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Volumn 71, Issue 3, 2009, Pages 748-762

Ribosome biogenesis is temperature-dependent and delayed in Escherichia coli lacking the chaperones DnaK or DnaJ

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CHAPERONIN; COMPLEMENTARY DNA; PROTEIN DNAJ; PROTEIN DNAK; RNA 16S;

EID: 58449101336     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2008.06561.x     Document Type: Article
Times cited : (51)

References (82)
  • 1
    • 22544466402 scopus 로고    scopus 로고
    • Protein-independent folding pathway of the 16S rRNA 5′ domain
    • Adilakshmi, T., Ramaswamy, P. Woodson, S.A. (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
    • Adilakshmi, T.1    Ramaswamy, P.2    Woodson, S.A.3
  • 2
    • 30344462410 scopus 로고    scopus 로고
    • Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells
    • Albanèse, V., Yam, A.Y., Baughman, J., Parnot, C. Frydman, J. (2006) Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells. Cell 124 : 75 88.
    • (2006) Cell , vol.124 , pp. 75-88
    • Albanèse, V.1    Yam, A.Y.2    Baughman, J.3    Parnot, C.4    Frydman, J.5
  • 3
    • 0005730329 scopus 로고
    • Extrinsic factors in ribosome assembly
    • In. Nierhaus, K.H., Franceschi, F., Subramanian, H., Erdmann, V. Wittmann-Liebold, B. (eds). New York: Plenum, pp.
    • Alix, J.H. (1993) Extrinsic factors in ribosome assembly. In The Translational Apparatus. Nierhaus, K.H., Franceschi, F., Subramanian, H., Erdmann, V. Wittmann-Liebold, B. (eds). New York : Plenum, pp. 173 184.
    • (1993) The Translational Apparatus. , pp. 173-184
    • Alix, J.H.1
  • 4
    • 0038382885 scopus 로고    scopus 로고
    • DnaK-facilitated ribosome assembly in Escherichia coli revisited
    • Alix, J.H. 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
  • 5
    • 0027551469 scopus 로고
    • RNA processing in prokaryotic cells
    • Apirion, D. 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
  • 6
    • 0018026811 scopus 로고
    • Construction and characterization of new cloning vehicles. III. Derivatives of plasmid pBR322 carrying unique Eco RI sites for selection of Eco RI generated recombinant DNA molecules
    • Bolivar, F. (1978) Construction and characterization of new cloning vehicles. III. Derivatives of plasmid pBR322 carrying unique Eco RI sites for selection of Eco RI generated recombinant DNA molecules. Gene 4 : 121 136.
    • (1978) Gene , vol.4 , pp. 121-136
    • Bolivar, F.1
  • 7
    • 33845719997 scopus 로고    scopus 로고
    • Maturation of the 5′ end of Bacillus subtilis 16S rRNA by the essential ribonuclease YkqC/RNase J1
    • Britton, R.A., Wen, T., Schaefer, L., Pellegrini, O., Uicker, W.C., Mathy, N., et al. (2007) Maturation of the 5′ end of Bacillus subtilis 16S rRNA by the essential ribonuclease YkqC/RNase J1. Mol Microbiol 63 : 127 138.
    • (2007) Mol Microbiol , vol.63 , pp. 127-138
    • Britton, R.A.1    Wen, T.2    Schaefer, L.3    Pellegrini, O.4    Uicker, W.C.5    Mathy, N.6
  • 8
    • 0025048776 scopus 로고
    • Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone
    • Bukau, B. Walker, G.C. (1990) Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone. EMBO J 9 : 4027 4036.
    • (1990) EMBO J , vol.9 , pp. 4027-4036
    • Bukau, B.1    Walker, G.C.2
  • 9
    • 0030877499 scopus 로고    scopus 로고
    • Depletion of pre-16S rRNA in starved Escherichia coli cells
    • Cangelosi, G.A. Brabant, W.H. (1997) Depletion of pre-16S rRNA in starved Escherichia coli cells. J Bacteriol 179 : 4457 4463.
    • (1997) J Bacteriol , vol.179 , pp. 4457-4463
    • Cangelosi, G.A.1    Brabant, W.H.2
  • 10
    • 33845443409 scopus 로고    scopus 로고
    • The other target for ribosomal antibiotics: Inhibition of bacterial ribosomal subunit formation
    • Champney, W.S. (2006) The other target for ribosomal antibiotics: inhibition of bacterial ribosomal subunit formation. Infect Disord Drug Targets 6 : 377 390.
