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Volumn 62, Issue 1, 2006, Pages 201-211

Requirement for the acetyl phosphate pathway in Escherichia coli ATP-dependent proteolysis

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID; ACETIC ACID DERIVATIVE; ADENOSINE TRIPHOSPHATE; PHOSPHATE; PUROMYCIN;

EID: 33748672490     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2006.05360.x     Document Type: Article
Times cited : (17)

References (59)
  • 1
    • 0033770817 scopus 로고    scopus 로고
    • Control of methionine biosynthesis in Escherichia coli by proteolysis
    • Biran, D., Gur, E., Gollan, L., and Ron, E.Z. (2000) Control of methionine biosynthesis in Escherichia coli by proteolysis. Mol Microbiol 37: 1436-1443.
    • (2000) Mol Microbiol , vol.37 , pp. 1436-1443
    • Biran, D.1    Gur, E.2    Gollan, L.3    Ron, E.Z.4
  • 2
    • 0031939765 scopus 로고    scopus 로고
    • Regulation of RssB-dependent proteolysis in Escherichia coli: A role for acetyl phosphate in a response regulator-controlled process
    • Bouche, S., Klauck, E., Fischer, D., Lucassen, M., Jung, K., and Hengge-Aronis, R. (1998) Regulation of RssB-dependent proteolysis in Escherichia coli: a role for acetyl phosphate in a response regulator-controlled process. Mol Microbiol 27: 787-795.
    • (1998) Mol Microbiol , vol.27 , pp. 787-795
    • Bouche, S.1    Klauck, E.2    Fischer, D.3    Lucassen, M.4    Jung, K.5    Hengge-Aronis, R.6
  • 3
    • 0027318150 scopus 로고
    • Change in direction of flagellar rotation in Escherichia coli mediated by acetate kinase
    • Dailey, F.E., and Berg, H.C. (1993) Change in direction of flagellar rotation in Escherichia coli mediated by acetate kinase. J Bacteriol 175: 3236-3239.
    • (1993) J Bacteriol , vol.175 , pp. 3236-3239
    • Dailey, F.E.1    Berg, H.C.2
  • 4
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 5
    • 0026709953 scopus 로고
    • In vitro phosphorylation of AlgR, a regulator of mucoidy in Pseudomonas aeruginosa, by a histidine protein kinase and effects of small phospho-donor molecules
    • Deretic, V., Leveau, J.H., Mohr, C.D., and Hibler, N.S. (1992) In vitro phosphorylation of AlgR, a regulator of mucoidy in Pseudomonas aeruginosa, by a histidine protein kinase and effects of small phospho-donor molecules. Mol Microbiol 6: 2761-2767.
    • (1992) Mol Microbiol , vol.6 , pp. 2761-2767
    • Deretic, V.1    Leveau, J.H.2    Mohr, C.D.3    Hibler, N.S.4
  • 6
    • 0036210995 scopus 로고    scopus 로고
    • ClpS, a substrate modulator of the ClpAP machine
    • Dougan, D.A., Reid, B.G., Horwich, A.L., and Bukau, B. (2002) ClpS, a substrate modulator of the ClpAP machine. Mol Cell 9: 673-683.
    • (2002) Mol Cell , vol.9 , pp. 673-683
    • Dougan, D.A.1    Reid, B.G.2    Horwich, A.L.3    Bukau, B.4
  • 7
    • 32544432878 scopus 로고    scopus 로고
    • ClpS is an essential component of the N-end rule pathway in Escherichia coli
    • Erbse, A., Schmidt, R., Bornemann, T., Schneider-Mergener, J., Mogk, A., Zahn, R., et al. (2006) ClpS is an essential component of the N-end rule pathway in Escherichia coli. Nature 439: 753-756.
