메뉴 건너뛰기




Volumn 260, Issue 2-3, 1998, Pages 199-206

DnaK-dependent ribosome biogenesis in Escherichia coli: Competition for dominance between the alleles dnaK756 and dnaK+

Author keywords

DnaK chaperone; Dominance biogenesis; Escherichia coli; Ribosome assembly

Indexed keywords

CHAPERONE; PROTEIN DNAK;

EID: 0031737451     PISSN: 00268925     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004380050886     Document Type: Article
Times cited : (11)

References (41)
  • 1
    • 0027362954 scopus 로고
    • Mutant DnaK chaperones cause ribosome assembly defects in Escherichia coll
    • Alix JH, Guérin MF (1993) Mutant DnaK chaperones cause ribosome assembly defects in Escherichia coll. Proc Natl Acad Sci USA 90:9725-9729
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9725-9729
    • Alix, J.H.1    Guérin, M.F.2
  • 2
    • 0024669886 scopus 로고
    • The heat-shock-regulated grpE gene of Escherichia coli is required for bacterial growth at all temperatures but is dispensable in certain mutant backgrounds
    • Ang D, Georgopoulos C (1989) The heat-shock-regulated grpE gene of Escherichia coli is required for bacterial growth at all temperatures but is dispensable in certain mutant backgrounds. J Bacteriol 171:2748-2755
    • (1989) J Bacteriol , vol.171 , pp. 2748-2755
    • Ang, D.1    Georgopoulos, C.2
  • 3
    • 0028288217 scopus 로고
    • Overexpression in Escherichia coli, purification and characterization of the molecular chaperone HSC70
    • Benaroudj N, Fang B, Triniolles F, Ghelis C, Ladjimi MM (1994) Overexpression in Escherichia coli, purification and characterization of the molecular chaperone HSC70. Eur J Biochem 221:121-128
    • (1994) Eur J Biochem , vol.221 , pp. 121-128
    • Benaroudj, N.1    Fang, B.2    Triniolles, F.3    Ghelis, C.4    Ladjimi, M.M.5
  • 5
    • 0029746254 scopus 로고    scopus 로고
    • Effect of nucleotides, peptides, and unfolded proteins on the self-association of the molecular chaperone HSC70
    • Benaroudj N, Triniolles F, Ladjimi MM (1996) Effect of nucleotides, peptides, and unfolded proteins on the self-association of the molecular chaperone HSC70. J Biol Chem 271:18471-18476
    • (1996) J Biol Chem , vol.271 , pp. 18471-18476
    • Benaroudj, N.1    Triniolles, F.2    Ladjimi, M.M.3
  • 6
    • 0027164203 scopus 로고
    • Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers
    • Blond-Elguindi S, Fourie AM, Sambrook JF, Gething MJ (1993) Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers. J Biol Chem 268:12730-12735
    • (1993) J Biol Chem , vol.268 , pp. 12730-12735
    • Blond-Elguindi, S.1    Fourie, A.M.2    Sambrook, J.F.3    Gething, M.J.4
  • 7
    • 0026498778 scopus 로고
    • Physiological consequences of DnaK and DnaJ overproduction in Escherichia coli
    • Blum P, Ory J, Bauernfeind J, Krska J (1992) Physiological consequences of DnaK and DnaJ overproduction in Escherichia coli. J Bacteriol 174:7436-7444
    • (1992) J Bacteriol , vol.174 , pp. 7436-7444
    • Blum, P.1    Ory, J.2    Bauernfeind, J.3    Krska, J.4
  • 9
    • 0028297010 scopus 로고
    • The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171
    • Buchberger A, Valencia A, McMacken R, Sander C, Bukau B (1994) The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171. EMBO J 13:1687-1695
    • (1994) EMBO J , vol.13 , pp. 1687-1695
    • Buchberger, A.1    Valencia, A.2    McMacken, R.3    Sander, C.4    Bukau, B.5
  • 11
    • 0031973622 scopus 로고    scopus 로고
    • RimM and RbfA are essential for efficient processing of 16S rRNA in Escherichia coli
    • Bylund G, Wipemo C, Lundberg LAC, Wikström PM (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, C.2    Lundberg, L.A.C.3    Wikström, P.M.4
  • 12
    • 0025258481 scopus 로고
    • The mitochondrial chaperonin hsp60 is required for its own assembly
    • Cheng MY, Hartl FU, Horwich AL (1990) The mitochondrial chaperonin hsp60 is required for its own assembly. Nature 348:455-458
    • (1990) Nature , vol.348 , pp. 455-458
    • Cheng, M.Y.1    Hartl, F.U.2    Horwich, A.L.3
  • 14
    • 0030851815 scopus 로고    scopus 로고
    • Kinetic evidence for peptide-induced oligomerization of the molecular chaperone DnaK at heat shock temperatures
    • Farr CD, Witt SN (1997) Kinetic evidence for peptide-induced oligomerization of the molecular chaperone DnaK at heat shock temperatures. Biochemistry 36:10793-10800
