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Volumn 69, Issue 4, 2008, Pages 926-937

Periplasmic chaperone FkpA is essential for imported colicin M toxicity

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; COLICIN M; HISTIDINE; PEPTIDYLPROLYL ISOMERASE; PROTEIN FKPA; PROTEINASE K; TACROLIMUS;

EID: 47749139311     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2008.06327.x     Document Type: Article
Times cited : (43)

References (47)
  • 1
    • 0035188469 scopus 로고    scopus 로고
    • Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli
    • Arié, J.P., Sassoon, N. Betton, J.M. (2001) Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli. Mol Microbiol 39 : 199 210.
    • (2001) Mol Microbiol , vol.39 , pp. 199-210
    • Arié, J.P.1    Sassoon, N.2    Betton, J.M.3
  • 2
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: The Keio collection
    • Baba, T., Ara, T., Hasegawa, M., Takai, Y., Okumura, Y., Baba, M., et al. (2006) Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol Syst Biol 2 : E1 E11.
    • (2006) Mol Syst Biol , vol.2
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5    Baba, M.6
  • 3
    • 0035863210 scopus 로고    scopus 로고
    • The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity
    • Behrens, S., Maier, R., de Cock, H., Schmid, F.X. Gross, C.A. (2001) The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. EMBO J 20 : 285 294.
    • (2001) EMBO J , vol.20 , pp. 285-294
    • Behrens, S.1    Maier, R.2    De Cock, H.3    Schmid, F.X.4    Gross, C.A.5
  • 4
    • 0026541379 scopus 로고
    • Colicin a unfolds during its translocation in Escherichia coli cells and spans the whole cell envelope when its pore has formed
    • Benedetti, H., Lloubes, R., Lazdunski, C. Letellier, L. (1992) Colicin A unfolds during its translocation in Escherichia coli cells and spans the whole cell envelope when its pore has formed. EMBO J 11 : 441 447.
    • (1992) EMBO J , vol.11 , pp. 441-447
    • Benedetti, H.1    Lloubes, R.2    Lazdunski, C.3    Letellier, L.4
  • 5
    • 47749148726 scopus 로고    scopus 로고
    • Periplasmic chaperones and peptidyl-prolyl isomerases
    • In. Ehrmann, M. (ed.). Washington, DC: American Society for Microbiology Press, pp.
    • Betton, J.M. (2007) Periplasmic chaperones and peptidyl-prolyl isomerases. In The Periplasm. Ehrmann, M. (ed.). Washington, DC : American Society for Microbiology Press, pp. 141 149.
    • (2007) The Periplasm. , pp. 141-149
    • Betton, J.M.1
  • 7
    • 0039423955 scopus 로고    scopus 로고
    • The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA - I. Increased functional expression of antibody fragments with and without cis-prolines
    • Bothmann, H. Plückthun, A. (2000) The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA - I. Increased functional expression of antibody fragments with and without cis-prolines. J Biol Chem 275 : 17100 17105.
    • (2000) J Biol Chem , vol.275 , pp. 17100-17105
    • Bothmann, H.1    Plückthun, A.2
  • 8
    • 0042838110 scopus 로고    scopus 로고
    • In vivo reconstitution of the FhuA transport protein of Escherichia coli K-12
    • Braun, M., Endriss, F., Killmann, H. Braun, V. (2003) In vivo reconstitution of the FhuA transport protein of Escherichia coli K-12. J Bacteriol 185 : 5508 5518.
    • (2003) J Bacteriol , vol.185 , pp. 5508-5518
    • Braun, M.1    Endriss, F.2    Killmann, H.3    Braun, V.4
  • 9
    • 0029155042 scopus 로고
    • Energy-coupled transport and signal-transduction through the gram-negative outer-membrane via TonB-ExbB-ExbD-dependent receptor proteins
    • Braun, V. (1995) Energy-coupled transport and signal-transduction through the gram-negative outer-membrane via TonB-ExbB-ExbD-dependent receptor proteins. FEMS Microbiol Rev 16 : 295 307.
    • (1995) FEMS Microbiol Rev , vol.16 , pp. 295-307
    • Braun, V.1
  • 11
    • 0018946246 scopus 로고
    • Penetration of colicin M into cells of Escherichia coli
    • Braun, V., Frenz, J., Hantke, K. Schaller, K. (1980) Penetration of colicin M into cells of Escherichia coli. J Bacteriol 142 : 162 168.