    • (2006) Nature , vol.439 , pp. 753-756
    • Erbse, A.1    Schmidt, R.2    Bornemann, T.3    Schneider-Mergener, J.4    Mogk, A.5    Zahn, R.6
  • 8
    • 25144452838 scopus 로고    scopus 로고
    • Cytoplasmic degradation of ssrA-tagged proteins
    • Farrell, C.M., Grossman, A.D., and Sauer, R.T. (2005) Cytoplasmic degradation of ssrA-tagged proteins. Mol Microbiol 57: 1750-1761.
    • (2005) Mol Microbiol , vol.57 , pp. 1750-1761
    • Farrell, C.M.1    Grossman, A.D.2    Sauer, R.T.3
  • 9
    • 0026662751 scopus 로고
    • Role of phosphorylated metabolic intermediates in the regulation of glutamine synthetase synthesis in Escherichia coli
    • Feng, J., Atkinson, M.R., McCleary, W., Stock, J.B., Wanner, B.L., and Ninfa, A.J. (1992) Role of phosphorylated metabolic intermediates in the regulation of glutamine synthetase synthesis in Escherichia coli. J Bacteriol 174: 6061-6070.
    • (1992) J Bacteriol , vol.174 , pp. 6061-6070
    • Feng, J.1    Atkinson, M.R.2    McCleary, W.3    Stock, J.B.4    Wanner, B.L.5    Ninfa, A.J.6
  • 10
    • 0037351068 scopus 로고    scopus 로고
    • Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals
    • Flynn, J.M., Neher, S.B., Kim, Y.I., Sauer, R.T., and Baker, T.A. (2003) Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol Cell 11: 671-683.
    • (2003) Mol Cell , vol.11 , pp. 671-683
    • Flynn, J.M.1    Neher, S.B.2    Kim, Y.I.3    Sauer, R.T.4    Baker, T.A.5
  • 11
    • 33748295599 scopus 로고    scopus 로고
    • Acetyl phosphate-sensitive regulation of flagellar biogenesis and capsular biosynthesis depends on the Rcs phosphorelay
    • Fredericks, C.E., Shibata, S., Aizawa, S.I., Reimann, S.A., and Wolfe, A.J. (2006) Acetyl phosphate-sensitive regulation of flagellar biogenesis and capsular biosynthesis depends on the Rcs phosphorelay. Mol Microbiol 61: 734-747.
    • (2006) Mol Microbiol , vol.61 , pp. 734-747
    • Fredericks, C.E.1    Shibata, S.2    Aizawa, S.I.3    Reimann, S.A.4    Wolfe, A.J.5
  • 12
    • 0015292247 scopus 로고
    • Degradation of abnormal proteins in Escherichia coli (protein breakdown-protein structure-mistranslation-amino acid analogs-puromycin)
    • Goldberg, A.L. (1972) Degradation of abnormal proteins in Escherichia coli (protein breakdown-protein structure-mistranslation-amino acid analogs-puromycin). Proc Natl Acad Sci USA 69: 422-426.
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 422-426
    • Goldberg, A.L.1
  • 13
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg, A.L. (2003) Protein degradation and protection against misfolded or damaged proteins. Nature 426: 895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 14
    • 0344824655 scopus 로고    scopus 로고
    • Proteolysis in bacterial regulatory circuits
    • Gottesman, S. (2003) Proteolysis in bacterial regulatory circuits. Annu Rev Cell Dev Biol 19: 565-587.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 565-587
    • Gottesman, S.1
  • 15
    • 0023322682 scopus 로고
    • Sigma 32 synthesis can regulate the synthesis of heat shock proteins in Escherichia coli
    • Grossman, A.D., Straus, D.B., Walter, W.A., and Gross, C.A. (1987) Sigma 32 synthesis can regulate the synthesis of heat shock proteins in Escherichia coli. Genes Dev 1: 179-184.
    • (1987) Genes Dev , vol.1 , pp. 179-184
    • Grossman, A.D.1    Straus, D.B.2    Walter, W.A.3    Gross, C.A.4
  • 16
    • 0027364289 scopus 로고
    • ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities
    • Gottesman, S., Clark, W.P., de Crecy-Lagard, V., and Maurizi, M.R. (1993) ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities. J Biol Chem 268: 22618-22626.
