. 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.H.2
  • 6
    • 17144456169 scopus 로고    scopus 로고
    • The PRC-barrel: A widespread, conserved domain shared by photosynthetic reaction center subunits and proteins of RNA metabolism
    • Anantharaman, V. and Aravind, L. 2002. The PRC-barrel: A widespread, conserved domain shared by photosynthetic reaction center subunits and proteins of RNA metabolism. Genome Biol 3:61-69.
    • (2002) Genome Biol , vol.3 , pp. 61-69
    • Anantharaman, V.1    Aravind, L.2
  • 8
    • 33646806139 scopus 로고    scopus 로고
    • YebU is a m5 C methyltransferase specific for 16S rRNA nucleotide 1407
    • Andersen, N. and Douthwaite, S. 2006. YebU is a m5 C methyltransferase specific for 16S rRNA nucleotide 1407. Mol Biol 359:777-786.
    • (2006) Mol Biol , vol.359 , pp. 777-786
    • Andersen, N.1    Douthwaite, S.2
  • 9
    • 0027551469 scopus 로고
    • RNA processing in prokaryotic cells
    • Apirion, D. and Miczak, A. 1993. RNA processing in prokaryotic cells. Bioessays 15:113-120.
    • (1993) Bioessays , vol.15 , pp. 113-120
    • Apirion, D.1    Miczak, A.2
  • 10
    • 0030923669 scopus 로고    scopus 로고
    • Molecular characterization of the prokaryotic efp gene product involved in a peptidyltransferase reaction
    • Aoki, H., Adams, S.L., Turner, M.A., and Ganoza, M.C. 1997. Molecular characterization of the prokaryotic efp gene product involved in a peptidyltransferase reaction. Biochimie 79:7-11.
    • (1997) Biochimie , vol.79 , pp. 7-11
    • Aoki, H.1    Adams, S.L.2    Turner, M.A.3    Ganoza, M.C.4
  • 12
    • 0037139583 scopus 로고    scopus 로고
    • Recoding: Translational bifurcations in gene expression
    • Baranov, P.V., Gesteland, R.F., and Atkins, J.F. 2002. Recoding: translational bifurcations in gene expression. Gene 286:187-201.
    • (2002) Gene , vol.286 , pp. 187-201
    • Baranov, P.V.1    Gesteland, R.F.2    Atkins, J.F.3
  • 13
    • 0000254254 scopus 로고    scopus 로고
    • Bassler, J., Grandi, P., Gadal, O., Lessmann, T., Petfalski, E., Tollervey, D., and al., E. 2001. Identification of a 60S preribosomal particle that is closely linked to nuclear export. Mol Cell 8:517-529.
    • Bassler, J., Grandi, P., Gadal, O., Lessmann, T., Petfalski, E., Tollervey, D., and al., E. 2001. Identification of a 60S preribosomal particle that is closely linked to nuclear export. Mol Cell 8:517-529.
  • 14
    • 0023102643 scopus 로고
    • Reconstitution of peptidyltransferase activity on 50S and 70S ribosomal particles by peptide fragments of protein L16
    • Baxter, R.M., Ganoza, M.G., Zahid, N., and Chung, D.-G. 1987. Reconstitution of peptidyltransferase activity on 50S and 70S ribosomal particles by peptide fragments of protein L16. Eur. J Biochem 163:473-479.
    • (1987) Eur. J Biochem , vol.163 , pp. 473-479
    • Baxter, R.M.1    Ganoza, M.G.2    Zahid, N.3    Chung, D.-G.4
  • 15
    • 0023091436 scopus 로고
    • Sites of action of two ribosomal RNA methylases responsible for resistance to aminoglycosides
    • Beauclerk, A.A.D. and Cundliffe, E. 1987. Sites of action of two ribosomal RNA methylases responsible for resistance to aminoglycosides. J Mol Biol 193:661-671.
    • (1987) J Mol Biol , vol.193 , pp. 661-671
    • Beauclerk, A.A.D.1    Cundliffe, E.2
  • 16
    • 0022052166 scopus 로고
    • Sequence of the relB transcription unit from Escherichia coli and identification of the relB gene
    • Bech, F.W., Jorgensen, S.T., Diderichsen, B., and Karlstrom, O.H. 1985. Sequence of the relB transcription unit from Escherichia coli and identification of the relB gene. EMBO J 4:1059-1066.
    • (1985) EMBO J , vol.4 , pp. 1059-1066
    • Bech, F.W.1    Jorgensen, S.T.2    Diderichsen, B.3    Karlstrom, O.H.4
  • 17
    • 14644444230 scopus 로고    scopus 로고
    • Obg/CgtA, a signalling protein that controls replication, translation and morphological development
    • Bénédicte, M. 2005. Obg/CgtA, a signalling protein that controls replication, translation and morphological development. Dev Cell 9:300-301.
    • (2005) Dev Cell , vol.9 , pp. 300-301
    • Bénédicte, M.1
  • 18
    • 33751075737 scopus 로고    scopus 로고
    • Cooperative and critical roles for both G domains in the GTPase activity and cellular function of ribosome-associated Escherichia coli EngA
    • Bharat, A., Jiang, M., Sullivan, S.M., Maddock, J.R., and Brown, E.D. 2006. Cooperative and critical roles for both G domains in the GTPase activity and cellular function of ribosome-associated Escherichia coli EngA. J Bacteriol 188:7992-7996.
    • (2006) J Bacteriol , vol.188 , pp. 7992-7996
    • Bharat, A.1    Jiang, M.2    Sullivan, S.M.3    Maddock, J.R.4    Brown, E.D.5
  • 19
    • 0033792046 scopus 로고    scopus 로고
    • Identification of loci essential for the growth of Helicobacter pylori under acidic conditions
    • Bijlsma, J.J., Lie, A.L.M., Nootenboom, I.C., Vandenbroucke-Grauls, C.M., and Kusters, J.G. 2000. Identification of loci essential for the growth of Helicobacter pylori under acidic conditions. J Infect Dis 182:1566-1569.
    • (2000) J Infect Dis , vol.182 , pp. 1566-1569
    • Bijlsma, J.J.1    Lie, A.L.M.2    Nootenboom, I.C.3    Vandenbroucke-Grauls, C.M.4    Kusters, J.G.5
  • 20
    • 0029111710 scopus 로고
    • X-ray crystallography shows that translational initiation factor IF3 consists of two compact alpha/beta domains linked by an alpha-helix
    • Biou, V., Shu, F., and Ramakrishnan, V. 1995. X-ray crystallography shows that translational initiation factor IF3 consists of two compact alpha/beta domains linked by an alpha-helix. EMBO J 14:4056-4064.
    • (1995) EMBO J , vol.14 , pp. 4056-4064
    • Biou, V.1    Shu, F.2    Ramakrishnan, V.3
  • 22
    • 0016611284 scopus 로고
    • Purification and properties of stringent factor
    • Block, R. and Haseltine, W. 1975. Purification and properties of stringent factor. J Biol Chem 250:1212-1217.
    • (1975) J Biol Chem , vol.250 , pp. 1212-1217
    • Block, R.1    Haseltine, W.2
  • 24
    • 0018901271 scopus 로고
    • The ribonuclease III site flanking 23S sequences in the 30S ribosomal precursor RNA of E. coli
    • Bram, R.J., Young, R.A., and Steitz, J.A. 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
  • 25
    • 0031953140 scopus 로고    scopus 로고
    • Cell cycle arrest in Era GTPase mutants: A potential growth rate-regulated checkpoint in Escherichia coli
    • Britton, R.A., Powell, B.S., Dasgupta, S., Sun, Q., Margolin, W., Lupski, J.R., and Court, D.L. 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, R.A.1    Powell, B.S.2    Dasgupta, S.3    Sun, Q.4    Margolin, W.5    Lupski, J.R.6    Court, D.L.7
  • 26
    • 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
  • 27
    • 0028238896 scopus 로고
    • Recognition of novel and divergent higher plant chloroplast ribosomal proteins by Escherichia coli ribosome during in vivo assembly
    • Bubunenko, M.G. and Subramanian, A.R. 1994. Recognition of novel and divergent higher plant chloroplast ribosomal proteins by Escherichia coli ribosome during in vivo assembly. J Biol Chem 269:18223-18231.
    • (1994) J Biol Chem , vol.269 , pp. 18223-18231
    • Bubunenko, M.G.1    Subramanian, A.R.2
  • 28
    • 0028074974 scopus 로고
    • Protein-protein recognition: Crystal structural analysis of a barnase-barstar complex at 2.0 Å resolution
    • Buckle, A., Schreiber, G., and Fersht, A. 1994. Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0 Å resolution. Biochemistry 33:8878-8889.
    • (1994) Biochemistry , vol.33 , pp. 8878-8889
    • Buckle, A.1    Schreiber, G.2    Fersht, A.3
  • 30
    • 0036849768 scopus 로고    scopus 로고
    • Structural and biochemical analysis of the Obg GTP binding protein
    • Buglino, J., Shen, V., Hakimian, P., and Lima, C.D. 2002. Structural and biochemical analysis of the Obg GTP binding protein. Structure 10:1581-1592.
    • (2002) Structure , vol.10 , pp. 1581-1592
    • Buglino, J.1    Shen, V.2    Hakimian, P.3    Lima, C.D.4
  • 31
    • 0031973622 scopus 로고    scopus 로고
    • RimM and RbfA are essential for efficient processing of 16S rRNA in Escherichia coli
    • Bylund, G., Wipemo, L., Lundberg, L., and Wikstrom, P. 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.1    Wipemo, L.2    Lundberg, L.3    Wikstrom, P.4
  • 32
    • 0030791574 scopus 로고    scopus 로고
    • A novel ribosome-associated protein is important for efficient translation in Escherichia coli
    • Bylund, G.O., Persson, B.C., Lundberg, L.A.C., and Wikstrom, P.M. 1997. A novel ribosome-associated protein is important for efficient translation in Escherichia coli. J Bacteriol 179:4567-4574.
    • (1997) J Bacteriol , vol.179 , pp. 4567-4574
    • Bylund, G.O.1    Persson, B.C.2    Lundberg, L.A.C.3    Wikstrom, P.M.4
  • 33
    • 0034685640 scopus 로고    scopus 로고
    • Translational defects of Escherichia coli mutants deficient in the Um(2552) 23S ribosomal RNA methyltransferase RrmJ/FtsJ
    • Caldas, T., Binet, E., Bouloc, P., and Richarme, G. 2000. Translational defects of Escherichia coli mutants deficient in the Um(2552) 23S ribosomal RNA methyltransferase RrmJ/FtsJ. J Biochem Biophys Res Commun 271:714-718.
    • (2000) J Biochem Biophys Res Commun , vol.271 , pp. 714-718
    • Caldas, T.1    Binet, E.2    Bouloc, P.3    Richarme, G.4
  • 34
    • 0034909325 scopus 로고    scopus 로고
    • Evolution of a molecular switch: Universal bacterial GTPases regulate ribosome function
    • Caldon, C.E., Yoong, P., and March, P.E. 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
  • 35
    • 4344605018 scopus 로고    scopus 로고
    • Thermus thermophilus L11 methyltransferase, PrmA, is dispensable for growth and preferentially modifies free ribosomal protein L11 prior to ribosome assembly
    • Cameron, D., Gregory, S., Thompson, J., Suh, M., Limbach, P., and Dahlberg, A. 2004. Thermus thermophilus L11 methyltransferase, PrmA, is dispensable for growth and preferentially modifies free ribosomal protein L11 prior to ribosome assembly. J Bacteriol 186:5819-5825.
    • (2004) J Bacteriol , vol.186 , pp. 5819-5825
    • Cameron, D.1    Gregory, S.2    Thompson, J.3    Suh, M.4    Limbach, P.5    Dahlberg, A.6
  • 36
    • 23644457992 scopus 로고    scopus 로고
    • Characterization of the Bacillus subtillis GTPase YloQ and its role in ribosome function
    • Campbell, T.L., Daigle, D.M., and Brown, E.D. 2005. Characterization of the Bacillus subtillis GTPase YloQ and its role in ribosome function. Biochem J 389:843-852.