    • (1980) J Bacteriol , vol.142 , pp. 162-168
    • Braun, V.1    Frenz, J.2    Hantke, K.3    Schaller, K.4
  • 12
    • 0036589164 scopus 로고    scopus 로고
    • Ton-dependent colicins and microcins: Modular design and evolution
    • Braun, V., Patzer, S.I. Hantke, K. (2002) Ton-dependent colicins and microcins: modular design and evolution. Biochimie 84 : 365 380.
    • (2002) Biochimie , vol.84 , pp. 365-380
    • Braun, V.1    Patzer, S.I.2    Hantke, K.3
  • 13
    • 33744754593 scopus 로고    scopus 로고
    • Ferrichrome- and citrate-mediated iron transport
    • In. Crosa, J.H., Mey, A.R., Payne, S.M. (eds). Washington, DC: American Society for Microbiology Press, pp.
    • Braun, V., Braun, M. Killmann, H. (2004) Ferrichrome- and citrate-mediated iron transport. In Iron Transport in Bacteria. Crosa, J.H., Mey, A.R., Payne, S.M. (eds). Washington, DC : American Society for Microbiology Press, pp. 158 177.
    • (2004) Iron Transport in Bacteria. , pp. 158-177
    • Braun, V.1    Braun, M.2    Killmann, H.3
  • 14
    • 34249095469 scopus 로고    scopus 로고
    • Structure of colicin I receptor bound to the R-domain of colicin Ia: Implications for protein import
    • Buchanan, S.K., Lukacik, P., Grizot, S., Ghirlando, R., Ali, M.M., Barnard, T.J., et al. (2007) Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import. EMBO J 26 : 2594 2604.
    • (2007) EMBO J , vol.26 , pp. 2594-2604
    • Buchanan, S.K.1    Lukacik, P.2    Grizot, S.3    Ghirlando, R.4    Ali, M.M.5    Barnard, T.J.6
  • 15
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu
    • Casadaban, M.J. (1976) Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J Mol Biol 104 : 541 555.
    • (1976) J Mol Biol , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 17
    • 0029886388 scopus 로고    scopus 로고
    • A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins
    • Chen, R. Henning, U. (1996) A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Mol Microbiol 19 : 1287 1294.
    • (1996) Mol Microbiol , vol.19 , pp. 1287-1294
    • Chen, R.1    Henning, U.2
  • 19
    • 0027938907 scopus 로고
    • Unfolding of colicin a during its translocation through the Escherichia coli envelope as demonstrated by disulfide bond engineering
    • Duché, D., Baty, D., Chartier, M. Letellier, L. (1994) Unfolding of colicin A during its translocation through the Escherichia coli envelope as demonstrated by disulfide bond engineering. J Biol Chem 269 : 24820 24825.
    • (1994) J Biol Chem , vol.269 , pp. 24820-24825
    • Duché, D.1    Baty, D.2    Chartier, M.3    Letellier, L.4
  • 20
    • 33747354636 scopus 로고    scopus 로고
    • Colicin M exerts its bacteriolytic effect via enzymatic degradation of undecaprenyl phosphate-linked peptidoglycan precursors
    • El Ghachi, M., Bouhss, A., Barreteau, H., Touze, T., Auger, G., Blanot, D. Mengin-Lecreulx, D. (2006) Colicin M exerts its bacteriolytic effect via enzymatic degradation of undecaprenyl phosphate-linked peptidoglycan precursors. J Biol Chem 281 : 22761 22772.
    • (2006) J Biol Chem , vol.281 , pp. 22761-22772
    • El Ghachi, M.1    Bouhss, A.2    Barreteau, H.3    Touze, T.4    Auger, G.5    Blanot, D.6    Mengin-Lecreulx, D.7
  • 21
    • 0030007664 scopus 로고    scopus 로고
    • Colicin M is inactivated during import by its immunity protein
    • Groß, P. Braun, V. (1996) Colicin M is inactivated during import by its immunity protein. Mol Gen Genet 251 : 388 396.
    • (1996) Mol Gen Genet , vol.251 , pp. 388-396
    • Groß, P.1    Braun, V.2
  • 22
    • 0024520998 scopus 로고
    • Colicin M inhibits peptidoglycan biosynthesis by interfering with lipid carrier recycling
    • Harkness, R.E. Braun, V. (1989) Colicin M inhibits peptidoglycan biosynthesis by interfering with lipid carrier recycling. J Biol Chem 264 : 6177 6182.
    • (1989) J Biol Chem , vol.264 , pp. 6177-6182
    • Harkness, R.E.1    Braun, V.2
  • 23
    • 0025280089 scopus 로고
    • Colicin M is only bactericidal when provided from outside the cell
    • Harkness, R.E. Braun, V. (1990) Colicin M is only bactericidal when provided from outside the cell. Mol Gen Genet 222 : 37 40.