    • (1993) J Biol Chem , vol.268 , pp. 22618-22626
    • Gottesman, S.1    Clark, W.P.2    De Crecy-Lagard, V.3    Maurizi, M.R.4
  • 17
    • 0030726160 scopus 로고    scopus 로고
    • Regulatory subunits of energy-dependent proteases
    • Gottesman, S., Maurizi, M.R., and Wickner, S. (1997) Regulatory subunits of energy-dependent proteases. Cell 91: 435-438.
    • (1997) Cell , vol.91 , pp. 435-438
    • Gottesman, S.1    Maurizi, M.R.2    Wickner, S.3
  • 18
    • 8644290874 scopus 로고    scopus 로고
    • A chaperone network controls the heat shock response in E. coli
    • Guisbert, E., Herman, C., Lu, C.Z., and 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
  • 19
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose pBAD promoter
    • Guzman, L.M., Belin, D., Carson, M.J., and Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose pBAD promoter. J Bacteriol 177: 4121-4130.
    • (1995) J Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 20
    • 0141789762 scopus 로고    scopus 로고
    • Proteolysis in prokaryotes: Protein quality control and regulatory principles
    • Hengge, R., and Bukau, B. (2003) Proteolysis in prokaryotes: protein quality control and regulatory principles. Mol Microbiol 49: 1451-1462.
    • (2003) Mol Microbiol , vol.49 , pp. 1451-1462
    • Hengge, R.1    Bukau, B.2
  • 21
    • 0029144247 scopus 로고
    • Autophosphorylation and activation of transcriptional activator PhoB of Escherichia coli by acetyl phosphate in vitro
    • Hiratsu, K., Nakata, A., Shinagawa, H., and Makino, K. (1995) Autophosphorylation and activation of transcriptional activator PhoB of Escherichia coli by acetyl phosphate in vitro. Gene 161: 7-10.
    • (1995) Gene , vol.161 , pp. 7-10
    • Hiratsu, K.1    Nakata, A.2    Shinagawa, H.3    Makino, K.4
  • 22
    • 0034035586 scopus 로고    scopus 로고
    • Two-component and phosphorelay signal transduction
    • Hoch, J.A. (2000) Two-component and phosphorelay signal transduction. Curr Opin Microbiol 3: 165-170.
    • (2000) Curr Opin Microbiol , vol.3 , pp. 165-170
    • Hoch, J.A.1
  • 23
    • 0035830914 scopus 로고    scopus 로고
    • The molecular chaperone DnaJ is required for the degradation of a soluble abnormal protein in Escherichia coli
    • Huang, H.C., Sherman, M.Y., Kandror, O., and Goldberg, A.L. (2001) The molecular chaperone DnaJ is required for the degradation of a soluble abnormal protein in Escherichia coli. J Biol Chem 276: 3920-3928.
    • (2001) J Biol Chem , vol.276 , pp. 3920-3928
    • Huang, H.C.1    Sherman, M.Y.2    Kandror, O.3    Goldberg, A.L.4
  • 25
    • 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., and 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
  • 26
    • 0030613795 scopus 로고    scopus 로고
    • Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli
    • Kanemori, M., Nishihara, K., Yanagi, H., and Yura, T. (1997) Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli. J Bacteriol 179: 7219-7225.
    • (1997) J Bacteriol , vol.179 , pp. 7219-7225
    • Kanemori, M.1    Nishihara, K.2    Yanagi, H.3    Yura, T.4
  • 27
    • 0033023919 scopus 로고    scopus 로고
    • The ATP-dependent HslVU/ClpQY protease participates in turnover of cell division inhibitor SulA in Escherichia coli
    • Kanemori, M., Yanagi, H., and Yura, T. (1999) The ATP-dependent HslVU/ClpQY protease participates in turnover of cell division inhibitor SulA in Escherichia coli. J Bacteriol 181: 3674-3680.