    • (2005) Biochem J , vol.389 , pp. 843-852
    • Campbell, T.L.1    Daigle, D.M.2    Brown, E.D.3
  • 38
    • 2542557396 scopus 로고    scopus 로고
    • CsdA, a cold-shock RNA helicase from Escherichia coli, is involved in the biogenesis of 50S ribosomal subunit
    • Charollais, J., Dreyfus, M., and Iost, I. 2004. CsdA, a cold-shock RNA helicase from Escherichia coli, is involved in the biogenesis of 50S ribosomal subunit. Nucleic Acids Ress 32:2751-2759.
    • (2004) Nucleic Acids Ress , vol.32 , pp. 2751-2759
    • Charollais, J.1    Dreyfus, M.2    Iost, I.3
  • 39
    • 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., Pflieger, D., Vinh, J., Dreyfus, M., and Iost, I. 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
  • 40
    • 0031949801 scopus 로고    scopus 로고
    • The mediator for stringent control, ppGpp, binds to the beta-subunit of Escherichia coli RNA polymerase
    • Chatterji, D., Fujita, N., and Ishihama, A. 1998. The mediator for stringent control, ppGpp, binds to the beta-subunit of Escherichia coli RNA polymerase. Genes Cells 3:279-287.
    • (1998) Genes Cells , vol.3 , pp. 279-287
    • Chatterji, D.1    Fujita, N.2    Ishihama, A.3
  • 41
    • 0033587699 scopus 로고    scopus 로고
    • Crystal structure of ERA: A GTPase-dependent cell cycle regulator containing an RNA binding motif
    • Chen, X., Court, D., and Ji, X. 1999. Crystal structure of ERA: a GTPase-dependent cell cycle regulator containing an RNA binding motif. Proc Natl Acad Sci USA 96:8396-8401.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8396-8401
    • Chen, X.1    Court, D.2    Ji, X.3
  • 42
    • 0035807805 scopus 로고    scopus 로고
    • RelE, a global inhibitor of translation, is activated during nutritional stress
    • Christensen, S., Mikkelsen, M., Pedersen, K., and Gerdes, K. 2001. RelE, a global inhibitor of translation, is activated during nutritional stress. Proc Natl Acad Sci USA 98:14328-14333.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14328-14333
    • Christensen, S.1    Mikkelsen, M.2    Pedersen, K.3    Gerdes, K.4
  • 44
    • 33748414041 scopus 로고    scopus 로고
    • Non-ribosomal factors in ribosome subunit assembly are emerging targets for new antibacterial drugs
    • Comartin, D.J. and Brown, E.D. 2006. Non-ribosomal factors in ribosome subunit assembly are emerging targets for new antibacterial drugs. Curr Opin Pharmacol 6:453-458.
    • (2006) Curr Opin Pharmacol , vol.6 , pp. 453-458
    • Comartin, D.J.1    Brown, E.D.2
  • 45
    • 33748309126 scopus 로고    scopus 로고
    • Shutdown decay of mRNA
    • Condon, C. 2006. Shutdown decay of mRNA. Mol Microbiol 61:573-583.
    • (2006) Mol Microbiol , vol.61 , pp. 573-583
    • Condon, C.1
  • 46
    • 0344443255 scopus 로고    scopus 로고
    • Ribosomal protection proteins and their mechanism of tetracycline resistance
    • Connell, S.R., Tracz, D.M., Nierhaus, K.H., and Taylor, D.E. 2003a. Ribosomal protection proteins and their mechanism of tetracycline resistance. Antimicrob Agents Chemother 47:3675-3681.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 3675-3681
    • Connell, S.R.1    Tracz, D.M.2    Nierhaus, K.H.3    Taylor, D.E.4
  • 48
    • 0036035221 scopus 로고    scopus 로고
    • The tetracycline resistance protein Tet(O) perturbs the conformation of the ribosomal decoding centre
    • Connell, S.R., Trieber, C.A., Stelzl, U., Einfeldt, E., Taylor, D.E., and Nierhaus, K.H. 2002. The tetracycline resistance protein Tet(O) perturbs the conformation of the ribosomal decoding centre. Mol Microbiol 45:1463-1472.
    • (2002) Mol Microbiol , vol.45 , pp. 1463-1472
    • Connell, S.R.1    Trieber, C.A.2    Stelzl, U.3    Einfeldt, E.4    Taylor, D.E.5    Nierhaus, K.H.6
  • 49
    • 0033570135 scopus 로고    scopus 로고
    • A phylogenetic approach to target selection for structural genomics: Solution structure of YciH
    • Cort, J., Koonin, E., Bash, P., and Kennedy, M. 1999. A phylogenetic approach to target selection for structural genomics: solution structure of YciH. Nucleic Acids Res 27:4018-4027.
    • (1999) Nucleic Acids Res , vol.27 , pp. 4018-4027
    • Cort, J.1    Koonin, E.2    Bash, P.3    Kennedy, M.4
  • 50
    • 23644443534 scopus 로고    scopus 로고
    • The Obg subfamily of bacterial GTP-binding proteins: Essential proteins of largely unknown functions that are evolutionarily conserved from bacteria to humans
    • Czyz, A. and Wegrzyn, G. 2005. The Obg subfamily of bacterial GTP-binding proteins: essential proteins of largely unknown functions that are evolutionarily conserved from bacteria to humans. Acta Biochemica Polonica 52:35-43.
    • (2005) Acta Biochemica Polonica , vol.52 , pp. 35-43
    • Czyz, A.1    Wegrzyn, G.2
  • 51
    • 1342346614 scopus 로고    scopus 로고
    • Studies of the interaction of Escherichia coli YjeQ with the ribosome in vitro
    • Daigle, D.M. and Brown, E.D. 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
  • 52
    • 0037125960 scopus 로고    scopus 로고
    • YjeQ, an essential, conserved, uncharacterized protein from Escherichia coli, is an unusual GTPase with circularly permuted G-motifs and marked burst kinetics
    • Daigle, D.M., Rossi, L., Berghuis, A.M., Aravind, L., Koonin, E.V., and Brown, E.D. 2002. YjeQ, an essential, conserved, uncharacterized protein from Escherichia coli, is an unusual GTPase with circularly permuted G-motifs and marked burst kinetics. Biochemistry 41:11109-11117.
    • (2002) Biochemistry , vol.41 , pp. 11109-11117
    • Daigle, D.M.1    Rossi, L.2    Berghuis, A.M.3    Aravind, L.4    Koonin, E.V.5    Brown, E.D.6
  • 53
    • 0027273672 scopus 로고
    • A cold-sensitive mutation in 16S rRNA provides evidence for helical switching in ribosome assembly
    • Dammel, C.S. and Noller, H.F. 1993. A cold-sensitive mutation in 16S rRNA provides evidence for helical switching in ribosome assembly. Genes Dev 7:660-670.
    • (1993) Genes Dev , vol.7 , pp. 660-670
    • Dammel, C.S.1    Noller, H.F.2
  • 54
    • 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 Noller, H.F. 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
  • 55
    • 0032752483 scopus 로고    scopus 로고
    • A new essential gene of the 'minimal genome' affecting cell division
    • Dassain, M., Leroy, A., Colosetti, L., Carole, S., and Bouche, J.P. 1999. A new essential gene of the 'minimal genome' affecting cell division. Biochimie 81:889-895.
    • (1999) Biochimie , vol.81 , pp. 889-895
    • Dassain, M.1    Leroy, A.2    Colosetti, L.3    Carole, S.4    Bouche, J.P.5
  • 56
    • 12844288568 scopus 로고    scopus 로고
    • The yeast GTPase Mtg2p is required for mitochondrial translation and partially suppresses an rRNA methyltransferase mutant, mrm2
    • Datta, K., Fuentes, J.L., and Maddock, J.R. 2005. The yeast GTPase Mtg2p is required for mitochondrial translation and partially suppresses an rRNA methyltransferase mutant, mrm2. Mol Biol Cell 16:954-963.
    • (2005) Mol Biol Cell , vol.16 , pp. 954-963
    • Datta, K.1    Fuentes, J.L.2    Maddock, J.R.3
  • 57
    • 0036629250 scopus 로고    scopus 로고
    • rRNA modifications and ribosome function
    • Decatur, W. and Fournier, M. 2002. rRNA modifications and ribosome function. TIBS 27:344-351.
    • (2002) TIBS , vol.27 , pp. 344-351
    • Decatur, W.1    Fournier, M.2
  • 58
    • 0035163770 scopus 로고    scopus 로고
    • Identification and site of action of the remaining four putative pseudouridine synthases in Escherichia coli
    • Del Campo, M., Kaya, Y., and Ofengand, J. 2001. Identification and site of action of the remaining four putative pseudouridine synthases in Escherichia coli. RNA 7:1603-1615.
    • (2001) RNA , vol.7 , pp. 1603-1615
    • Del Campo, M.1    Kaya, Y.2    Ofengand, J.3
  • 59
    • 0035193362 scopus 로고    scopus 로고
    • Exoribonucleases and their multiple roles in RNA metabolism
    • Deutscher, M.P. and Li, Z. 2001. Exoribonucleases and their multiple roles in RNA metabolism. Prog Nucleic Acid Res Mol Biol 66:67-105.
    • (2001) Prog Nucleic Acid Res Mol Biol , vol.66 , pp. 67-105
    • Deutscher, M.P.1    Li, Z.2
  • 60
    • 8844280894 scopus 로고    scopus 로고
    • Ribosome synthesis meets the cell cycle
    • Dez, C. and Tollervey, D. 2004. Ribosome synthesis meets the cell cycle. Curr Opin Microbiol 7:631-637.
    • (2004) Curr Opin Microbiol , vol.7 , pp. 631-637
    • Dez, C.1    Tollervey, D.2
  • 61
    • 0022518007 scopus 로고
    • lep operon proximal gene is not required for growth or secretion by Escherichia coli
    • Dibb, N.J. and Wolfe, P.B. 1986. lep operon proximal gene is not required for growth or secretion by Escherichia coli. J Bacteriol 166:83-87.
    • (1986) J Bacteriol , vol.166 , pp. 83-87
    • Dibb, N.J.1    Wolfe, P.B.2
  • 62
    • 24944586007 scopus 로고    scopus 로고
    • Deacylated tRNA is released from the E site upon A site occupation but before GTP is hydrolyzed by EF-Tu
    • Dinos, G., Kalpaxis, D.L., Wilson, D.N., and Nierhaus, K.H. 2005. Deacylated tRNA is released from the E site upon A site occupation but before GTP is hydrolyzed by EF-Tu. Nucleic Acids Res 33:5291-5296.
    • (2005) Nucleic Acids Res , vol.33 , pp. 5291-5296
    • Dinos, G.1    Kalpaxis, D.L.2    Wilson, D.N.3    Nierhaus, K.H.4
  • 63
    • 27244434760 scopus 로고    scopus 로고
    • The ribosomal subunit assembly line
    • Dlakic, M. 2005. The ribosomal subunit assembly line. Genome Biol 6:234.
    • (2005) Genome Biol , vol.6 , pp. 234
    • Dlakic, M.1
  • 64
    • 1842471295 scopus 로고    scopus 로고
    • The tylosin-resistance methyltransferase RlmA(II) (TlrB) modifies the N-1 position of 23S rRNA nucleotide G748
    • Douthwaite, S., Crain, P., Liu, M., and Poehlsgaard, J. 2004. The tylosin-resistance methyltransferase RlmA(II) (TlrB) modifies the N-1 position of 23S rRNA nucleotide G748. J Mol Biol 337:1073-1077.