    • (1997) Biochemistry , vol.36 , pp. 10793-10800
    • Farr, C.D.1    Witt, S.N.2
  • 16
    • 0029953178 scopus 로고    scopus 로고
    • Effect of constitutive 70 kDa heat shock protein polymerization on its interaction with protein substrate
    • Gao B, Eisenberg E, Greene L (1996) Effect of constitutive 70 kDa heat shock protein polymerization on its interaction with protein substrate. J Biol Chem. 271:16792-16797
    • (1996) J Biol Chem. , vol.271 , pp. 16792-16797
    • Gao, B.1    Eisenberg, E.2    Greene, L.3
  • 17
    • 0017342285 scopus 로고
    • A new bacterial gene (groPC) which affects lambda DNA replication
    • Georgopoulos CP (1977) A new bacterial gene (groPC) which affects lambda DNA replication. Mol Gen Genet 151:35-39
    • (1977) Mol Gen Genet , vol.151 , pp. 35-39
    • Georgopoulos, C.P.1
  • 18
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J (1997) Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276:431-435
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Di Liberto, M.3    Hartl, F.4    Kuriyan, J.5
  • 19
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381:571-579
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 21
    • 0029118986 scopus 로고
    • Polymerization of 70-kDa heat shock protein by yeast DnaJ in ATP
    • King C, Eisenberg E, Greene L (1995) Polymerization of 70-kDa heat shock protein by yeast DnaJ in ATP. J Biol Chem 270:22535-22540
    • (1995) J Biol Chem , vol.270 , pp. 22535-22540
    • King, C.1    Eisenberg, E.2    Greene, L.3
  • 22
    • 0025205189 scopus 로고
    • (Mg-ATP)-dependent self-assembly of molecular chaperone GroEL
    • Lissin NM, Venyaminov S, Girshovich AS (1990) (Mg-ATP)-dependent self-assembly of molecular chaperone GroEL. Nature 348:339-342
    • (1990) Nature , vol.348 , pp. 339-342
    • Lissin, N.M.1    Venyaminov, S.2    Girshovich, A.S.3
  • 23
    • 0014945433 scopus 로고
    • Calcium-dependent bacteriophage DNA infection
    • Mandel M, Higa A (1970) Calcium-dependent bacteriophage DNA infection. J Mol Biol 53:159-162
    • (1970) J Mol Biol , vol.53 , pp. 159-162
    • Mandel, M.1    Higa, A.2
  • 25
    • 0013805762 scopus 로고
    • A regulator gene that is dominant on an episome and recessive on a chromosome
    • Markovitz A, Rosenbaum N (1965) A regulator gene that is dominant on an episome and recessive on a chromosome. Proc Natl Acad Sci USA 54:1084-1091
    • (1965) Proc Natl Acad Sci USA , vol.54 , pp. 1084-1091
    • Markovitz, A.1    Rosenbaum, N.2
  • 26
    • 0027954650 scopus 로고
    • DnaK mutants defective in ATPase activity are defective in negative regulation of the heat shock response: Expression of mutant DnaK proteins results in filamentation
    • McCarty JS, Walker GC (1994) DnaK mutants defective in ATPase activity are defective in negative regulation of the heat shock response: expression of mutant DnaK proteins results in filamentation. J Bacteriol 176:764-780
    • (1994) J Bacteriol , vol.176 , pp. 764-780
    • McCarty, J.S.1    Walker, G.C.2
  • 27
    • 0029922568 scopus 로고    scopus 로고
    • Mutational analysis of Hsp90 alpha dimerization and subcellular localization: Dimer disruption does not impede in vivo interaction with estrogen receptor
    • Meng X, Devin J, Sullivan WP, Toft D, Baulieu EE, Catelli MG (1996) Mutational analysis of Hsp90 alpha dimerization and subcellular localization: dimer disruption does not impede in vivo interaction with estrogen receptor. J Cell Sci 109:1677-1687
    • (1996) J Cell Sci , vol.109 , pp. 1677-1687
    • Meng, X.1    Devin, J.2    Sullivan, W.P.3    Toft, D.4    Baulieu, E.E.5    Catelli, M.G.6
  • 28
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Miller JH (1972) Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 29
    • 0026772142 scopus 로고
    • DNA sequence analysis of the dnaK gene of Escherichia coli B and of two dnaK genes carrying the temperature-sensitive mutations dnaK7(Ts) and dnaK756(Ts)
    • Miyazaki T, Tanaka S, Fujita H, Itikawa H (1992) DNA sequence analysis of the dnaK gene of Escherichia coli B and of two dnaK genes carrying the temperature-sensitive mutations dnaK7(Ts) and dnaK756(Ts). J Bacteriol 174:3715-3722
    • (1992) J Bacteriol , vol.174 , pp. 3715-3722