    • (1999) J Bacteriol , vol.181 , pp. 3674-3680
    • Kanemori, M.1    Yanagi, H.2    Yura, T.3
  • 28
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
    • Keiler, K.C., Waller, P.R., and Sauer, R.T. (1996) Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA. Science 271: 990-993.
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.2    Sauer, R.T.3
  • 29
    • 0029844678 scopus 로고    scopus 로고
    • Involvement of the sensor kinase EnvZ in the in vivo activation of the response-regulator PhoB by acetyl phosphate
    • Kim, S.K., Wilmes-Riesenberg, M.R., and Wanner, B.L. (1996) Involvement of the sensor kinase EnvZ in the in vivo activation of the response-regulator PhoB by acetyl phosphate. Mol Microbiol 22: 135-147.
    • (1996) Mol Microbiol , vol.22 , pp. 135-147
    • Kim, S.K.1    Wilmes-Riesenberg, M.R.2    Wanner, B.L.3
  • 30
    • 0035958678 scopus 로고    scopus 로고
    • Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli
    • Kuroda, A., Nomura, K., Ohtomo, R., Kato, J., Ikeda, T., Takiguchi, N., et al. (2001) Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli. Science 293: 705-708.
    • (2001) Science , vol.293 , pp. 705-708
    • Kuroda, A.1    Nomura, K.2    Ohtomo, R.3    Kato, J.4    Ikeda, T.5    Takiguchi, N.6
  • 31
    • 0035266072 scopus 로고    scopus 로고
    • ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
    • Lee, C., Schwartz, M.P., Prakash, S., Iwakura, M., and Matouschek, A. (2001) ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol Cell 7: 627-637.
    • (2001) Mol Cell , vol.7 , pp. 627-637
    • Lee, C.1    Schwartz, M.P.2    Prakash, S.3    Iwakura, M.4    Matouschek, A.5
  • 32
    • 0034730496 scopus 로고    scopus 로고
    • A specificity-enhancing factor for the ClpXP degradation machine
    • Levchenko, I., Seidel, M., Sauer, R.T., and Baker, T.A. (2000) A specificity-enhancing factor for the ClpXP degradation machine. Science 289: 2354-2356.
    • (2000) Science , vol.289 , pp. 2354-2356
    • Levchenko, I.1    Seidel, M.2    Sauer, R.T.3    Baker, T.A.4
  • 33
    • 0026512864 scopus 로고
    • Phosphorylation of bacterial response regulator proteins by low molecular weight phospho-donors
    • Lukat, G.S., McCleary, W.R., Stock, A.M., and Stock, J.B. (1992) Phosphorylation of bacterial response regulator proteins by low molecular weight phospho-donors. Proc Natl Acad Sci USA 89: 718-722.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 718-722
    • Lukat, G.S.1    McCleary, W.R.2    Stock, A.M.3    Stock, J.B.4
  • 34
    • 0029896773 scopus 로고    scopus 로고
    • The activation of PhoB by acetylphosphate
    • McCleary, W.R. (1996) The activation of PhoB by acetylphosphate. Mol Microbiol 20: 1155-1163.
    • (1996) Mol Microbiol , vol.20 , pp. 1155-1163
    • McCleary, W.R.1
  • 35
    • 0028075844 scopus 로고
    • Acetyl phosphate and the activation of two-component response regulators
    • McCleary, W.R., and Stock, J.B. (1994) Acetyl phosphate and the activation of two-component response regulators. J Biol Chem 269: 31567-31572.
    • (1994) J Biol Chem , vol.269 , pp. 31567-31572
    • McCleary, W.R.1    Stock, J.B.2
  • 36
    • 0027207516 scopus 로고
    • Is acetyl phosphate a global signal in Escherichia coli?
    • McCleary, W.R., Stock, J.B., and Ninfa, A.J. (1993) Is acetyl phosphate a global signal in Escherichia coli? J Bacteriol 175: 2793-2798.