    • (2004) J Mol Biol , vol.337 , pp. 1073-1077
    • Douthwaite, S.1    Crain, P.2    Liu, M.3    Poehlsgaard, J.4
  • 65
    • 27744513696 scopus 로고    scopus 로고
    • The activity of ribosome modulation factor during growth of Escherichia coli under acidic conditions
    • El-Sharoud, W.M. and Niven, G.W. 2005. The activity of ribosome modulation factor during growth of Escherichia coli under acidic conditions. Arch Microbiol 184:18-24.
    • (2005) Arch Microbiol , vol.184 , pp. 18-24
    • El-Sharoud, W.M.1    Niven, G.W.2
  • 66
    • 33846318176 scopus 로고    scopus 로고
    • The influence of ribosome modulation factor on the survival of stationary-phase Escherichia coli during acid stress
    • El-Sharoud, W.M. and Niven, G.W. 2007. The influence of ribosome modulation factor on the survival of stationary-phase Escherichia coli during acid stress. Microbiology 153:247-253.
    • (2007) Microbiology , vol.153 , pp. 247-253
    • El-Sharoud, W.M.1    Niven, G.W.2
  • 67
    • 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., Sbai, M., and Alix, J.H. 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
  • 70
    • 0033522507 scopus 로고    scopus 로고
    • Structure and interactions of the translation initiation factor eIF1
    • Fletcher, C.M., Pestova, T.V., Hellen, C.U.T., and Wagner, G. 1999. Structure and interactions of the translation initiation factor eIF1. EMBO J 18:2631-2637.
    • (1999) EMBO J , vol.18 , pp. 2631-2637
    • Fletcher, C.M.1    Pestova, T.V.2    Hellen, C.U.T.3    Wagner, G.4
  • 71
    • 0016299779 scopus 로고
    • A new relaxed mutant of Escherichia coli with an altered 50S ribosomal subunit
    • Friesen, J.D., Fiil, N.P., Parker, J.M., and Haseltine, W.A. 1974. A new relaxed mutant of Escherichia coli with an altered 50S ribosomal subunit. Proc Natl Acad Sci USA 71:3465-3469.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 3465-3469
    • Friesen, J.D.1    Fiil, N.P.2    Parker, J.M.3    Haseltine, W.A.4
  • 73
    • 0033838039 scopus 로고    scopus 로고
    • Peptide bond synthesis: Function of the efp gene product
    • Ganoza, M.C. and Aoki, H. 2000. Peptide bond synthesis: function of the efp gene product. Biol Chem 381:553-559.
    • (2000) Biol Chem , vol.381 , pp. 553-559
    • Ganoza, M.C.1    Aoki, H.2
  • 74
    • 0036715039 scopus 로고    scopus 로고
    • Evolutionary conservation of reactions in translation
    • Ganoza, M.C., Kiel, M.C., and Aoki, H. 2002. Evolutionary conservation of reactions in translation. Microbiol Mol Biol Rev 66:460-485.
    • (2002) Microbiol Mol Biol Rev , vol.66 , pp. 460-485
    • Ganoza, M.C.1    Kiel, M.C.2    Aoki, H.3
  • 75
    • 0021925965 scopus 로고
    • Stimulation of peptidyltransferase reactions by a soluble protein
    • Ganoza, M.C., Zahid, N., and Baxter, R.M. 1985. Stimulation of peptidyltransferase reactions by a soluble protein. Eur J Biochem 146:287-294.
    • (1985) Eur J Biochem , vol.146 , pp. 287-294
    • Ganoza, M.C.1    Zahid, N.2    Baxter, R.M.3
  • 76
    • 34250380391 scopus 로고    scopus 로고
    • Scaffolding as an organizing principle in trans-translation: The roles of small protein B and ribosomal protein S1
    • Epub
    • Gillet, R., Kaur, S., Li, W., Hallier, M., Felden, B., and Frank, J. 2007. Scaffolding as an organizing principle in trans-translation: The roles of small protein B and ribosomal protein S1. J Biol Chem. Epub.
    • (2007) J Biol Chem
    • Gillet, R.1    Kaur, S.2    Li, W.3    Hallier, M.4    Felden, B.5    Frank, J.6
  • 77
    • 0016704154 scopus 로고
    • The 30S ribosomal precursor RNA from E. coli. A primary transcript containing 23S, 16S, and 5S sequences
    • Ginsburg, D. and Steitz, J.A. 1975. The 30S ribosomal precursor RNA from E. coli. A primary transcript containing 23S, 16S, and 5S sequences. J Biol Chem 250:5647-5654.
    • (1975) J Biol Chem , vol.250 , pp. 5647-5654
    • Ginsburg, D.1    Steitz, J.A.2
  • 78
    • 0016824833 scopus 로고
    • Identification of a soluble protein that stimulates peptide bond synthesis
    • Glick, B.R. and Ganoza, M.C. 1975. Identification of a soluble protein that stimulates peptide bond synthesis. Proc Natl Acad. Sci USA 72:4257-4260.
    • (1975) Proc Natl Acad. Sci USA , vol.72 , pp. 4257-4260
    • Glick, B.R.1    Ganoza, M.C.2
  • 79
    • 0017028286 scopus 로고
    • Characterization and site of action of a soluble protein that stimulates peptide-bond synthesis
    • Glick, B.R. and Ganoza, M.C. 1976. Characterization and site of action of a soluble protein that stimulates peptide-bond synthesis. Eur J Biochem 71:483-491.
    • (1976) Eur J Biochem , vol.71 , pp. 483-491
    • Glick, B.R.1    Ganoza, M.C.2
  • 80
    • 0031816179 scopus 로고    scopus 로고
    • The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family
    • Gotfredsen, M. and Gerdes, K. 1998. The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family. Mol Microbiol 29:1065-1076.
    • (1998) Mol Microbiol , vol.29 , pp. 1065-1076
    • Gotfredsen, M.1    Gerdes, K.2
  • 81
    • 2342447390 scopus 로고    scopus 로고
    • Structural inhibition of the colicin D tRNase by the tRNA-mimicking immunity protein
    • Graille, M., Mora, L., Buckingham, R., Van Tilbeurgh, H., and De Zamaroczy, M. 2004. Structural inhibition of the colicin D tRNase by the tRNA-mimicking immunity protein. EMBO J 23:1474-1482.
    • (2004) EMBO J , vol.23 , pp. 1474-1482
    • Graille, M.1    Mora, L.2    Buckingham, R.3    Van Tilbeurgh, H.4    De Zamaroczy, M.5
  • 82
    • 0025365804 scopus 로고
    • Initiation of messenger-RNA translation in prokaryotes
    • Gualerzi, C.O. and Pon, C.L. 1990. Initiation of messenger-RNA translation in prokaryotes. Biochemistry 29:5881-5889.
    • (1990) Biochemistry , vol.29 , pp. 5881-5889
    • Gualerzi, C.O.1    Pon, C.L.2
  • 83
    • 22244456758 scopus 로고    scopus 로고
    • The pseudouridine synthase RluD is required for normal ribosome assembly and function in Escherichia coli
    • Gutgsell, N.S., Deutscher, M.P., and Ofengand, J. 2005. The pseudouridine synthase 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
  • 84
    • 1342302787 scopus 로고    scopus 로고
    • Dial tm for rescue: TmRNA engages ribosomes stalled on defective mRNAs
    • Haebel, P.W., Gutmann, S., and Ban, N. 2004. Dial tm for rescue: tmRNA engages ribosomes stalled on defective mRNAs. Curr Opin Struct Biol 14:58-65.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 58-65
    • Haebel, P.W.1    Gutmann, S.2    Ban, N.3
  • 85
    • 0036828880 scopus 로고    scopus 로고
    • Active site in RrmJ, a heat shock-induced methyltransferase
    • Hager, J., Staker, B.L., Bügl, H., and Jakob, U. 2002. Active site in RrmJ, a heat shock-induced methyltransferase. J Biol Chem 277:41978-41986.
    • (2002) J Biol Chem , vol.277 , pp. 41978-41986
    • Hager, J.1    Staker, B.L.2    Bügl, H.3    Jakob, U.4
  • 89
    • 0007825206 scopus 로고
    • Synthesis of guanosine tetraand pentaphosphate requires the presence of a codon-specific, uncharged transfer ribonucleic acid in the acceptor site of ribosomes
    • Haseltine, W.A. and Block, R. 1973. Synthesis of guanosine tetraand pentaphosphate requires the presence of a codon-specific, uncharged transfer ribonucleic acid in the acceptor site of ribosomes. Proc Natl Acad Sci USA 70:1564-1568.
    • (1973) Proc Natl Acad Sci USA , vol.70 , pp. 1564-1568
    • Haseltine, W.A.1    Block, R.2
  • 90
    • 0015515019 scopus 로고
    • MSI and MSII made on ribosome in idling step of protein synthesis
    • Haseltine, W.A., Block, R., Gilbert, W., and Weber, K. 1972. MSI and MSII made on ribosome in idling step of protein synthesis. Nature 238:381-384.
    • (1972) Nature , vol.238 , pp. 381-384
    • Haseltine, W.A.1    Block, R.2    Gilbert, W.3    Weber, K.4
  • 91
    • 0015121549 scopus 로고
    • Change in methylation of 16S ribosomal RNA associated with mutation to kasugamycin resistance in Escherichia coli
    • Helser, T.L., Davies, J.E., and Dahlberg, J.E. 1971. Change in methylation of 16S ribosomal RNA associated with mutation to kasugamycin resistance in Escherichia coli. Nat New Biol 233:12-14.
    • (1971) Nat New Biol , vol.233 , pp. 12-14
    • Helser, T.L.1    Davies, J.E.2    Dahlberg, J.E.3
  • 92
    • 0015494418 scopus 로고
    • Mechanism of kasugamycin resistance in Escherichia coli
    • Helser, T.L., Davies, J.E., and Dahlberg, J.E. 1972. Mechanism of kasugamycin resistance in Escherichia coli. Nat New Biol 235:6-9.
    • (1972) Nat New Biol , vol.235 , pp. 6-9
    • Helser, T.L.1    Davies, J.E.2    Dahlberg, J.E.3
  • 94
    • 33645231008 scopus 로고    scopus 로고
    • Mechanism and regulation of protein synthesis initiation in eukaryotes
    • Nierhaus, K.H. and Wilson, D.N. eds. WILEY-VCH Verlag GmbH&Co, Weinheim, Germany
    • Hinnebusch, A.G., Dever, T.E., and Sonenberg, N. 2004. Mechanism and regulation of protein synthesis initiation in eukaryotes. In Protein synthesis and ribosome structure: translating the genome. pp. 241-322. Nierhaus, K.H. and Wilson, D.N. eds. WILEY-VCH Verlag GmbH&Co., Weinheim, Germany.
    • (2004) Protein synthesis and ribosome structure: Translating the genome , pp. 241-322
    • Hinnebusch, A.G.1    Dever, T.E.2    Sonenberg, N.3
  • 96
    • 0037459257 scopus 로고    scopus 로고
    • Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation protein from Escherichia coli
    • Huang, Y., Swapna, G., Rajan, P., Ke, H., Xia, B., Shukla, K., Inouye, M., and Montelione, G. 2003. Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation protein from Escherichia coli. J Mol Biol 327:521-536.
    • (2003) J Mol Biol , vol.327 , pp. 521-536
    • Huang, Y.1    Swapna, G.2    Rajan, P.3    Ke, H.4    Xia, B.5    Shukla, K.6    Inouye, M.7    Montelione, G.8
  • 97
    • 33748486487 scopus 로고    scopus 로고
    • The tandem GTPase, Der, is essential for the biogenesis of 50S ribosomal subunits in Escherichia coli
    • Hwang, J. and Inouye, M. 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
  • 98
    • 33745757322 scopus 로고    scopus 로고
    • Era and RbfA have overlapping function in ribosome biogenesis in Escherichia coli
    • Inoue, K., Chen, J., and Inouye, M. 2006. Era and RbfA have overlapping function in ribosome biogenesis in Escherichia coli. J Mol Microbiol Biotechnol 11:41-52.