    • (2006) Infect Disord Drug Targets , vol.6 , pp. 377-390
    • Champney, W.S.1
  • 11
    • 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. 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
  • 12
    • 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. Iost, I. (2004) CsdA, a cold-shock RNA helicase from Escherichia coli, is involved in the biogenesis of 50S ribosomal subunit. Nucleic Acids Res 32 : 2751 2759.
    • (2004) Nucleic Acids Res , vol.32 , pp. 2751-2759
    • Charollais, J.1    Dreyfus, M.2    Iost, I.3
  • 13
    • 0037319895 scopus 로고    scopus 로고
    • Assembly of the 30S ribosomal subunit
    • Culver, G.M. (2003) Assembly of the 30S ribosomal subunit. Biopolymers 68 : 234 249.
    • (2003) Biopolymers , vol.68 , pp. 234-249
    • Culver, G.M.1
  • 14
    • 35649008817 scopus 로고    scopus 로고
    • Structural aspects of RbfA action during small ribosomal subunit assembly
    • Datta, P.P., Wilson, D.N., Kawazoe, M., Swami, N.K., Kaminishi, T., Sharma, M.R., et al. (2007) Structural aspects of RbfA action during small ribosomal subunit assembly. Mol Cell 28 : 434 445.
    • (2007) Mol Cell , vol.28 , pp. 434-445
    • Datta, P.P.1    Wilson, D.N.2    Kawazoe, M.3    Swami, N.K.4    Kaminishi, T.5    Sharma, M.R.6
  • 15
    • 34548341809 scopus 로고    scopus 로고
    • The Hsp40 chaperone Jjj1 is required for the nucleo-cytoplasmic recycling of preribosomal factors in Saccharomyces cerevisiae
    • Demoinet, E., Jacquier, A., Lutfalla, G. Fromont-Racine, M. (2007) The Hsp40 chaperone Jjj1 is required for the nucleo-cytoplasmic recycling of preribosomal factors in Saccharomyces cerevisiae. RNA 13 : 1570 1581.
    • (2007) RNA , vol.13 , pp. 1570-1581
    • Demoinet, E.1    Jacquier, A.2    Lutfalla, G.3    Fromont-Racine, M.4
  • 16
    • 0347595319 scopus 로고    scopus 로고
    • Authentic precursors to ribosomal subunits accumulate in Escherichia coli in the absence of functional DnaK chaperone
    • El Hage, A. Alix, J.H. (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
  • 17
    • 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. 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
  • 18
    • 0015950202 scopus 로고
    • Preparation of E. coli ribosomal subunits without loss of biological activity
    • Expert-Bezançon, A., Guerin, M.F., Hayes, D.H., Legault, L. Thibault, J. (1974) Preparation of E. coli ribosomal subunits without loss of biological activity. Biochimie 56 : 77 89.
    • (1974) Biochimie , vol.56 , pp. 77-89
    • Expert-Bezançon, A.1    Guerin, M.F.2    Hayes, D.H.3    Legault, L.4    Thibault, J.5
  • 19
    • 0022613101 scopus 로고
    • Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes
    • Fayet, O., Louarn, J.M. Georgopoulos, C. (1986) Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes. Mol Gen Genet 202 : 435 445.
    • (1986) Mol Gen Genet , vol.202 , pp. 435-445
    • Fayet, O.1    Louarn, J.M.2    Georgopoulos, C.3
  • 20
    • 42449098958 scopus 로고    scopus 로고
    • Characterization of a 30S ribosomal subunit assembly intermediate found in Escherichia coli cells growing with neomycin or paromomycin
    • Foster, C. Champney, W.S. (2008) Characterization of a 30S ribosomal subunit assembly intermediate found in Escherichia coli cells growing with neomycin or paromomycin. Arch Microbiol 189 : 441 449.
    • (2008) Arch Microbiol , vol.189 , pp. 441-449
    • Foster, C.1    Champney, W.S.2
  • 21
    • 0034806604 scopus 로고    scopus 로고
    • The djlA gene acts synergistically with dnaJ in promoting Escherichia coli growth
    • Genevaux, P., Schwager, F., Georgopoulos, C. Kelley, W.L. (2001) The djlA gene acts synergistically with dnaJ in promoting Escherichia coli growth. J Bacteriol 183 : 5747 5750.