    • (1993) J Bacteriol , vol.175 , pp. 2793-2798
    • McCleary, W.R.1    Stock, J.B.2    Ninfa, A.J.3
  • 37
    • 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., and 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
  • 38
    • 0029990928 scopus 로고    scopus 로고
    • The response regulator RssB controls stability of the sigma(S) subunit of RNA polymerase in Escherichia coli
    • Muffler, A., Fischer, D., Altuvia, S., Storz, G., and Hengge-Aronis, R. (1996) The response regulator RssB controls stability of the sigma(S) subunit of RNA polymerase in Escherichia coli. EMBO J 15: 1333-1339.
    • (1996) EMBO J , vol.15 , pp. 1333-1339
    • Muffler, A.1    Fischer, D.2    Altuvia, S.3    Storz, G.4    Hengge-Aronis, R.5
  • 39
    • 4544343195 scopus 로고    scopus 로고
    • Effects of inorganic polyphosphate on the proteolytic and DNA-binding activities of Lon in Escherichia coli
    • Nomura, K., Kato, J., Takiguchi, N., Ohtake, H., and Kuroda, A. (2004) Effects of inorganic polyphosphate on the proteolytic and DNA-binding activities of Lon in Escherichia coli. J Biol Chem 279: 34406-34410.
    • (2004) J Biol Chem , vol.279 , pp. 34406-34410
    • Nomura, K.1    Kato, J.2    Takiguchi, N.3    Ohtake, H.4    Kuroda, A.5
  • 40
    • 0034502532 scopus 로고    scopus 로고
    • Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP
    • Ortega, J., Singh, S.K., Ishikawa, T., Maurizi, M.R., and Steven, A.C. (2000) Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP. Mol Cell 6: 1515-1521.
    • (2000) Mol Cell , vol.6 , pp. 1515-1521
    • Ortega, J.1    Singh, S.K.2    Ishikawa, T.3    Maurizi, M.R.4    Steven, A.C.5
  • 41
    • 0037119954 scopus 로고    scopus 로고
    • Alternating translocation of protein substrates from both ends of ClpXP protease
    • Ortega, J., Lee, H.S., Maurizi, M.R., and Steven, A.C. (2002) Alternating translocation of protein substrates from both ends of ClpXP protease. EMBO J 21: 4938-4949.
    • (2002) EMBO J , vol.21 , pp. 4938-4949
    • Ortega, J.1    Lee, H.S.2    Maurizi, M.R.3    Steven, A.C.4
  • 42
    • 6044235523 scopus 로고    scopus 로고
    • RpoS proteolysis is regulated by a mechanism that does not require the SprE (RssB) response regulator phosphorylation site
    • Peterson, C.N., Ruiz, N., and Silhavy, T.J. (2004) RpoS proteolysis is regulated by a mechanism that does not require the SprE (RssB) response regulator phosphorylation site. J Bacteriol 186: 7403-7410.
    • (2004) J Bacteriol , vol.186 , pp. 7403-7410
    • Peterson, C.N.1    Ruiz, N.2    Silhavy, T.J.3
  • 43
    • 0016442420 scopus 로고
    • Degradation of abnormal proteins in Escherichia coli. Formation of protein inclusions in cells exposed to amino acid analogs
    • Prouty, W.F., Karnovsky, M.J., and Goldberg, A.L. (1975) Degradation of abnormal proteins in Escherichia coli. Formation of protein inclusions in cells exposed to amino acid analogs. J Biol Chem 250: 1112-1122.
    • (1975) J Biol Chem , vol.250 , pp. 1112-1122
    • Prouty, W.F.1    Karnovsky, M.J.2    Goldberg, A.L.3
  • 44
    • 0028340662 scopus 로고
    • Regulation of acetyl phosphate synthesis and degradation, and the control of flagellar expression in Escherichia coli
    • Pruss, B.M., and Wolfe, A.J. (1994) Regulation of acetyl phosphate synthesis and degradation, and the control of flagellar expression in Escherichia coli. Mol Microbiol 12: 973-984.