    • (2006) J Mol Microbiol Biotechnol , vol.11 , pp. 41-52
    • Inoue, K.1    Chen, J.2    Inouye, M.3
  • 99
    • 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., Alsina, J., Chen, J., and Inouye, M. 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
  • 100
    • 33749125440 scopus 로고    scopus 로고
    • DEAD-box RNA helicases in Escherichia coli
    • Iost, I. and Dreyfus, M. 2006. DEAD-box RNA helicases in Escherichia coli. Nucleic Acids Res 34:4189-4197.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4189-4197
    • Iost, I.1    Dreyfus, M.2
  • 101
    • 84955097637 scopus 로고    scopus 로고
    • Regulation of ribosome biosynthesis in Escherichia coli
    • Nierhaus, K.H. and Wilson, D.N. eds. WILEY-VCH Verlag GmbH&Co, Weinheim, Germany
    • Iskakova, M., Connell, S.R., and Nierhaus, K.H. 2004. Regulation of ribosome biosynthesis in Escherichia coli. In Protein synthesis and ribosome structure: translating the genome. pp. 429-448. Nierhaus, K.H. and Wilson, D.N. eds. WILEY-VCH Verlag GmbH&Co., Weinheim, Germany.
    • (2004) Protein synthesis and ribosome structure: Translating the genome , pp. 429-448
    • Iskakova, M.1    Connell, S.R.2    Nierhaus, K.H.3
  • 102
    • 0034859791 scopus 로고    scopus 로고
    • Expression of ribosome modulation factor (RMF) in Escherichia coli requires ppGpp
    • Izutsu, K., Wada, A., and Wada, C. 2001a. Expression of ribosome modulation factor (RMF) in Escherichia coli requires ppGpp. Genes Cells 6:665-676.
    • (2001) Genes Cells , vol.6 , pp. 665-676
    • Izutsu, K.1    Wada, A.2    Wada, C.3
  • 103
    • 0035053696 scopus 로고    scopus 로고
    • Escherichia coli ribosome-associated protein SRA, whose copy number increases during stationary phase
    • Izutsu, K., Wada, C., Komine, Y., Sako, T., Ueguchi, C., Nakura, S., and Wada, A. 2001b. Escherichia coli ribosome-associated protein SRA, whose copy number increases during stationary phase. J Bacteriol 183:2765-2773.
    • (2001) J Bacteriol , vol.183 , pp. 2765-2773
    • Izutsu, K.1    Wada, C.2    Komine, Y.3    Sako, T.4    Ueguchi, C.5    Nakura, S.6    Wada, A.7
  • 105
    • 0042858143 scopus 로고    scopus 로고
    • The NOG1 GTP-binding protein is required for biogenesis of the 60S ribosomal subunit
    • Jensen, B.C., Wang, Q., Kifer, C.T., and Parsons, M. 2003. The NOG1 GTP-binding protein is required for biogenesis of the 60S ribosomal subunit. J Biol Chem 278:32204-32211.
    • (2003) J Biol Chem , vol.278 , pp. 32204-32211
    • Jensen, B.C.1    Wang, Q.2    Kifer, C.T.3    Parsons, M.4
  • 106
    • 13444252553 scopus 로고    scopus 로고
    • Characterization of the tRNA and ribosome-dependent pppGpp-synthesis by recombinant stringent factor from Escherichia coli
    • Jenvert, R. and Schiavone, L. 2005. Characterization of the tRNA and ribosome-dependent pppGpp-synthesis by recombinant stringent factor from Escherichia coli. FEBS J 272:685-695.
    • (2005) FEBS J , vol.272 , pp. 685-695
    • Jenvert, R.1    Schiavone, L.2
  • 107
  • 108
    • 0030043216 scopus 로고    scopus 로고
    • Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli
    • Jones, P.G., Mitta, M., Kim, Y., Jiang, W.N., and Inouye, M. 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.N.4    Inouye, M.5
  • 109
    • 2342553864 scopus 로고    scopus 로고
    • Temperature sentivitiy caused by mutant release factor 1 is suppressed by mutations that affect 16S rRNA maturation
    • Kaczanowska, M. and Rydén-Aulin, M. 2004. Temperature sentivitiy 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    Rydén-Aulin, M.2
  • 110
    • 13444259766 scopus 로고    scopus 로고
    • The YrdC protein - a putative ribosome maturation factor
    • Kaczanowska, M. and Rydén-Aulin, M. 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
  • 111
    • 0038316568 scopus 로고    scopus 로고
    • The putative GTPases Nog1p and Lsg1p are required for 60S ribosomal subunit biogenesis and are localized to the nucleus and cytoplasm, respectively
    • Kallstrom, G., Hedges, J., and Johnson, A. 2003. The putative GTPases Nog1p and Lsg1p are required for 60S ribosomal subunit biogenesis and are localized to the nucleus and cytoplasm, respectively. Mol Biol Cell 23:4344-4355.
    • (2003) Mol Biol Cell , vol.23 , pp. 4344-4355
    • Kallstrom, G.1    Hedges, J.2    Johnson, A.3
  • 112
    • 27444442034 scopus 로고    scopus 로고
    • YxiN is a modular protein combining a DExD/H core and a specific RNA-binding domain
    • Karginov, F., Caruthers, J., Hu, Y., McKay, D., and Uhlenbeck, O. 2005. YxiN is a modular protein combining a DExD/H core and a specific RNA-binding domain. J Biol Chem 280:35499-35505.
    • (2005) J Biol Chem , vol.280 , pp. 35499-35505
    • Karginov, F.1    Caruthers, J.2    Hu, Y.3    McKay, D.4    Uhlenbeck, O.5
  • 113
    • 0345465673 scopus 로고    scopus 로고
    • SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA)
    • Karzai, A.W., Susskind, M.M., and Sauer, R.T. 1999. SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA). EMBO J 18:3793-3799.
    • (1999) EMBO J , vol.18 , pp. 3793-3799
    • Karzai, A.W.1    Susskind, M.M.2    Sauer, R.T.3
  • 114
    • 23744453392 scopus 로고    scopus 로고
    • A new mechanism for chloramphenicol, florfenicol and clindamycin resistance: Methylation of 23S ribosomal RNA at A2503
    • Kehrenberg, C., Schwarz, S., Jacobsen, L., Hansen, L., and Vester, B. 2005. A new mechanism for chloramphenicol, florfenicol and clindamycin resistance: methylation of 23S ribosomal RNA at A2503. Mol. Microbiol. 57:1064-1073.
    • (2005) Mol. Microbiol , vol.57 , pp. 1064-1073
    • Kehrenberg, C.1    Schwarz, S.2    Jacobsen, L.3    Hansen, L.4    Vester, B.5
  • 115
    • 0033451909 scopus 로고    scopus 로고
    • Identification of a ribosomal ATPase in Escherichia coli cells
    • Kiel, M.C., Aoki, H., and Ganoza, M.C. 1999. Identification of a ribosomal ATPase in Escherichia coli cells. Biochemie 81:1097-1108.
    • (1999) Biochemie , vol.81 , pp. 1097-1108
    • Kiel, M.C.1    Aoki, H.2    Ganoza, M.C.3
  • 116
    • 0034817912 scopus 로고    scopus 로고
    • Functional interactions of an Escherichia coli ribosomal ATPase
    • Kiel, M.C. and Ganoza, M.C. 2001. Functional interactions of an Escherichia coli ribosomal ATPase. Eur J Biochem 268:278-286.
    • (2001) Eur J Biochem , vol.268 , pp. 278-286
    • Kiel, M.C.1    Ganoza, M.C.2
  • 117
    • 0032167995 scopus 로고    scopus 로고
    • Crystal structures of eukaryotic translation initiation factor 5A from Methanococcus jannaschii at 1.8 Å resolution
    • Kim, K.K., Hung, L.W., Yokota, H., Kim, R., and Kim, S.H. 1998. Crystal structures of eukaryotic translation initiation factor 5A from Methanococcus jannaschii at 1.8 Å resolution. Proc Natl Acad Sci USA 95:10419-10424.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10419-10424
    • Kim, K.K.1    Hung, L.W.2    Yokota, H.3    Kim, R.4    Kim, S.H.5
  • 118
    • 0028845118 scopus 로고
    • GUF1, a gene encoding a novel evolutionarily conserved GTPase in budding yeast
    • Kiser, G.L. and Weinert, T.A. 1995. GUF1, a gene encoding a novel evolutionarily conserved GTPase in budding yeast. Yeast 11:1311-1316.
    • (1995) Yeast , vol.11 , pp. 1311-1316
    • Kiser, G.L.1    Weinert, T.A.2
  • 120
    • 0034651522 scopus 로고    scopus 로고
    • Hsp15: A ribosome-associated heat shock protein
    • Korber, P., Stahl, J.M., Nierhaus, K.H., and Bardwell, J.C. 2000. Hsp15: a ribosome-associated heat shock protein. EMBO J 19:741-748.
    • (2000) EMBO J , vol.19 , pp. 741-748
    • Korber, P.1    Stahl, J.M.2    Nierhaus, K.H.3    Bardwell, J.C.4
  • 122
    • 0031915895 scopus 로고    scopus 로고
    • Universally conserved translation initiation factors
    • Kyrpides, N.C. and Woese, C.R. 1998. Universally conserved translation initiation factors. Proc Natl Acad Sci USA 95:224-228.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 224-228
    • Kyrpides, N.C.1    Woese, C.R.2
  • 124
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe, D.D., Wolf, Y.I., Koonin, E.V., and Aravind, L. 2002. Classification and evolution of P-loop GTPases and related ATPases. J Mol Biol 15:41-72.
    • (2002) J Mol Biol , vol.15 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 125
    • 0027120825 scopus 로고
    • Cold sensitive growth and decreased GTP-hydrolytic activity from substitution of Pro17 for Val in Era, an essential Escherichia coli GTPase
    • Lerner, C.G., Sood, P., Ahnn, J., and Inouye, M. 1992. Cold sensitive growth and decreased GTP-hydrolytic activity from substitution of Pro17 for Val in Era, an essential Escherichia coli GTPase. FEMS Microbiol Lett 74:137-142.
    • (1992) FEMS Microbiol Lett , vol.74 , pp. 137-142
    • Lerner, C.G.1    Sood, P.2    Ahnn, J.3    Inouye, M.4
  • 127
    • 33750290824 scopus 로고    scopus 로고
    • Identification of Escherichia coli m(2)G methyltransferases: I. The ycbY Gene encodes a methyltransferase specific for G2445 of the 23S rRNA
    • Lesnyak, D., Sergiev, P., Bogdanov, A., and Dontsova, O. 2006. Identification of Escherichia coli m(2)G 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.1    Sergiev, P.2    Bogdanov, A.3    Dontsova, O.4
  • 128
    • 0027305857 scopus 로고
    • Coupling of rRNA transcription and ribosomal assembly in vivo - formation of active ribosomal subunits in Escherichia coli requires transcription of rRNA genes by host RNA polymerase which cannot be replaced by bacteriophage-T7 RNA polymerase
    • Lewicki, B.T., Margus, T., Remme, J., and Nierhaus, K.H. 1993. Coupling of rRNA transcription and ribosomal assembly in vivo - formation of active ribosomal subunits in Escherichia coli requires transcription of rRNA genes by host RNA polymerase which cannot be replaced by bacteriophage-T7 RNA polymerase. J Mol Biol 231:581-593.
    • (1993) J Mol Biol , vol.231 , pp. 581-593
    • Lewicki, B.T.1    Margus, T.2    Remme, J.3    Nierhaus, K.H.4
  • 130
    • 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., Pandit, S., and Deutscher, M.P. 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
  • 131
    • 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 Remme, J. 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
  • 132
    • 0032861460 scopus 로고    scopus 로고
    • The Caulobacter crescentus CgtA protein displays unsual guanine nucleotide binding and exchange properties
    • Lin, B., Covalle, K.L., and Maddock, J.R. 1999. The Caulobacter crescentus CgtA protein displays unsual guanine nucleotide binding and exchange properties. J Bacteriol 181:5825-5832.