    • (2001) J Bacteriol , vol.183 , pp. 5747-5750
    • Genevaux, P.1    Schwager, F.2    Georgopoulos, C.3    Kelley, W.L.4
  • 22
    • 35748962910 scopus 로고    scopus 로고
    • The Hsp70 chaperone machines of Escherichia coli: A paradigm for the repartition of chaperone functions
    • Genevaux, P., Georgopoulos, C. Kelley, W.L. (2007) The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions. Mol Microbiol 66 : 840 857.
    • (2007) Mol Microbiol , vol.66 , pp. 840-857
    • Genevaux, P.1    Georgopoulos, C.2    Kelley, W.L.3
  • 23
    • 0037008763 scopus 로고    scopus 로고
    • A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase
    • Germaniuk, A., Liberek, K. Marszalek, J. (2002) A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase. J Biol Chem 277 : 27801 27808.
    • (2002) J Biol Chem , vol.277 , pp. 27801-27808
    • Germaniuk, A.1    Liberek, K.2    Marszalek, J.3
  • 24
    • 0026483711 scopus 로고
    • Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli
    • Gragerov, A., Nudler, E., Komissarova, N., Gaitanaris, G.A., Gottesman, M.E. Nikiforov, V. (1992) Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli. Proc Natl Acad Sci USA 89 : 10341 10344.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10341-10344
    • Gragerov, A.1    Nudler, E.2    Komissarova, N.3    Gaitanaris, G.A.4    Gottesman, M.E.5    Nikiforov, V.6
  • 25
    • 8644290874 scopus 로고    scopus 로고
    • A chaperone network controls the heat shock response in E. coli
    • Guisbert, E., Herman, C., Lu, C.Z. Gross, C.A. (2004) A chaperone network controls the heat shock response in E. coli. Genes Dev 18 : 2812 2821.
    • (2004) Genes Dev , vol.18 , pp. 2812-2821
    • Guisbert, E.1    Herman, C.2    Lu, C.Z.3    Gross, C.A.4
  • 26
    • 51949087754 scopus 로고    scopus 로고
    • Convergence of molecular, modeling, and systems approaches for an understanding of the Escherichia coli heat shock response
    • Guisbert, E., Yura, T., Rhodius, V.A. Gross, C.A. (2008) Convergence of molecular, modeling, and systems approaches for an understanding of the Escherichia coli heat shock response. Microbiol Mol Biol Rev 72 : 545 554.
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 545-554
    • Guisbert, E.1    Yura, T.2    Rhodius, V.A.3    Gross, C.A.4
  • 27
    • 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. 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
  • 28
    • 4544273801 scopus 로고    scopus 로고
    • Substrate binding analysis of the 23S rRNA methyltransferase RrmJ
    • Hager, J., Staker, B.L. Jakob, U. (2004) Substrate binding analysis of the 23S rRNA methyltransferase RrmJ. J Bacteriol 186 : 6634 6642.
    • (2004) J Bacteriol , vol.186 , pp. 6634-6642
    • Hager, J.1    Staker, B.L.2    Jakob, U.3
  • 29
    • 0017273722 scopus 로고
    • Processing of the 17-S Escherichia coli precursor RNA in the 27-S pre-ribosomal particle
    • Hayes, F. Vasseur, M. (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
  • 30
    • 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., Wurm, R., Menzel, A. Wagner, R. (2005) The seven E. coli ribosomal RNA operon upstream regulatory regions differ in structure and transcription factor binding efficiencies. Biol Chem 386 : 523 534.
    • (2005) Biol Chem , vol.386 , pp. 523-534
    • Hillebrand, A.1    Wurm, R.2    Menzel, A.3    Wagner, R.4
  • 32
    • 0742322957 scopus 로고    scopus 로고
    • Mapping structural differences between 30S ribosomal subunit assembly intermediates
    • Holmes, K.L. Culver, G.M. (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
  • 33
    • 33748486487 scopus 로고    scopus 로고
    • The tandem GTPase, Der, is essential for the biogenesis of 50S ribosomal subunits in Escherichia coli
    • Hwang, J. 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
  • 34
    • 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. 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
  • 35
    • 33745757322 scopus 로고    scopus 로고
    • Era and RbfA have overlapping function in ribosome biogenesis in Escherichia coli
    • Inoue, K., Chen, J., Tan, Q. 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    Tan, Q.3    Inouye, M.4
  • 36
    • 33749125440 scopus 로고    scopus 로고
    • DEAD-box RNA helicases in Escherichia coli
    • Iost, I. 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
  • 37
    • 38649135052 scopus 로고    scopus 로고
    • The E. coli RhlE RNA helicase regulates the function of related RNA helicases during ribosome assembly
    • Jain, C. (2008) The E. coli RhlE RNA helicase regulates the function of related RNA helicases during ribosome assembly. RNA 14 : 381 389.