    • (1990) Mol Gen Genet , vol.222 , pp. 37-40
    • Harkness, R.E.1    Braun, V.2
  • 24
    • 0022500907 scopus 로고
    • Overproduction of the proFhuA outer membrane receptor protein of Escherichia coli K-12: Isolation, properties, and immunocytochemical localization at the inner side of the cytoplasmic membrane
    • Hoffmann, H., Fischer, E., Schwarz, H. Braun, V. (1986) Overproduction of the proFhuA outer membrane receptor protein of Escherichia coli K-12: isolation, properties, and immunocytochemical localization at the inner side of the cytoplasmic membrane. Arch Microbiol 145 : 334 341.
    • (1986) Arch Microbiol , vol.145 , pp. 334-341
    • Hoffmann, H.1    Fischer, E.2    Schwarz, H.3    Braun, V.4
  • 25
    • 33749363905 scopus 로고    scopus 로고
    • Structural plasticity of peptidyl-prolyl isomerase sFkpA is a key to its chaperone function as revealed by solution NMR
    • Hu, K., Galius, V. Pervushin, K. (2006) Structural plasticity of peptidyl-prolyl isomerase sFkpA is a key to its chaperone function as revealed by solution NMR. Biochemistry 45 : 11983 11991.
    • (2006) Biochemistry , vol.45 , pp. 11983-11991
    • Hu, K.1    Galius, V.2    Pervushin, K.3
  • 27
    • 0029836552 scopus 로고    scopus 로고
    • Ligand-induced conformational change in the ferrichrome-iron receptor of Escherichia coli K-12
    • Moeck, G.S., Tawa, P., Xiang, H., Ismail, A.A., Turnbull, J.L. Coulton, J.W. (1996) Ligand-induced conformational change in the ferrichrome-iron receptor of Escherichia coli K-12. Mol Microbiol 22 : 459 471.
    • (1996) Mol Microbiol , vol.22 , pp. 459-471
    • Moeck, G.S.1    Tawa, P.2    Xiang, H.3    Ismail, A.A.4    Turnbull, J.L.5    Coulton, J.W.6
  • 28
    • 22144495426 scopus 로고    scopus 로고
    • Interactions between folding factors and bacterial outer membrane proteins
    • Mogensen, J.E. Otzen, D.E. (2005) Interactions between folding factors and bacterial outer membrane proteins. Mol Microbiol 57 : 326 346.
    • (2005) Mol Microbiol , vol.57 , pp. 326-346
    • Mogensen, J.E.1    Otzen, D.E.2
  • 29
    • 0025794355 scopus 로고
    • Binding of the immunity protein inactivates colicin M
    • Ölschläger, T., Turba, A. Braun, V. (1991) Binding of the immunity protein inactivates colicin M. Mol Microbiol 5 : 1105 1111.
    • (1991) Mol Microbiol , vol.5 , pp. 1105-1111
    • Ölschläger, T.1    Turba, A.2    Braun, V.3
  • 31
    • 0042065285 scopus 로고    scopus 로고
    • Touch and go: Tying TonB to transport
    • Postle, K. Kadner, R.J. (2003) Touch and go: tying TonB to transport. Mol Microbiol 49 : 869 882.
    • (2003) Mol Microbiol , vol.49 , pp. 869-882
    • Postle, K.1    Kadner, R.J.2
  • 32
    • 0038831330 scopus 로고    scopus 로고
    • The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro
    • Ramm, K. Plückthun, A. (2000) The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro. J Biol Chem 275 : 17106 17113.
    • (2000) J Biol Chem , vol.275 , pp. 17106-17113
    • Ramm, K.1    Plückthun, A.2
  • 33
    • 0035816225 scopus 로고    scopus 로고
    • High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA
    • Ramm, K. Plückthun, A. (2001) High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA. J Mol Biol 310 : 485 498.
    • (2001) J Mol Biol , vol.310 , pp. 485-498
    • Ramm, K.1    Plückthun, A.2
  • 34
    • 0035161025 scopus 로고    scopus 로고
    • Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli
    • Rizzitello, A.E., Harper, J.R. Silhavy, T.J. (2001) Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli. J Bacteriol 183 : 6794 6800.
    • (2001) J Bacteriol , vol.183 , pp. 6794-6800
    • Rizzitello, A.E.1    Harper, J.R.2    Silhavy, T.J.3
  • 35
    • 0030476750 scopus 로고    scopus 로고
    • SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins
    • Rouviere, P.E. Gross, C.A. (1996) SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. Genes Dev 10 : 3170 3182.