    • (1999) J Bacteriol , vol.181 , pp. 5825-5832
    • Lin, B.1    Covalle, K.L.2    Maddock, J.R.3
  • 133
    • 0346024113 scopus 로고    scopus 로고
    • The Caulobacter crescentus CgtAC protein cosediments with the free 50S ribosomal subunit
    • Lin, B., Thayer, D.A., andMaddock, J.R. 2004. The Caulobacter crescentus CgtAC protein cosediments with the free 50S ribosomal subunit. J Bacteriol 186:481-489.
    • (2004) J Bacteriol , vol.186 , pp. 481-489
    • Lin, B.1    Thayer, D.A.2    andMaddock, J.R.3
  • 134
    • 0015894763 scopus 로고
    • Two new ribosomal precursor particles in E. coli
    • Lindahl, L. 1973. Two new ribosomal precursor particles in E. coli. Nat New Biol 243:170-172.
    • (1973) Nat New Biol , vol.243 , pp. 170-172
    • Lindahl, L.1
  • 135
    • 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
  • 136
    • 7044262105 scopus 로고    scopus 로고
    • Methylation of 23S rRNA nucleotide G745 is a secondary function of the RlmAI methyltransferase
    • Liu, M., Novotny, G.W., and Douthwaite, S. 2004. Methylation of 23S rRNA nucleotide G745 is a secondary function of the RlmAI methyltransferase. RNA 10:1713-1720.
    • (2004) RNA , vol.10 , pp. 1713-1720
    • Liu, M.1    Novotny, G.W.2    Douthwaite, S.3
  • 137
    • 33745599646 scopus 로고    scopus 로고
    • The Cfr rRNA methyltransferase confers resistance to phenicols, lincosamides, oxazolidinones, pleuromutilins, and streptogramin A antibiotics
    • Long, K., Poehlsgaard, J., Kehrenberg, C., Schwarz, S., and Vester, B. 2006. The Cfr rRNA methyltransferase confers resistance to phenicols, lincosamides, oxazolidinones, pleuromutilins, and streptogramin A antibiotics. Antimicrob Agents Chemother 50:2500-2505.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 2500-2505
    • Long, K.1    Poehlsgaard, J.2    Kehrenberg, C.3    Schwarz, S.4    Vester, B.5
  • 138
    • 7044240796 scopus 로고    scopus 로고
    • The PRC-barrel domain of the ribosome maturation protein RimM mediates binding to ribosomal protein S19 in the 30S ribosomal subunits
    • Lövgren, J., Bylund, G., Srivastava, M., Lundberg, L., Persson, O., Wingsle, G., and Wikström, P. 2004. The PRC-barrel domain of the ribosome maturation protein RimM mediates binding to ribosomal protein S19 in the 30S ribosomal subunits. RNA 10:1798-1812.
    • (2004) RNA , vol.10 , pp. 1798-1812
    • Lövgren, J.1    Bylund, G.2    Srivastava, M.3    Lundberg, L.4    Persson, O.5    Wingsle, G.6    Wikström, P.7
  • 139
    • 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 Inouye, M. 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
  • 140
    • 0027967867 scopus 로고
    • The function of the hypusine-containing proteins of yeast and other eukaryotes is well conserved
    • Magdolen, V., Klier, H., Wohl, T., Klink, F., Hirt, H., Hauber, J., and Lottspeich, F. 1994. The function of the hypusine-containing proteins of yeast and other eukaryotes is well conserved. Mol Gen Genet 244:646-652.
    • (1994) Mol Gen Genet , vol.244 , pp. 646-652
    • Magdolen, V.1    Klier, H.2    Wohl, T.3    Klink, F.4    Hirt, H.5    Hauber, J.6    Lottspeich, F.7
  • 141
    • 0036342369 scopus 로고    scopus 로고
    • The DnaK chaperone system facilitates 30S ribosomal subunit assembly
    • Maki, J.A., Schnobrich, D.J., and Culver, G.M. 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
  • 142
    • 0034489577 scopus 로고    scopus 로고
    • Two proteins, YfiA and YhbH, associated with resting ribosomes in stationary phase
    • Maki, Y., Yoshida, H., and Wada, A. 2000. Two proteins, YfiA and YhbH, associated with resting ribosomes in stationary phase. Escherichia coli Genes Cells 5:965-974.
    • (2000) Escherichia coli Genes Cells , vol.5 , pp. 965-974
    • Maki, Y.1    Yoshida, H.2    Wada, A.3
  • 143
    • 33846887420 scopus 로고    scopus 로고
    • Phylogenetic distribution of translational GTPases in bacteria
    • Margus, T., Remm, M., and Tenson, T. 2007. Phylogenetic distribution of translational GTPases in bacteria. BMC Genomics 8:15.
    • (2007) BMC Genomics , vol.8 , pp. 15
    • Margus, T.1    Remm, M.2    Tenson, T.3
  • 144
    • 0027522090 scopus 로고
    • chpA and chpB, Escherichia coli chromosomal homologs of the pem locus responsible for stable maintenance of plasmid R100
    • Masuda, Y., Miyakawa, K., Nishimura, Y., and Ohtsubo, E. 1993. chpA and chpB, Escherichia coli chromosomal homologs of the pem locus responsible for stable maintenance of plasmid R100. J Bacteriol 175:6850-6856.
    • (1993) J Bacteriol , vol.175 , pp. 6850-6856
    • Masuda, Y.1    Miyakawa, K.2    Nishimura, Y.3    Ohtsubo, E.4
  • 145
    • 33646371247 scopus 로고    scopus 로고
    • The GTP-binding protein YlqF participates in the late step of 50S ribosomal subunit assembly in Bacillus subtilis
    • Matsuo, Y., Morimoto, T., Kuwano, M., Loh, P.C., Oshima, T., and Ogasawara, N. 2006. The GTP-binding protein YlqF participates in the late step of 50S ribosomal subunit assembly in Bacillus subtilis. J Biol Chem 281:8110-8117.
    • (2006) J Biol Chem , vol.281 , pp. 8110-8117
    • Matsuo, Y.1    Morimoto, T.2    Kuwano, M.3    Loh, P.C.4    Oshima, T.5    Ogasawara, N.6
  • 146
    • 13444266430 scopus 로고    scopus 로고
    • The small subunit rRNA modification database
    • McCloskey, J.A. and Rozenski, J. 2005. The small subunit rRNA modification database. Nucleic Acids Res 33:D135-D138.
    • (2005) Nucleic Acids Res , vol.33
    • McCloskey, J.A.1    Rozenski, J.2
  • 147
    • 0035476599 scopus 로고    scopus 로고
    • Methylation of the nucleobases in RNA oligonucleotides mediates duplex-hairpin conversion
    • Micura, R., Pils, W., Hobartner, C., Grubmayr, K., Ebert, M., and Jaun, B. 2001. Methylation of the nucleobases in RNA oligonucleotides mediates duplex-hairpin conversion. Nucleic Acids Res 29:3997-4005.
    • (2001) Nucleic Acids Res , vol.29 , pp. 3997-4005
    • Micura, R.1    Pils, W.2    Hobartner, C.3    Grubmayr, K.4    Ebert, M.5    Jaun, B.6
  • 148
    • 0036855348 scopus 로고    scopus 로고
    • Six GTP-binding proteins of the Era/Obg family are essential for cell growth in Bacillus subtilis
    • Morimoto, T., Loh, P., Hirai, T., Asai, K., Kobayashi, K., Moriya, S., and Ogasawara, N. 2002. Six GTP-binding proteins of the Era/Obg family are essential for cell growth in Bacillus subtilis. Microbiology 148:3539-3552.
    • (2002) Microbiology , vol.148 , pp. 3539-3552
    • Morimoto, T.1    Loh, P.2    Hirai, T.3    Asai, K.4    Kobayashi, K.5    Moriya, S.6    Ogasawara, N.7
  • 149
    • 33747584905 scopus 로고    scopus 로고
    • The essential GTPase YphC displays a major domain rearrangement associated with nucleotide binding
    • Muench, S.P., Xu, L., Sedelnikova, S.E., and Rice, D.W. 2006. The essential GTPase YphC displays a major domain rearrangement associated with nucleotide binding. Proc Natl Acad Sci USA 103:12359-12364.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 12359-12364
    • Muench, S.P.1    Xu, L.2    Sedelnikova, S.E.3    Rice, D.W.4
  • 150
    • 0026694534 scopus 로고
    • Isolation and characterisation of SUA5, a novel gene required for normal growth in Saccharomyces cerevisiae
    • Na, J.G., Pinto, I., and Hampsey, M. 1992. Isolation and characterisation of SUA5, a novel gene required for normal growth in Saccharomyces cerevisiae. Genetics 131:791-801.
    • (1992) Genetics , vol.131 , pp. 791-801
    • Na, J.G.1    Pinto, I.2    Hampsey, M.3
  • 152
    • 0025912715 scopus 로고
    • The assembly of prokaryotic ribosomes
    • Nierhaus, K.H. 1991. The assembly of prokaryotic ribosomes. Biochimie 73:739-755.
    • (1991) Biochimie , vol.73 , pp. 739-755
    • Nierhaus, K.H.1
  • 155
    • 4544345165 scopus 로고    scopus 로고
    • Ribosome modulation factor protects Escherichia coli during heat stress, but this may not be dependent on ribosome dimerization
    • Niven, G.W. 2004. Ribosome modulation factor protects Escherichia coli during heat stress, but this may not be dependent on ribosome dimerization. Arch Microbiol 182:60-66.
    • (2004) Arch Microbiol , vol.182 , pp. 60-66
    • Niven, G.W.1
  • 156
    • 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. Ann Rev Biochem 53:75-117.
    • (1984) Ann Rev Biochem , vol.53 , pp. 75-117
    • Nomura, M.1    Gourse, R.2    Baughman, G.3
  • 157
    • 1842832249 scopus 로고    scopus 로고
    • Crystal structure of E. coli YhbY: A representative of a novel class of RNA binding proteins
    • Osthelmer, G.J., Barken, A., and Matthews, B.W. 2002. Crystal structure of E. coli YhbY: A representative of a novel class of RNA binding proteins. Structure 10:1593-1601.
    • (2002) Structure , vol.10 , pp. 1593-1601
    • Osthelmer, G.J.1    Barken, A.2    Matthews, B.W.3
  • 158
    • 0027370986 scopus 로고
    • Is hypusine essential for eukaryotic cell proliferation?
    • Park, M.H., Wolff, E.C., and Folk, J.E. 1993. Is hypusine essential for eukaryotic cell proliferation?. Trends Biochem Sci 18:475-479.
    • (1993) Trends Biochem Sci , vol.18 , pp. 475-479
    • Park, M.H.1    Wolff, E.C.2    Folk, J.E.3
  • 159
    • 0017235273 scopus 로고
    • A relaxed mutant with an altered ribosomal protein L11
    • Parker, J., Watson, R.J., Friesen, J.D., and Fiil, N.P. 1976. A relaxed mutant with an altered ribosomal protein L11. Mol Gen Genet 144:111-114.
    • (1976) Mol Gen Genet , vol.144 , pp. 111-114
    • Parker, J.1    Watson, R.J.2    Friesen, J.D.3    Fiil, N.P.4
  • 160
    • 0035909058 scopus 로고    scopus 로고
    • Solution structure of HI0257, a bacterial ribosome binding protein
    • Parsons, L., Eisenstein, E., and Orban, J. 2001. Solution structure of HI0257, a bacterial ribosome binding protein. Biochemistry 40:10979-10986.
    • (2001) Biochemistry , vol.40 , pp. 10979-10986
    • Parsons, L.1    Eisenstein, E.2    Orban, J.3
  • 161
    • 0032530708 scopus 로고    scopus 로고
    • Structure of translation initiation factor 5A from Pyrobaculum aerophilum at 1.75 Å resolution
    • Peat, T.S., Newman, J., Waldo, G.S., Berendzen, J., and Terwilliger, T.C. 1998. Structure of translation initiation factor 5A from Pyrobaculum aerophilum at 1.75 Å resolution. Structure 6:1207-1214.