    • (2008) RNA , vol.14 , pp. 381-389
    • Jain, C.1
  • 39
    • 34548513288 scopus 로고    scopus 로고
    • G-protein control of the ribosome-associated stress response protein SpoT
    • Jiang, M., Sullivan, S.M., Wout, P.K. Maddock, J.R. (2007) G-protein control of the ribosome-associated stress response protein SpoT. J Bacteriol 189 : 6140 6147.
    • (2007) J Bacteriol , vol.189 , pp. 6140-6147
    • Jiang, M.1    Sullivan, S.M.2    Wout, P.K.3    Maddock, J.R.4
  • 40
    • 13444259766 scopus 로고    scopus 로고
    • The YrdC protein - A putative ribosome maturation factor
    • Kaczanowska, M. 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
  • 41
    • 34548728025 scopus 로고    scopus 로고
    • Ribosome biogenesis and the translation process in Escherichia coli
    • Kaczanowska, M. Rydén-Aulin, M. (2007) Ribosome biogenesis and the translation process in Escherichia coli. Microbiol Mol Biol Rev 71 : 477 494.
    • (2007) Microbiol Mol Biol Rev , vol.71 , pp. 477-494
    • Kaczanowska, M.1    Rydén-Aulin, M.2
  • 42
    • 0027983768 scopus 로고
    • Induction of heat shock proteins by abnormal proteins results from stabilization and not increased synthesis of sigma 32 in Escherichia coli
    • Kanemori, M., Mori, H. Yura, T. (1994) Induction of heat shock proteins by abnormal proteins results from stabilization and not increased synthesis of sigma 32 in Escherichia coli. J Bacteriol 176 : 5648 5653.
    • (1994) J Bacteriol , vol.176 , pp. 5648-5653
    • Kanemori, M.1    Mori, H.2    Yura, T.3
  • 43
    • 0344731385 scopus 로고    scopus 로고
    • The effect of some antibiotic-resistance-conferring plasmids on the removal of the heat-aggregated proteins from Escherichia coli cells
    • Kedzierska, S., Staniszewska, M., Potrykus, J. Wegrzyn, G. (1999a) The effect of some antibiotic-resistance-conferring plasmids on the removal of the heat-aggregated proteins from Escherichia coli cells. FEMS Microbiol Lett 176 : 279 284.
    • (1999) FEMS Microbiol Lett , vol.176 , pp. 279-284
    • Kedzierska, S.1    Staniszewska, M.2    Potrykus, J.3    Wegrzyn, G.4
  • 44
    • 0033063634 scopus 로고    scopus 로고
    • The role of DnaK/DnaJ and GroEL/GroES systems in the removal of endogenous proteins aggregated by heat-shock from Escherichia coli cells
    • Kedzierska, S., Staniszewska, M., Wegrzyn, A. Taylor, A. (1999b) The role of DnaK/DnaJ and GroEL/GroES systems in the removal of endogenous proteins aggregated by heat-shock from Escherichia coli cells. FEBS Lett 446 : 331 337.
    • (1999) FEBS Lett , vol.446 , pp. 331-337
    • Kedzierska, S.1    Staniszewska, M.2    Wegrzyn, A.3    Taylor, A.4
  • 45
    • 22744447508 scopus 로고    scopus 로고
    • Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli
    • Kerner, M.J., Naylor, D.J., Ishihama, Y., Maier, T., Chang, H.C., Stines, A.P., et al. (2005) Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell 122 : 209 220.