    • (1996) Genes Dev , vol.10 , pp. 3170-3182
    • Rouviere, P.E.1    Gross, C.A.2
  • 36
    • 0346366809 scopus 로고    scopus 로고
    • Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity
    • Saul, F.A., Arie, J.P., Vulliez-le Normand, B., Kahn, R., Betton, J.M. Bentley, G.A. (2004) Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. J Mol Biol 335 : 595 608.
    • (2004) J Mol Biol , vol.335 , pp. 595-608
    • Saul, F.A.1    Arie, J.P.2    Vulliez-Le Normand, B.3    Kahn, R.4    Betton, J.M.5    Bentley, G.A.6
  • 37
    • 0038105593 scopus 로고    scopus 로고
    • Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins
    • Schäfer, U., Beck, K. Müller, M. (1999) Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J Biol Chem 274 : 24567 24574.
    • (1999) J Biol Chem , vol.274 , pp. 24567-24574
    • Schäfer, U.1    Beck, K.2    Müller, M.3
  • 38
    • 0019355106 scopus 로고
    • Temperature-sensitive, colicin M-tolerant mutant of Escherichia coli
    • Schaller, K., Krauel, A. Braun, V. (1981) Temperature-sensitive, colicin M-tolerant mutant of Escherichia coli. J Bacteriol 147 : 135 139.
    • (1981) J Bacteriol , vol.147 , pp. 135-139
    • Schaller, K.1    Krauel, A.2    Braun, V.3
  • 39
    • 0020366141 scopus 로고
    • Colicin M is an inhibitor of murein biosynthesis
    • Schaller, K., Höltje, J.-V. Braun, V. (1982) Colicin M is an inhibitor of murein biosynthesis. J Bacteriol 152 : 994 1000.
    • (1982) J Bacteriol , vol.152 , pp. 994-1000
    • Schaller, K.1    Höltje, J.-V.2    Braun, V.3
  • 40
    • 0024676062 scopus 로고
    • Transport across the outer membrane of Escherichia coli K12 via the FhuA receptor is regulated by the TonB protein of the cytoplasmic membrane
    • Schöffler, H. Braun, V. (1989) Transport across the outer membrane of Escherichia coli K12 via the FhuA receptor is regulated by the TonB protein of the cytoplasmic membrane. Mol Gen Genet 217 : 378 383.
    • (1989) Mol Gen Genet , vol.217 , pp. 378-383
    • Schöffler, H.1    Braun, V.2
  • 41
    • 34548179597 scopus 로고    scopus 로고
    • Structure of the complex of the colicin E2 R-domain and its BtuB receptor. the outer membrane colicin translocon
    • Sharma, O., Yamashita, E., Zhalnina, M.V., Zakharov, S.D., Datsenko, K.A., Wanner, B.L. Cramer, W.A. (2007) Structure of the complex of the colicin E2 R-domain and its BtuB receptor. The outer membrane colicin translocon. J Biol Chem 282 : 23163 23170.
    • (2007) J Biol Chem , vol.282 , pp. 23163-23170
    • Sharma, O.1    Yamashita, E.2    Zhalnina, M.V.3    Zakharov, S.D.4    Datsenko, K.A.5    Wanner, B.L.6    Cramer, W.A.7
  • 42
    • 34948827356 scopus 로고    scopus 로고
    • Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli
    • Sklar, J.G., Wu, T., Kahne, D. Silhavy, T.J. (2007) Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli. Genes Dev 21 : 2473 2484.
    • (2007) Genes Dev , vol.21 , pp. 2473-2484
    • Sklar, J.G.1    Wu, T.2    Kahne, D.3    Silhavy, T.J.4
  • 43
    • 0035930345 scopus 로고    scopus 로고
    • Crystal structure of colicin E3: Implications for cell entry and ribosome inactivation
    • Soelaiman, S., Jakes, K., Wu, N., Li, C. Shoham, M. (2001) Crystal structure of colicin E3: implications for cell entry and ribosome inactivation. Mol Cell 8 : 1053 1062.
    • (2001) Mol Cell , vol.8 , pp. 1053-1062
    • Soelaiman, S.1    Jakes, K.2    Wu, N.3    Li, C.4    Shoham, M.5
  • 44
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F.W. Moffatt, B.A. (1986) Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189 : 113 130.
    • (1986) J Mol Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 47
    • 2442666884 scopus 로고    scopus 로고
    • On the mechanism and pathway of colicin import across the E. coli outer membrane
    • Zakharov, S.D. Cramer, W.A. (2004) On the mechanism and pathway of colicin import across the E. coli outer membrane. Front Biosci 9 : 1311 1317.
    • (2004) Front Biosci , vol.9 , pp. 1311-1317
    • Zakharov, S.D.1    Cramer, W.A.2


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