    • Miyazaki, T.1    Tanaka, S.2    Fujita, H.3    Itikawa, H.4
  • 31
    • 0025100983 scopus 로고
    • An essential member of the HSP70 gene family of Saccharomyces cerevisiae is homologous to immunoglobulin heavy chain binding protein
    • Nicholson RC, Williams DB, Moran LA (1990) An essential member of the HSP70 gene family of Saccharomyces cerevisiae is homologous to immunoglobulin heavy chain binding protein. Proc Natl Acad Sci USA 87:1159-1163
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 1159-1163
    • Nicholson, R.C.1    Williams, D.B.2    Moran, L.A.3
  • 32
    • 0027537708 scopus 로고
    • Initiation of lambda DNA replication. The Escherichis coli small heat shock proteins. DnaJ and GrpE, increase DnaK's affinity for the lambda P protein
    • Osipiuk J, Georgopoulos C, Zylicz M (1993) Initiation of lambda DNA replication. The Escherichis coli small heat shock proteins. DnaJ and GrpE, increase DnaK's affinity for the lambda P protein. J Biol Chem 268:4821-4827
    • (1993) J Biol Chem , vol.268 , pp. 4821-4827
    • Osipiuk, J.1    Georgopoulos, C.2    Zylicz, M.3
  • 33
    • 0023123175 scopus 로고
    • Escherichia coli dnaK null mutants are inviable at high temperature
    • Pack KH, Walker GC (1987) Escherichia coli dnaK null mutants are inviable at high temperature. J Bacteriol 169:283-290
    • (1987) J Bacteriol , vol.169 , pp. 283-290
    • Pack, K.H.1    Walker, G.C.2
  • 34
    • 0026063035 scopus 로고
    • Interaction of hsp70 with unfolded proteins: Effects of temperature and nucleotides on the kinetics of binding
    • Palleros DR, Welch WJ, Fink AL (1991) Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding. Proc Natl Acad Sci USA 88:5719-5723
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5719-5723
    • Palleros, D.R.1    Welch, W.J.2    Fink, A.L.3
  • 36
    • 0028929052 scopus 로고
    • The DnaK chaperone system of Escherichia coli: Quaternary structures and interactions of the DnaK and GrpE components
    • Schönfeld HJ, Schmidt D, Schröder H, Bukau B (1995) The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components. J Biol Chem 270:2183-2189
    • (1995) J Biol Chem , vol.270 , pp. 2183-2189
    • Schönfeld, H.J.1    Schmidt, D.2    Schröder, H.3    Bukau, B.4
  • 38
    • 0032474433 scopus 로고    scopus 로고
    • NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: A preview of chaperone-protein interaction
    • Wang H, Kurochkin AV, Pang Y, Hu W, Flynn GC, Zuiderweg ERP (1998) NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction. Biochemistry 37:7929-7940
    • (1998) Biochemistry , vol.37 , pp. 7929-7940
    • Wang, H.1    Kurochkin, A.V.2    Pang, Y.3    Hu, W.4    Flynn, G.C.5    Zuiderweg, E.R.P.6
  • 39
    • 0026684855 scopus 로고
    • Partial loss-of-function mutations in DnaK, the Escherichia coli homologue of the 70-kDa heat shock proteins, affect highly conserved amino acids implicated in ATP binding and hydrolysis
    • Wild J, Kamath-Loeb A, Ziegelhoffer E, Lonetto M, Kawasaki Y, Gross CA (1992) Partial loss-of-function mutations in DnaK, the Escherichia coli homologue of the 70-kDa heat shock proteins, affect highly conserved amino acids implicated in ATP binding and hydrolysis. Proc Natl Acad Sci USA 89:7139-7143
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7139-7143
    • Wild, J.1    Kamath-Loeb, A.2    Ziegelhoffer, E.3    Lonetto, M.4    Kawasaki, Y.5    Gross, C.A.6
  • 40
    • 0025992789 scopus 로고
    • Residual guanosine 3′, 5′ -bispyrophosphate synthetic activity of rclA null mutants can be eliminated by spoT null mutations
    • Xiao H, Kalman M, Ikehara K, Zemel S, Glaser G, Cashel M (1991) Residual guanosine 3′, 5′ -bispyrophosphate synthetic activity of rclA null mutants can be eliminated by spoT null mutations. J Biol Chem 266:5980-5990
    • (1991) J Biol Chem , vol.266 , pp. 5980-5990
    • Xiao, H.1    Kalman, M.2    Ikehara, K.3    Zemel, S.4    Glaser, G.5    Cashel, M.6
  • 41
    • 0021137114 scopus 로고
    • Purification and properties of the Escherichia coli DnaK replication protein
    • Zylicz M, Georgopoulos C (1984) Purification and properties of the Escherichia coli DnaK replication protein. J Biol Chem 259:8820-8825
    • (1984) J Biol Chem , vol.259 , pp. 8820-8825
    • Zylicz, M.1    Georgopoulos, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.