    • (2005) Cell , vol.122 , pp. 209-220
    • Kerner, M.J.1    Naylor, D.J.2    Ishihama, Y.3    Maier, T.4    Chang, H.C.5    Stines, A.P.6
  • 46
    • 0019834067 scopus 로고
    • Cold-sensitive ribosome assembly in an Escherichia coli mutant lacking a single methyl group in ribosomal protein L3
    • Lhoest, J. Colson, C. (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
  • 47
    • 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. 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
  • 48
    • 0029052538 scopus 로고
    • The DnaJ chaperone catalytically activates the DnaK chaperone to preferentially bind the sigma 32 heat shock transcriptional regulator
    • Liberek, K., Wall, D. Georgopoulos, C. (1995) The DnaJ chaperone catalytically activates the DnaK chaperone to preferentially bind the sigma 32 heat shock transcriptional regulator. Proc Natl Acad Sci USA 92 : 6224 6228.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6224-6228
    • Liberek, K.1    Wall, D.2    Georgopoulos, C.3
  • 49
    • 38549119467 scopus 로고    scopus 로고
    • Chaperones in control of protein disaggregation
    • Liberek, K., Lewandowska, A. Zietkiewicz, S. (2008) Chaperones in control of protein disaggregation. EMBO J 27 : 328 335.
    • (2008) EMBO J , vol.27 , pp. 328-335
    • Liberek, K.1    Lewandowska, A.2    Zietkiewicz, S.3
  • 50
    • 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
  • 51
    • 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.M., Bylund, G.O., Srivastava, M.K., Lundberg, L.A., Persson, O.P., Wingsle, G. Wikstrom, P.M. (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.M.1    Bylund, G.O.2    Srivastava, M.K.3    Lundberg, L.A.4    Persson, O.P.5    Wingsle, G.6    Wikstrom, P.M.7
  • 52
    • 0036342369 scopus 로고    scopus 로고
    • The DnaK chaperone system facilitates 30S ribosomal subunit assembly
    • Maki, J.A., Schnobrich, D.J. 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
  • 53
    • 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., Southworth, D.R. Culver, G.M. (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
  • 54
  • 55
    • 33846818906 scopus 로고    scopus 로고
    • The specialized cytosolic J-protein, Jjj1, functions in 60S ribosomal subunit biogenesis
    • Meyer, A.E., Hung, N.J., Yang, P., Johnson, A.W. Craig, E.A. (2007) The specialized cytosolic J-protein, Jjj1, functions in 60S ribosomal subunit biogenesis. Proc Natl Acad Sci USA 104 : 1558 1563.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1558-1563
    • Meyer, A.E.1    Hung, N.J.2    Yang, P.3    Johnson, A.W.4    Craig, E.A.5
  • 56
    • 0003785155 scopus 로고
    • Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press.
    • Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor, New York : Cold Spring Harbor Laboratory Press.
    • (1972) Experiments in Molecular Genetics.
    • Miller, J.H.1
  • 57
    • 0027229503 scopus 로고
    • The Escherichia coli heat shock gene htpY: Mutational analysis, cloning, sequencing, and transcriptional regulation
    • Missiakas, D., Georgopoulos, C. Raina, S. (1993) The Escherichia coli heat shock gene htpY: mutational analysis, cloning, sequencing, and transcriptional regulation. J Bacteriol 175 : 2613 2624.
    • (1993) J Bacteriol , vol.175 , pp. 2613-2624
    • Missiakas, D.1    Georgopoulos, C.2    Raina, S.3
  • 58
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
    • Mogk, A., Tomoyasu, T., Goloubinoff, P., Rudiger, S., Roder, D., Langen, H. Bukau, B. (1999) Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J 18 : 6934 6949.
    • (1999) EMBO J , vol.18 , pp. 6934-6949
    • Mogk, A.1    Tomoyasu, T.2    Goloubinoff, P.3    Rudiger, S.4    Roder, D.5    Langen, H.6    Bukau, B.7
  • 59
    • 26944462957 scopus 로고    scopus 로고
    • Assembly of the procaryotic ribosome
    • In. Nierhaus, K. Wilson, D. (eds). Weinheim, Germany: Wiley VCH, pp.
    • Nierhaus, K.H. (2004) Assembly of the procaryotic ribosome. In Protein Synthesis and Ribosome Structure. Nierhaus, K. Wilson, D. (eds). Weinheim, Germany : Wiley VCH, pp. 85 105.
    • (2004) Protein Synthesis and Ribosome Structure. , pp. 85-105
    • Nierhaus, K.H.1
  • 60
    • 47249094203 scopus 로고    scopus 로고
    • Ribosome assembly in Escherichia coli strains lacking the RNA helicase DeaD/CsdA or DbpA
    • Peil, L., Virumae, K. Remme, J. (2008) Ribosome assembly in Escherichia coli strains lacking the RNA helicase DeaD/CsdA or DbpA. FEBS J 275 : 3772 3782.