    • (1994) Mol Microbiol , vol.12 , pp. 973-984
    • Pruss, B.M.1    Wolfe, A.J.2
  • 47
    • 14544289538 scopus 로고    scopus 로고
    • A defect in the acetyl coenzyme A. acetate pathway poisons recombinational repair-deficient mutants of Escherichia coli
    • Shi, I.Y., Stansbury, J., and Kuzminov, A. (2005) A defect in the acetyl coenzyme A. acetate pathway poisons recombinational repair-deficient mutants of Escherichia coli. J Bacteriol 187: 1266-1275.
    • (2005) J Bacteriol , vol.187 , pp. 1266-1275
    • Shi, I.Y.1    Stansbury, J.2    Kuzminov, A.3
  • 48
    • 0141566368 scopus 로고    scopus 로고
    • Dynamic control of Dps protein levels by ClpXP and ClpAP proteases in Escherichia coli
    • Stephani, K., Weichart, D., and Hengge, R. (2003) Dynamic control of Dps protein levels by ClpXP and ClpAP proteases in Escherichia coli. Mol Microbiol 49: 1605-1614.
    • (2003) Mol Microbiol , vol.49 , pp. 1605-1614
    • Stephani, K.1    Weichart, D.2    Hengge, R.3
  • 50
    • 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., and 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
  • 51
    • 0035029482 scopus 로고    scopus 로고
    • Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol
    • Tomoyasu, T., Mogk, A., Langen, H., Goloubinoff, P., and Bukau, B. (2001) Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol. Mol Microbiol 40: 397-413.
    • (2001) Mol Microbiol , vol.40 , pp. 397-413
    • Tomoyasu, T.1    Mogk, A.2    Langen, H.3    Goloubinoff, P.4    Bukau, B.5
  • 52
    • 0033134869 scopus 로고    scopus 로고
    • Aggregates in neurodegenerative disease: Crowds and power?
    • Tran, P.B., and Miller, R.J. (1999) Aggregates in neurodegenerative disease: crowds and power? Trends Neurosci 22: 194-197.
    • (1999) Trends Neurosci , vol.22 , pp. 194-197
    • Tran, P.B.1    Miller, R.J.2
  • 53
    • 0023278164 scopus 로고
    • Involvement of ack-pta operon products in alpha-ketobutyrate metabolism by Salmonella typhimurium
    • Van Dyk, T.K., and LaRossa, R.A. (1987) Involvement of ack-pta operon products in alpha-ketobutyrate metabolism by Salmonella typhimurium. Mol Gen Genet 207: 435-440.
    • (1987) Mol Gen Genet , vol.207 , pp. 435-440
    • Van Dyk, T.K.1    LaRossa, R.A.2
  • 54
    • 0023391343 scopus 로고
    • Induction of the heat shock regulon does not produce thermotolerance in Escherichia coli
    • VanBogelen, R.A., Acton, M.A., and Neidhardt, F.C. (1987) Induction of the heat shock regulon does not produce thermotolerance in Escherichia coli. Genes Dev 1: 525-531.
    • (1987) Genes Dev , vol.1 , pp. 525-531
    • VanBogelen, R.A.1    Acton, M.A.2    Neidhardt, F.C.3
  • 55
    • 0026576546 scopus 로고
    • Is cross regulation by phosphorylation of two-component response regulator proteins important in bacteria?
    • Wanner, B.L. (1992) Is cross regulation by phosphorylation of two-component response regulator proteins important in bacteria? J Bacteriol 174: 2053-2058.
    • (1992) J Bacteriol , vol.174 , pp. 2053-2058
    • Wanner, B.L.1
  • 56
    • 0033520987 scopus 로고    scopus 로고
    • Post-translational quality control: Folding, refolding, and degrading proteins
    • Wickner, S., Maurizi, M.R., and Gottesman, S. (1999) Post-translational 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
  • 57
    • 0027519423 scopus 로고
    • Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli
    • Wojtkowiak, D., Georgopoulos, C., and Zylicz, M. (1993) Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli. J Biol Chem 268: 22609-22617.
    • (1993) J Biol Chem , vol.268 , pp. 22609-22617
    • Wojtkowiak, D.1    Georgopoulos, C.2    Zylicz, M.3


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