    • (1998) Structure , vol.6 , pp. 1207-1214
    • Peat, T.S.1    Newman, J.2    Waldo, G.S.3    Berendzen, J.4    Terwilliger, T.C.5
  • 162
    • 0037428226 scopus 로고    scopus 로고
    • The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site
    • Pedersen, K., Zavialov, A.V., Pavlov, M.Y., Elf, J., Gerdes, K., and Ehrenberg, M. 2003. The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site. Cell 112:131-140.
    • (2003) Cell , vol.112 , pp. 131-140
    • Pedersen, K.1    Zavialov, A.V.2    Pavlov, M.Y.3    Elf, J.4    Gerdes, K.5    Ehrenberg, M.6
  • 163
    • 0030587497 scopus 로고    scopus 로고
    • Deletion of the putative effector region of Era, an essential GTP-binding protein in Escherichia coli, causes a donminant-negatiove phenotype
    • Pillutla, R.C., Ahnn, J., and Inouye, M. 1996. Deletion of the putative effector region of Era, an essential GTP-binding protein in Escherichia coli, causes a donminant-negatiove phenotype. FEMS Microbiol Lett 143:47-55.
    • (1996) FEMS Microbiol Lett , vol.143 , pp. 47-55
    • Pillutla, R.C.1    Ahnn, J.2    Inouye, M.3
  • 164
    • 0037303518 scopus 로고    scopus 로고
    • Macrolide antibiotic interaction and resistance on the bacterial ribosome
    • Poehlsgaard, J. and Douthwaite, S. 2003. Macrolide antibiotic interaction and resistance on the bacterial ribosome. Curr Opin Investig Drugs 4:140-148.
    • (2003) Curr Opin Investig Drugs , vol.4 , pp. 140-148
    • Poehlsgaard, J.1    Douthwaite, S.2
  • 165
    • 0034460090 scopus 로고    scopus 로고
    • YsxC, a putative GTP-binding protein essential for growth of Bacillus subtilis 168
    • Prágai, Z. and Harwood, C. 2000. YsxC, a putative GTP-binding protein essential for growth of Bacillus subtilis 168. J Bacteriol 182:6819-6823.
    • (2000) J Bacteriol , vol.182 , pp. 6819-6823
    • Prágai, Z.1    Harwood, C.2
  • 166
    • 33750799914 scopus 로고    scopus 로고
    • The highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome
    • Qin, Y., Polacek, N., Vesper, O., Staub, E., Einfeldt, E., Wilson, D.N., and Nierhaus, K.H. 2006. The highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome. Cell 127:721-733.
    • (2006) Cell , vol.127 , pp. 721-733
    • Qin, Y.1    Polacek, N.2    Vesper, O.3    Staub, E.4    Einfeldt, E.5    Wilson, D.N.6    Nierhaus, K.H.7
  • 167
    • 0036921539 scopus 로고    scopus 로고
    • Solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli
    • Rak, A., Kalinin, A., Shcherbakov, D., and Bayer, P. 2002. Solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli. Biochem Biophys Res Commun 299:710-714.
    • (2002) Biochem Biophys Res Commun , vol.299 , pp. 710-714
    • Rak, A.1    Kalinin, A.2    Shcherbakov, D.3    Bayer, P.4
  • 168
    • 2442563845 scopus 로고
    • Localization of the stringent protein of Escherichia coli on the 50S ribosomal subunit
    • Ramagopal, S. and Davis, B.D. 1974. Localization of the stringent protein of Escherichia coli on the 50S ribosomal subunit. Proc Natl Acad Sci USA 71:820-824.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 820-824
    • Ramagopal, S.1    Davis, B.D.2
  • 169
    • 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
  • 170
    • 34248328786 scopus 로고    scopus 로고
    • Regulation of the stringent response is the essential function of the conserved bacterial G protein CgtA in Vibrio cholerae
    • Raskin, D.M., Judson, N., and Mekalanos, J.J. 2007. Regulation of the stringent response is the essential function of the conserved bacterial G protein CgtA in Vibrio cholerae. Proc Natl Acad Sci USA. 104:4636-46341.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4636-46341
    • Raskin, D.M.1    Judson, N.2    Mekalanos, J.J.3
  • 172
    • 0017263835 scopus 로고
    • Stringent factor from Escherichia coli directs ribosomal binding and release of uncharged tRNA
    • Richter, D. 1976. Stringent factor from Escherichia coli directs ribosomal binding and release of uncharged tRNA. Proc Natl Acad Sci USA 73:707-711.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 707-711
    • Richter, D.1
  • 173
    • 0016801495 scopus 로고
    • Escherichia coli stringent factor binds to ribosomes at a site different from that of elongation factor Tu or G
    • Richter, D., Nowak, P., and Kleinert, U. 1975. Escherichia coli stringent factor binds to ribosomes at a site different from that of elongation factor Tu or G. Biochemistry 14:4414-4420.
    • (1975) Biochemistry , vol.14 , pp. 4414-4420
    • Richter, D.1    Nowak, P.2    Kleinert, U.3
  • 174
    • 0036196566 scopus 로고    scopus 로고
    • Resistance to tetracycline, macrolide-lincosamide- streptogramin, trimethoprim, and sulfonamide drug classes
    • Roberts, M.C. 2002. Resistance to tetracycline, macrolide-lincosamide- streptogramin, trimethoprim, and sulfonamide drug classes. Mol Biotechnol 20:261-283.
    • (2002) Mol Biotechnol , vol.20 , pp. 261-283
    • Roberts, M.C.1
  • 175
    • 17144412507 scopus 로고    scopus 로고
    • Update on acquired tetracycline resistance genes
    • Roberts, M.C. 2005. Update on acquired tetracycline resistance genes. FEMS Microbiol Lett 245:195-203.
    • (2005) FEMS Microbiol Lett , vol.245 , pp. 195-203
    • Roberts, M.C.1
  • 176
    • 1842848075 scopus 로고    scopus 로고
    • Domain arrangement of Der, a switch protein containing two GTPase domains
    • Robinson, V., Hwang, J., Fox, E., Inouye, M., and Stock, A. 2002. Domain arrangement of Der, a switch protein containing two GTPase domains. Structure 10:1649-1658.
    • (2002) Structure , vol.10 , pp. 1649-1658
    • Robinson, V.1    Hwang, J.2    Fox, E.3    Inouye, M.4    Stock, A.5
  • 178
    • 2342580711 scopus 로고    scopus 로고
    • Ruzheinikov, S.N., Das, S.K., Sedelnikova, S.E., Baker, P.J., Artymiuk, P.J., Garc?a-Lara, J., Foster, S.J., and Rice, D.W. 2004. Analysis of the open and closed conformations of the GTP-binding protein YsxC from Bacillus subtilis. J Mol Biol 339:265-278.
    • Ruzheinikov, S.N., Das, S.K., Sedelnikova, S.E., Baker, P.J., Artymiuk, P.J., Garc?a-Lara, J., Foster, S.J., and Rice, D.W. 2004. Analysis of the open and closed conformations of the GTP-binding protein YsxC from Bacillus subtilis. J Mol Biol 339:265-278.
  • 179
    • 0141925858 scopus 로고    scopus 로고
    • Interfering with different steps of protein synthesis explored by transcriptional profiling of Escherichia coli K-12
    • Sabina, J., Dover, N., Templeton, L.J., Smulski, D.R., Soll, D., and LaRossa, R.A. 2003. Interfering with different steps of protein synthesis explored by transcriptional profiling of Escherichia coli K-12. J Bacteriol 185:6158-6170.
    • (2003) J Bacteriol , vol.185 , pp. 6158-6170
    • Sabina, J.1    Dover, N.2    Templeton, L.J.3    Smulski, D.R.4    Soll, D.5    LaRossa, R.A.6
  • 180
    • 24744470258 scopus 로고    scopus 로고
    • tmRNA and associated ligands: A puzzling relationship
    • Saguy, M., Gillet, R., Metzinger, L., and Felden, B. 2005. tmRNA and associated ligands: a puzzling relationship. Biochimie 87:897-903.
    • (2005) Biochimie , vol.87 , pp. 897-903
    • Saguy, M.1    Gillet, R.2    Metzinger, L.3    Felden, B.4
  • 182
    • 0035890063 scopus 로고    scopus 로고
    • Nog2p, a putative GTPase associated with pre-60S subunits and required for late 60S maturation steps
    • Saveanu, C., Bienvenu, D., Namane, A., Gleizes, P.E., Gas, N., Jacquier, A., and Fromont-Racine, M. 2001. Nog2p, a putative GTPase associated with pre-60S subunits and required for late 60S maturation steps. EMBO J 20:6475-6484.
    • (2001) EMBO J , vol.20 , pp. 6475-6484
    • Saveanu, C.1    Bienvenu, D.2    Namane, A.3    Gleizes, P.E.4    Gas, N.5    Jacquier, A.6    Fromont-Racine, M.7
  • 184
    • 33751565433 scopus 로고    scopus 로고
    • Multiple GTPases participate in the assembly of the large ribosomal subunit in Bacillus subtilis
    • Schaefer, L., Uicker, W.C., Wicker-Planquart, C., Foucher, A., Jault, J., and Britton, R.A. 2006. Multiple GTPases participate in the assembly of the large ribosomal subunit in Bacillus subtilis. J Bacteriol 188:8252-8258.
    • (2006) J Bacteriol , vol.188 , pp. 8252-8258
    • Schaefer, L.1    Uicker, W.C.2    Wicker-Planquart, C.3    Foucher, A.4    Jault, J.5    Britton, R.A.6
  • 185
    • 0026783192 scopus 로고
    • Kinetic and thermodynamic parameters for tRNA binding to the ribosome and for the translocation reaction
    • Schilling-Bartetzko, S., Bartetzko, A., and Nierhaus, K.H. 1992. Kinetic and thermodynamic parameters for tRNA binding to the ribosome and for the translocation reaction. J Biol Chem267:4703-4712.
    • (1992) J Biol Chem , vol.267 , pp. 4703-4712
    • Schilling-Bartetzko, S.1    Bartetzko, A.2    Nierhaus, K.H.3
  • 186
    • 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., Yonath, A., and Franceschi, F. 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    Yonath, A.7    Franceschi, F.8
  • 189
    • 0033579365 scopus 로고    scopus 로고
    • Crystal structure of Thermotoga maritima ribosome recycling factor: A tRNA mimic
    • Selmer, M., Al-Karadaghi, S., Hirakawa, G., Kaji, A., and Liljas, A. 1999. Crystal structure of Thermotoga maritima ribosome recycling factor: A tRNA mimic. Science 286:2349-2352.
    • (1999) Science , vol.286 , pp. 2349-2352
    • Selmer, M.1    Al-Karadaghi, S.2    Hirakawa, G.3    Kaji, A.4    Liljas, A.5
  • 190
    • 33750378312 scopus 로고    scopus 로고
    • Identification of Escherichia coli m(2)G methyltransferases: II. The ygjO gene encodes a methyltransferase specific for G1835 of the 23S rRNA
    • Sergiev, P., Lesnyak, D., Bogdanov, A., and Dontsova, O. 2006. Identification of Escherichia coli m(2)G 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.1    Lesnyak, D.2    Bogdanov, A.3    Dontsova, O.4
  • 193
    • 4444285829 scopus 로고    scopus 로고
    • Crystal structure of YjeQ from Thermotoga maritima contains a circularly permuted GTPase domain
    • Shin, D.H., Lou, Y., Jancarik, J., Yokota, H., Kim, R., and Kim, S. 2004. Crystal structure of YjeQ from Thermotoga maritima contains a circularly permuted GTPase domain. Proc Natl Acad Sci USA 101:13198-13203.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13198-13203
    • Shin, D.H.1    Lou, Y.2    Jancarik, J.3    Yokota, H.4    Kim, R.5    Kim, S.6
  • 197
    • 0022432313 scopus 로고
    • Ordered processing of Escherichia coli 23S rRNA in vitro
    • Sirdeshmukh, R. and Schlessinger, D. 1985a. Ordered processing of Escherichia coli 23S rRNA in vitro. Nucleic Acids Res 13:5041-5054.