    • (2008) FEBS J , vol.275 , pp. 3772-3782
    • Peil, L.1    Virumae, K.2    Remme, J.3
  • 61
    • 0037336121 scopus 로고    scopus 로고
    • Definition of the Escherichia coli MC4100 genome by use of a DNA array
    • Peters, J.E., Thate, T.E. Craig, N.L. (2003) Definition of the Escherichia coli MC4100 genome by use of a DNA array. J Bacteriol 185 : 2017 2021.
    • (2003) J Bacteriol , vol.185 , pp. 2017-2021
    • Peters, J.E.1    Thate, T.E.2    Craig, N.L.3
  • 62
    • 0019841516 scopus 로고
    • The plasmid cloning vector pBR325 contains a 482 base-pair-long inverted duplication
    • Prentki, P., Karch, F., Iida, S. Meyer, J. (1981) The plasmid cloning vector pBR325 contains a 482 base-pair-long inverted duplication. Gene 14 : 289 299.
    • (1981) Gene , vol.14 , pp. 289-299
    • Prentki, P.1    Karch, F.2    Iida, S.3    Meyer, J.4
  • 63
    • 43449118061 scopus 로고    scopus 로고
    • Mini-III, an unusual member of the RNase III family of enzymes, catalyses 23S ribosomal RNA maturation in B. subtilis
    • Redko, Y., Bechhofer, D.H. Condon, C. (2008) Mini-III, an unusual member of the RNase III family of enzymes, catalyses 23S ribosomal RNA maturation in B. subtilis. Mol Microbiol 68 : 1096 1106.
    • (2008) Mol Microbiol , vol.68 , pp. 1096-1106
    • Redko, Y.1    Bechhofer, D.H.2    Condon, C.3
  • 64
    • 44249096370 scopus 로고    scopus 로고
    • Suppression of a cold-sensitive mutation in ribosomal protein S5 reveals a role for RimJ in ribosome biogenesis
    • Roy-Chaudhuri, B., Kirthi, N., Kelley, T. Culver, G.M. (2008) Suppression of a cold-sensitive mutation in ribosomal protein S5 reveals a role for RimJ in ribosome biogenesis. Mol Microbiol 68 : 1547 1559.
    • (2008) Mol Microbiol , vol.68 , pp. 1547-1559
    • Roy-Chaudhuri, B.1    Kirthi, N.2    Kelley, T.3    Culver, G.M.4
  • 66
  • 67
    • 0025164669 scopus 로고
    • Isolation and characterization of dnaJ null mutants of Escherichia coli
    • Sell, S.M., Eisen, C., Ang, D., Zylicz, M. Georgopoulos, C. (1990) Isolation and characterization of dnaJ null mutants of Escherichia coli. J Bacteriol 172 : 4827 4835.
    • (1990) J Bacteriol , vol.172 , pp. 4827-4835
    • Sell, S.M.1    Eisen, C.2    Ang, D.3    Zylicz, M.4    Georgopoulos, C.5
  • 68
    • 20844460290 scopus 로고    scopus 로고
    • Interaction of Era with the 30S ribosomal subunit implications for 30S subunit assembly
    • Sharma, M.R., Barat, C., Wilson, D.N., Booth, T.M., Kawazoe, M., Hori-Takemoto, C., et al. (2005) Interaction of Era with the 30S ribosomal subunit implications for 30S subunit assembly. Mol Cell 18 : 319 329.
    • (2005) Mol Cell , vol.18 , pp. 319-329
    • Sharma, M.R.1    Barat, C.2    Wilson, D.N.3    Booth, T.M.4    Kawazoe, M.5    Hori-Takemoto, C.6
  • 69
    • 0025153770 scopus 로고
    • Mechanism and regulation of bacterial ribosomal RNA processing
    • Srivastava, A.K. Schlessinger, D. (1990) Mechanism and regulation of bacterial ribosomal RNA processing. Annu Rev Microbiol 44 : 105 129.
    • (1990) Annu Rev Microbiol , vol.44 , pp. 105-129
    • Srivastava, A.K.1    Schlessinger, D.2
  • 71
    • 0017355828 scopus 로고
    • The nature of the proteins in 'chloramphenicol particles' from Escherichia coli A19 (Hfr rel met rns)
    • Sykes, J., Metcalf, E. Pickering, J.D. (1977) The nature of the proteins in 'chloramphenicol particles' from Escherichia coli A19 (Hfr rel met rns). J Gen Microbiol 98 : 1 16.
    • (1977) J Gen Microbiol , vol.98 , pp. 1-16
    • Sykes, J.1    Metcalf, E.2    Pickering, J.D.3
  • 72
    • 28444479853 scopus 로고    scopus 로고
    • An assembly landscape for the 30S ribosomal subunit
    • Talkington, M.W., Siuzdak, G. Williamson, J.R. (2005) An assembly landscape for the 30S ribosomal subunit. Nature 438 : 628 632.
    • (2005) Nature , vol.438 , pp. 628-632
    • Talkington, M.W.1    Siuzdak, G.2    Williamson, J.R.3
  • 73
    • 0026579213 scopus 로고
    • Regulation of the expression of the cell-cycle gene ftsZ by DicF antisense RNA. Division does not require a fixed number of FtsZ molecules
    • Tetart, F. Bouché, J.P. (1992) Regulation of the expression of the cell-cycle gene ftsZ by DicF antisense RNA. Division does not require a fixed number of FtsZ molecules. Mol Microbiol 6 : 615 620.
    • (1992) Mol Microbiol , vol.6 , pp. 615-620
    • Tetart, F.1    Bouché, J.P.2
  • 74
    • 0031793242 scopus 로고    scopus 로고
    • Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli
    • Tomoyasu, T., Ogura, T., Tatsuta, T. Bukau, B. (1998) Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli. Mol Microbiol 30 : 567 581.
    • (1998) Mol Microbiol , vol.30 , pp. 567-581
    • Tomoyasu, T.1    Ogura, T.2    Tatsuta, T.3    Bukau, B.4
  • 75
    • 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., Condon, C., Balada, J.M., Squires, C. Squires, C.L. (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
  • 76
    • 0442307793 scopus 로고    scopus 로고
    • Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK
    • Vorderwülbecke, S., Kramer, G., Merz, F., Kurz, T.A., Rauch, T., Zachmann-Brand, B., et al. (2004) Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK. FEBS Lett 559 : 181 187.
    • (2004) FEBS Lett , vol.559 , pp. 181-187
    • Vorderwülbecke, S.1    Kramer, G.2    Merz, F.3    Kurz, T.A.4    Rauch, T.5    Zachmann-Brand, B.6
  • 77
    • 0025782890 scopus 로고
    • Construction of versatile low-copy-number vectors for cloning, sequencing and gene expression in Escherichia coli
    • Wang, R.F. Kushner, S.R. (1991) Construction of versatile low-copy-number vectors for cloning, sequencing and gene expression in Escherichia coli. Gene 100 : 195 199.
    • (1991) Gene , vol.100 , pp. 195-199
    • Wang, R.F.1    Kushner, S.R.2
  • 78
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Folding, refolding, and degrading proteins
    • Wickner, S., Maurizi, M.R. Gottesman, S. (1999) Posttranslational quality control: folding, refolding, and degrading proteins. Science 286 : 1888 1893.
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 79
    • 1642351870 scopus 로고    scopus 로고
    • Chaperone networks in bacteria: Analysis of protein homeostasis in minimal cells
    • Wong, P. Houry, W.A. (2004) Chaperone networks in bacteria: analysis of protein homeostasis in minimal cells. J Struct Biol 146 : 79 89.
    • (2004) J Struct Biol , vol.146 , pp. 79-89
    • Wong, P.1    Houry, W.A.2
  • 80
    • 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. 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
  • 81
    • 0003463151 scopus 로고
    • Complementary sequences 1700 nucleotides apart form a ribonuclease III cleavage site in Escherichia coli ribosomal precursor RNA
    • Young, R.A. 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
  • 82
    • 0028251157 scopus 로고
    • Diverse mechanisms for regulating ribosomal protein synthesis in Escherichia coli
    • Zengel, J.M. Lindahl, L. (1994) Diverse mechanisms for regulating ribosomal protein synthesis in Escherichia coli. Prog Nucleic Acid Res Mol Biol 47 : 331 370.
    • (1994) Prog Nucleic Acid Res Mol Biol , vol.47 , pp. 331-370
    • Zengel, J.M.1    Lindahl, L.2


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