    • (1985) Nucleic Acids Res , vol.13 , pp. 5041-5054
    • Sirdeshmukh, R.1    Schlessinger, D.2
  • 198
    • 0022419656 scopus 로고
    • Why is processing of 23S ribosomal RNA in Escherichia coli not obligate for its function?
    • Sirdeshmukh, R. and Schlessinger, D. 1985b. Why is processing of 23S ribosomal RNA in Escherichia coli not obligate for its function?. J Mol Biol 186:669-672.
    • (1985) J Mol Biol , vol.186 , pp. 669-672
    • Sirdeshmukh, R.1    Schlessinger, D.2
  • 199
    • 0027752458 scopus 로고
    • Functional requirement of a site-specific ribose methylation in ribosomal RNA
    • Sirum-Connolly, K. and Mason, T.L. 1993. Functional requirement of a site-specific ribose methylation in ribosomal RNA. Science 262:1886-1889.
    • (1993) Science , vol.262 , pp. 1886-1889
    • Sirum-Connolly, K.1    Mason, T.L.2
  • 202
    • 0038442836 scopus 로고    scopus 로고
    • More than one way to skin a cat: Translational autoregulation by ribosomal protein S15
    • Springer, M. and Portier, C. 2003. More than one way to skin a cat: translational autoregulation by ribosomal protein S15. Nature Struct Biol 10:420-422.
    • (2003) Nature Struct Biol , vol.10 , pp. 420-422
    • Springer, M.1    Portier, C.2
  • 203
    • 0034651793 scopus 로고    scopus 로고
    • Structure of Hsp15 reveals a novel RNA-binding motif
    • Staker, B.L., Korber, P., Bardwell, J.C., and Saper, M.A. 2000. Structure of Hsp15 reveals a novel RNA-binding motif. EMBO J 19:749-757.
    • (2000) EMBO J , vol.19 , pp. 749-757
    • Staker, B.L.1    Korber, P.2    Bardwell, J.C.3    Saper, M.A.4
  • 204
    • 0000975897 scopus 로고
    • A genetic locus for the regulation of ribonucleic acid synthesis
    • Stent, G.S. and Brenner, S. 1961. A genetic locus for the regulation of ribonucleic acid synthesis. Proc Natl Acad Sci USA 47:2005-2014.
    • (1961) Proc Natl Acad Sci USA , vol.47 , pp. 2005-2014
    • Stent, G.S.1    Brenner, S.2
  • 205
    • 33749827782 scopus 로고    scopus 로고
    • Characterization of a high-throughput screening assay for inhibitors of elongation factor P and ribosomal peptidyltransferase activity
    • Swaney, S., McCroskey, M., Shinabarger, D., Wang, Z., Turner, B.A., and Parker, C.N. 2006. Characterization of a high-throughput screening assay for inhibitors of elongation factor P and ribosomal peptidyltransferase activity. J Biochem Screen 11:736-742.
    • (2006) J Biochem Screen , vol.11 , pp. 736-742
    • Swaney, S.1    McCroskey, M.2    Shinabarger, D.3    Wang, Z.4    Turner, B.A.5    Parker, C.N.6
  • 206
    • 0015578636 scopus 로고
    • Identification of the synthesis of guanosine tetraphosphate (MS I) as insertion of a pyrophosphoryl group into the 3′-position in guanosine 5′-diphosphate
    • Sy, J. and Lipmann, F. 1973. Identification of the synthesis of guanosine tetraphosphate (MS I) as insertion of a pyrophosphoryl group into the 3′-position in guanosine 5′-diphosphate. Proc Natl Acad Sci USA 70:306-309.
    • (1973) Proc Natl Acad Sci USA , vol.70 , pp. 306-309
    • Sy, J.1    Lipmann, F.2
  • 207
    • 18744409067 scopus 로고    scopus 로고
    • Crystal structure of archaeal toxin-antitoxin (RelE-RelB) complex: Implications for toxin activity and antitoxin effects
    • Takagi, H., Kakuta, Y., Okada, T., Yao, M., Tanaka, I., and Kimura, M. 2005. Crystal structure of archaeal toxin-antitoxin (RelE-RelB) complex: implications for toxin activity and antitoxin effects. Nat Struct Mol Biol 12:327-331.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 327-331
    • Takagi, H.1    Kakuta, Y.2    Okada, T.3    Yao, M.4    Tanaka, I.5    Kimura, M.6
  • 208
    • 0036237999 scopus 로고    scopus 로고
    • Overexpression of two different GTPases rescues a null mutation in a heat-induced rRNA methyltransferase
    • Tan, J., Jakob, U., and Bardwell, J.C. 2002. Overexpression of two different GTPases rescues a null mutation in a heat-induced rRNA methyltransferase. J Bacteriol 184:2692-2698.
    • (2002) J Bacteriol , vol.184 , pp. 2692-2698
    • Tan, J.1    Jakob, U.2    Bardwell, J.C.3
  • 209
    • 0027956803 scopus 로고
    • A light-repressed transcript found in Synechococcus PCC 7002 is similar to a chloroplast-specific small subunit ribosomal protein and to a transcription modulator protein associated with sigma 54
    • Tan, X., Varughese, M., and Widger, W. 1994. A light-repressed transcript found in Synechococcus PCC 7002 is similar to a chloroplast-specific small subunit ribosomal protein and to a transcription modulator protein associated with sigma 54. J Biol Chem 269:20905-20912.
    • (1994) J Biol Chem , vol.269 , pp. 20905-20912
    • Tan, X.1    Varughese, M.2    Widger, W.3
  • 210
    • 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
  • 211
    • 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., Tereshko, V., Sanishvili, R., Joachimiak, A., Bushueva, T., Anderson, W.F., and Egli, M. 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
  • 212
    • 0017807310 scopus 로고
    • Protein L16 induces a conformational change when incorporation into an L16-deficient core derived from E. coli ribosomes
    • Teraoka, H. and Nierhaus, K.H. 1978. Protein L16 induces a conformational change when incorporation into an L16-deficient core derived from E. coli ribosomes. FEBS Lett 88:223-226.
    • (1978) FEBS Lett , vol.88 , pp. 223-226
    • Teraoka, H.1    Nierhaus, K.H.2
  • 213
    • 0024597088 scopus 로고
    • The Bacillus subtilis spoOB stage 0 sporulation operon encodes an essential GTP-binding protein
    • Trach, K. and Hoch, J.A. 1989. The Bacillus subtilis spoOB stage 0 sporulation operon encodes an essential GTP-binding protein. J Bacteriol 171:1362-1371.
    • (1989) J Bacteriol , vol.171 , pp. 1362-1371
    • Trach, K.1    Hoch, J.A.2
  • 214
    • 0017159973 scopus 로고
    • Modulation of RNA polymerase specificity by ppGpp
    • Travers, A. 1976. Modulation of RNA polymerase specificity by ppGpp. Mol Gen Genet 147:225-232.
    • (1976) Mol Gen Genet , vol.147 , pp. 225-232
    • Travers, A.1
  • 215
    • 0038045324 scopus 로고    scopus 로고
    • The avilamycin resistance determinants AviRa and AviRb methylate 23S rRNA at the guanosine 2535 base and the uridine 2479 ribose
    • Treede, I., Jakobsen, L., Kirpekar, F., Vester, B., Weitnauer, G., Bechthold, A., and Douthwaite, S. 2003. The avilamycin resistance determinants AviRa and AviRb methylate 23S rRNA at the guanosine 2535 base and the uridine 2479 ribose. Mol Microbiol 49:309-318.
    • (2003) Mol Microbiol , vol.49 , pp. 309-318
    • Treede, I.1    Jakobsen, L.2    Kirpekar, F.3    Vester, B.4    Weitnauer, G.5    Bechthold, A.6    Douthwaite, S.7
  • 216
    • 0029154909 scopus 로고
    • The elongation factor 3 unique in higher fungi and essential for protein biosynthesis is an E site factor
    • Triana-Alonso, F.J., Chakraburtty, K., and Nierhaus, K.H. 1995. The elongation factor 3 unique in higher fungi and essential for protein biosynthesis is an E site factor. J Biol Chem 270:20473-20478.
    • (1995) J Biol Chem , vol.270 , pp. 20473-20478
    • Triana-Alonso, F.J.1    Chakraburtty, K.2    Nierhaus, K.H.3
  • 217
    • 0031850047 scopus 로고    scopus 로고
    • Ribosomal protection from tetracycline mediated by Tet(O) interaction with ribosomes Is GTP-dependent
    • Trieber, C.A., Burkhardt, N., Nierhaus, K.H., and Taylor, D.E. 1998. Ribosomal protection from tetracycline mediated by Tet(O) interaction with ribosomes Is GTP-dependent. Biol Chem 379:847-855.
    • (1998) Biol Chem , vol.379 , pp. 847-855
    • Trieber, C.A.1    Burkhardt, N.2    Nierhaus, K.H.3    Taylor, D.E.4
  • 218
    • 29244463552 scopus 로고    scopus 로고
    • Ribosome binding proteins YhbH and YfiA have opposite functions during 100S formation in the stationary phase of Escherichia coli
    • Ueta, M., Yoshida, A., Wada, C., Baba, T., Mori, H., and Wada, A. 2005. Ribosome binding proteins YhbH and YfiA have opposite functions during 100S formation in the stationary phase of Escherichia coli. Genes Cells 10:1103-1112.
    • (2005) Genes Cells , vol.10 , pp. 1103-1112
    • Ueta, M.1    Yoshida, A.2    Wada, C.3    Baba, T.4    Mori, H.5    Wada, A.6
  • 219
    • 33645050402 scopus 로고    scopus 로고
    • The essential GTPase RbgA (YlqF) is required for 50S ribosome assembly in Bacillus subtilis
    • Uicker, W.C., Schaefer, L., and Britton, R.A. 2006. The essential GTPase RbgA (YlqF) is required for 50S ribosome assembly in Bacillus subtilis. Mol Microbiol 59:528-540.
    • (2006) Mol Microbiol , vol.59 , pp. 528-540
    • Uicker, W.C.1    Schaefer, L.2    Britton, R.A.3
  • 220
    • 0017134523 scopus 로고
    • The mechanism of action of ppGpp on rRNA synthesis in vitro
    • van Ooyen, A.J.J., Gruber, M., and Jorgensen, P. 1976. The mechanism of action of ppGpp on rRNA synthesis in vitro. Cell 8:123-128.
    • (1976) Cell , vol.8 , pp. 123-128
    • van Ooyen, A.J.J.1    Gruber, M.2    Jorgensen, P.3
  • 221
    • 33747136934 scopus 로고    scopus 로고
    • Ribosome recycling revisited
    • Vesper, O. and Wilson, D.N. 2006. Ribosome recycling revisited. Mol Biol (Moscow) 40:742-50.
    • (2006) Mol Biol (Moscow) , vol.40 , pp. 742-750
    • Vesper, O.1    Wilson, D.N.2
  • 222
    • 7544242316 scopus 로고    scopus 로고
    • Structural basis for the control of translational initiation during stress
    • Vila-Sanjurjo, A., Schuwirth, B.S., Hau, C.W., and Cate, J.H.D. 2004. Structural basis for the control of translational initiation during stress. Nature Struct Mol Biol 11:1054-1059.
    • (2004) Nature Struct Mol Biol , vol.11 , pp. 1054-1059
    • Vila-Sanjurjo, A.1    Schuwirth, B.S.2    Hau, C.W.3    Cate, J.H.D.4
  • 223
    • 0031925720 scopus 로고    scopus 로고
    • Growth phase coupled modulation of Escherichia coli ribosomes
    • Wada, A. 1998. Growth phase coupled modulation of Escherichia coli ribosomes. Genes Cells 3:203-208.
    • (1998) Genes Cells , vol.3 , pp. 203-208
    • Wada, A.1
  • 224
    • 0029059640 scopus 로고
    • Ribosome modulation factor: Stationary growth phase-specific inhibitor of ribosome functions from Escherichia coli
    • Wada, A., Igarashi, K., Yoshimura, S., Aimoto, S., and Ishihama, A. 1995. Ribosome modulation factor: Stationary growth phase-specific inhibitor of ribosome functions from Escherichia coli. Biochem Biophys Res Commun 214:410-417.
    • (1995) Biochem Biophys Res Commun , vol.214 , pp. 410-417
    • Wada, A.1    Igarashi, K.2    Yoshimura, S.3    Aimoto, S.4    Ishihama, A.5
  • 225
    • 0034098682 scopus 로고    scopus 로고
    • Growth-phase coupled changes of the ribosome profile in natural isolates and laboratory strains of Escherichia coli
    • Wada, A., Mikkola, R., Kurland, C.G., and Ishihama, A. 2000. Growth-phase coupled changes of the ribosome profile in natural isolates and laboratory strains of Escherichia coli. J Bacteriol 182:2893-2899.
    • (2000) J Bacteriol , vol.182 , pp. 2893-2899
    • Wada, A.1    Mikkola, R.2    Kurland, C.G.3    Ishihama, A.4
  • 226
    • 0025304290 scopus 로고
    • Structure and probable genetic location of a ribosome modulation factor associated with 100S ribosomes in stationary-phase Escherichia coli cells
    • Wada, A., Yamazaki, Y., Fujita, N., and Ishihama, A. 1990. Structure and probable genetic location of a ribosome modulation factor associated with 100S ribosomes in stationary-phase Escherichia coli cells. Proc Natl Acad Sci USA 87:2657-2661.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 2657-2661
    • Wada, A.1    Yamazaki, Y.2    Fujita, N.3    Ishihama, A.4
  • 227
    • 0018966526 scopus 로고
    • Escherichia coli elongation factor G blocks stringent factor
    • Wagner, E.G. and Kurland, C.G. 1980. Escherichia coli elongation factor G blocks stringent factor. Biochemistry 19:1234-1240.
    • (1980) Biochemistry , vol.19 , pp. 1234-1240
    • Wagner, E.G.1    Kurland, C.G.2
  • 228
    • 0041909570 scopus 로고    scopus 로고
    • Bacterial cold shock responses
    • Weber, M.H. and Marahiel, M.A. 2003. Bacterial cold shock responses. Sci Prog 86:9-75.
    • (2003) Sci Prog , vol.86 , pp. 9-75
    • Weber, M.H.1    Marahiel, M.A.2
  • 230
    • 29044436081 scopus 로고    scopus 로고
    • Species-specific antibiotic-ribosome interactions: Implications for drug development
    • Wilson, D.N., Harms, J., Nierhaus, K., Schlünzen, F., and Fucini, P. 2005. Species-specific antibiotic-ribosome interactions: Implications for drug development. Biol Chem 386:1239-1252.
    • (2005) Biol Chem , vol.386 , pp. 1239-1252
    • Wilson, D.N.1    Harms, J.2    Nierhaus, K.3    Schlünzen, F.4    Fucini, P.5
  • 231
    • 0035999670 scopus 로고    scopus 로고
    • Protein synthesis at atomic resolution: Mechanistics of translation in the light of highly resolved structures for the ribosome
    • Wilson, D.N., Blaha, G., Connell, S.R., Ivanov, P.V., Jenke, H., Stelzl, U., Teraoka, Y., and Nierhaus, K.H. 2002. Protein synthesis at atomic resolution: mechanistics of translation in the light of highly resolved structures for the ribosome. Curr Protein Pept Sci 3:1-53.
    • (2002) Curr Protein Pept Sci , vol.3 , pp. 1-53
    • Wilson, D.N.1    Blaha, G.2    Connell, S.R.3    Ivanov, P.V.4    Jenke, H.5    Stelzl, U.6    Teraoka, Y.7    Nierhaus, K.H.8
  • 234
    • 33845484606 scopus 로고    scopus 로고
    • The E-site Story: The importance of maintaining two tRNAs on the ribosome during protein synthesis
    • Wilson, D.N. and Nierhaus, K.H. 2006. The E-site Story: The importance of maintaining two tRNAs on the ribosome during protein synthesis. Cell Mol Life Sci 63:2725-2737.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 2725-2737
    • Wilson, D.N.1    Nierhaus, K.H.2
  • 235
    • 0016153103 scopus 로고
    • In vitro assembly of 30S ribosomal particles from precursor 16S RNA of E. coli
    • Wireman, J.W. and Sypherd, P.S. 1974. In vitro assembly of 30S ribosomal particles from precursor 16S RNA of E. coli. Nature 247:552-554.
    • (1974) Nature , vol.247 , pp. 552-554
    • Wireman, J.W.1    Sypherd, P.S.2
  • 236
    • 3843074167 scopus 로고    scopus 로고
    • The Escherichia coli GTPase CgtAE cofractionates with the 50S ribosomal subunit and interacts with SpoT, a ppGpp synthetase/hydrolase
    • Wout, P., Pu, K., Sullivan, S., Reese, V., Zhou, S., Lin, B., and Maddock, J. 2004. The Escherichia coli GTPase CgtAE cofractionates with the 50S ribosomal subunit and interacts with SpoT, a ppGpp synthetase/hydrolase. J Bacteriol 186:5249-5257.
    • (2004) J Bacteriol , vol.186 , pp. 5249-5257
    • Wout, P.1    Pu, K.2    Sullivan, S.3    Reese, V.4    Zhou, S.5    Lin, B.6    Maddock, J.7
  • 237
    • 0042235771 scopus 로고    scopus 로고
    • The role of RbfA in 16S rRNA processing and cell growth at low temperature in Escherichia coli
    • Xia, B., Ke, H., Shinde, U., and Inouye, M. 2003. The role of RbfA in 16S rRNA processing and cell growth at low temperature in Escherichia coli. J Mol Biol 332:575-584.
    • (2003) J Mol Biol , vol.332 , pp. 575-584
    • Xia, B.1    Ke, H.2    Shinde, U.3    Inouye, M.4
  • 238
    • 33644850774 scopus 로고    scopus 로고
    • Molecular localisation of a ribosome-dependent ATPase on Escherichia coli ribosomes
    • Xu, J., Kiel, M.C., Golshani, A., Chosay, J.G., Aoki, H., and Ganoza, M.C. 2006. Molecular localisation of a ribosome-dependent ATPase on Escherichia coli ribosomes. Nucleic Acids Res 34:1158-1165.
    • (2006) Nucleic Acids Res , vol.34 , pp. 1158-1165
    • Xu, J.1    Kiel, M.C.2    Golshani, A.3    Chosay, J.G.4    Aoki, H.5    Ganoza, M.C.6
  • 239
    • 0027463636 scopus 로고
    • Regulation of the Escherichia coli rmf gene encoding the ribosome modulation factor - growth phase-dependent and growth rate-dependent control
    • Yamagishi, M., Matsushima, H., Wada, A., Sakagami, M., Fujita, N., and Ishihama, A. 1993. Regulation of the Escherichia coli rmf gene encoding the ribosome modulation factor - growth phase-dependent and growth rate-dependent control. EMBO J 12:625-630.
    • (1993) EMBO J , vol.12 , pp. 625-630
    • Yamagishi, M.1    Matsushima, H.2    Wada, A.3    Sakagami, M.4    Fujita, N.5    Ishihama, A.6
  • 240
    • 0034666124 scopus 로고    scopus 로고
    • The plastid ribosomal proteins. Identification of all the proteins in the 30S subunit of an organelle ribosome (chloroplast)
    • Yamaguchi, K., von Knoblauch, K., and Subramanian, A.R. 2000. The plastid ribosomal proteins. Identification of all the proteins in the 30S subunit of an organelle ribosome (chloroplast). J Biol Chem 275:28455-28465.
    • (2000) J Biol Chem , vol.275 , pp. 28455-28465
    • Yamaguchi, K.1    von Knoblauch, K.2    Subramanian, A.R.3
  • 241
    • 0034751687 scopus 로고    scopus 로고
    • Involvement of the N terminus of ribosomal protein L11 in regulation of the RelA protein of Escherichia coli
    • Yang, X. and Ishiguro, E. 2001. Involvement of the N terminus of ribosomal protein L11 in regulation of the RelA protein of Escherichia coli. J Bacteriol 183:6532-6537.
    • (2001) J Bacteriol , vol.183 , pp. 6532-6537
    • Yang, X.1    Ishiguro, E.2
  • 242
    • 0037287421 scopus 로고    scopus 로고
    • Crystal structure of hyperthermophilic archaeal initiation factor 5 A: A homologue of eukaryotic initiation factor 5A (eIF-5A)
    • Yao, M., Ohsawa, A., Kikukawa, S., Tanaka, I., and Kimura, M. 2003. Crystal structure of hyperthermophilic archaeal initiation factor 5 A: a homologue of eukaryotic initiation factor 5A (eIF-5A). J Biochem (Tokyo) 133:75-81.
    • (2003) J Biochem (Tokyo) , vol.133 , pp. 75-81
    • Yao, M.1    Ohsawa, A.2    Kikukawa, S.3    Tanaka, I.4    Kimura, M.5
  • 243
    • 0036431442 scopus 로고    scopus 로고
    • Ribosome-associated factor Y adopts a fold resembling a double-stranded RNA binding domain scaffold
    • Ye, K., Serganov, A., Hu, W., Garber, M., and Patel, D.J. 2002. Ribosome-associated factor Y adopts a fold resembling a double-stranded RNA binding domain scaffold. Eur. J Biochem 269:5182-5191.
    • (2002) Eur. J Biochem , vol.269 , pp. 5182-5191
    • Ye, K.1    Serganov, A.2    Hu, W.3    Garber, M.4    Patel, D.J.5
  • 244
    • 0036947369 scopus 로고    scopus 로고
    • The ribosome modulation factor (RMF) binding site on the 100S ribosome of Escherichia coli
    • Yoshida, H., Maki, Y., Kato, H., Fujisawa, H., Izutsu, K., Wada, C., and Wada, A. 2002. The ribosome modulation factor (RMF) binding site on the 100S ribosome of Escherichia coli. J Biochem (Tokyo) 132:983-989.
    • (2002) J Biochem (Tokyo) , vol.132 , pp. 983-989
    • Yoshida, H.1    Maki, Y.2    Kato, H.3    Fujisawa, H.4    Izutsu, K.5    Wada, C.6    Wada, A.7
  • 245
    • 1942455714 scopus 로고    scopus 로고
    • RMF inactivates ribosomes by covering the peptidyl transferase centre and entrance of peptide exit tunnel
    • Yoshida, H., Yamamoto, H., Uchiumi, T., and Wada, A. 2004. RMF inactivates ribosomes by covering the peptidyl transferase centre and entrance of peptide exit tunnel. Genes Cells 9:271-278.
    • (2004) Genes Cells , vol.9 , pp. 271-278
    • Yoshida, H.1    Yamamoto, H.2    Uchiumi, T.3    Wada, A.4
  • 246
    • 0003463151 scopus 로고
    • Complementary sequences 1700 nucleotides apart form a ribonuclease III cleavage site in Escherichia coli ribosomal precursor RNA
    • Young, R.A. and Steitz, J.A. 1978. Complementary sequences 1700 nucleotides apart form 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
  • 248
    • 6044249053 scopus 로고    scopus 로고
    • Guanine nucleotides stabilize the binding of Bacillus subtilis Obg to ribosomes
    • Zhang, S. and Haldenwang, W.G. 2004. Guanine nucleotides stabilize the binding of Bacillus subtilis Obg to ribosomes. Biochem Biophys Res Commun 322:565-569.
    • (2004) Biochem Biophys Res Commun , vol.322 , pp. 565-569
    • Zhang, S.1    Haldenwang, W.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.