메뉴 건너뛰기




Volumn 42, Issue 6, 2008, Pages 506-513

Periplasmic chaperone FkpA reduces extracytoplasmic stress response and improves cell-surface display on Escherichia coli

Author keywords

Cell physiology; Cell surface display; Chaperone; FkpA; Recombinant protein production; Stress regulon; Yellow fluorescent protein

Indexed keywords

CELL PHYSIOLOGY; CELL-SURFACE DISPLAY; CHAPERONE; ENHANCED YELLOW FLUORESCENCE PROTEIN (EYFP); RECOMBINANT PROTEIN PRODUCTION; STRESS REGULON; YELLOW FLUORESCENT PROTEINS;

EID: 41149140751     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2008.01.019     Document Type: Article
Times cited : (5)

References (43)
  • 1
    • 1842558298 scopus 로고    scopus 로고
    • E in Escherichia coli
    • E in Escherichia coli. Curr Opin Microbiol 7 (2004) 157-162
    • (2004) Curr Opin Microbiol , vol.7 , pp. 157-162
    • Ades, S.E.1
  • 2
    • 2442563573 scopus 로고    scopus 로고
    • E-dependent envelope stress response
    • E-dependent envelope stress response. Mol Microbiol 5 (2004) 613-619
    • (2004) Mol Microbiol , vol.5 , pp. 613-619
    • Alba, B.M.1    Gross, C.A.2
  • 3
    • 0035188469 scopus 로고    scopus 로고
    • Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli
    • Arie J.P., Sassoon N., and Betton J.M. Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli. Mol Microbiol 39 (2001) 199-210
    • (2001) Mol Microbiol , vol.39 , pp. 199-210
    • Arie, J.P.1    Sassoon, N.2    Betton, J.M.3
  • 4
    • 13844257519 scopus 로고    scopus 로고
    • A generic system for the Escherichia coli cell-surface display of lipolytic enzymes
    • Becker S., Theile S., Heppeler N., Michalczyk A., Wentzel A., Wilhelm S., et al. A generic system for the Escherichia coli cell-surface display of lipolytic enzymes. FEBS Lett 579 (2005) 1177-1182
    • (2005) FEBS Lett , vol.579 , pp. 1177-1182
    • Becker, S.1    Theile, S.2    Heppeler, N.3    Michalczyk, A.4    Wentzel, A.5    Wilhelm, S.6
  • 5
    • 0035249432 scopus 로고    scopus 로고
    • Biotechnological applications of phage and cell display
    • Benhar I. Biotechnological applications of phage and cell display. Biotechnol Adv 19 (2001) 1-33
    • (2001) Biotechnol Adv , vol.19 , pp. 1-33
    • Benhar, I.1
  • 6
    • 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., and Pluckthun A. 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 (2000) 17100-17105
    • (2000) J Biol Chem , vol.275 , pp. 17100-17105
    • Bothmann, H.1    Pluckthun, A.2
  • 7
    • 0037026254 scopus 로고    scopus 로고
    • Cell-surface display of heterologous proteins: from high-throughput screening to environmental applications
    • Chen W., and Georgiou G. Cell-surface display of heterologous proteins: from high-throughput screening to environmental applications. Biotechnol Bioeng 79 (2002) 496-503
    • (2002) Biotechnol Bioeng , vol.79 , pp. 496-503
    • Chen, W.1    Georgiou, G.2
  • 8
    • 0027161270 scopus 로고
    • Preparation and storage of competent Escherichia coli cells
    • Chung C.T., and Miller R.H. Preparation and storage of competent Escherichia coli cells. Meth Enzymol 218 (1993) 621-627
    • (1993) Meth Enzymol , vol.218 , pp. 621-627
    • Chung, C.T.1    Miller, R.H.2
  • 9
    • 0031905590 scopus 로고    scopus 로고
    • CpxP, a stress-combative member of the Cpx regulon
    • Danese P.N., and Silhavy T.J. CpxP, a stress-combative member of the Cpx regulon. J Bacteriol 180 (1998) 831-839
    • (1998) J Bacteriol , vol.180 , pp. 831-839
    • Danese, P.N.1    Silhavy, T.J.2
  • 10
    • 0030998321 scopus 로고    scopus 로고
    • E and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli
    • E and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli. Genes & Development 11 (1997) 1183-1193
    • (1997) Genes & Development , vol.11 , pp. 1183-1193
    • Danese, P.N.1    Silhavy, T.J.2
  • 11
    • 0028951033 scopus 로고
    • The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP
    • Danese P.N., Snyder W.B., Cosma C.L., Davis L.J.B., and Silhavy T.J. The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP. Genes Dev 9 (1995) 387-398
    • (1995) Genes Dev , vol.9 , pp. 387-398
    • Danese, P.N.1    Snyder, W.B.2    Cosma, C.L.3    Davis, L.J.B.4    Silhavy, T.J.5
  • 12
    • 8844237557 scopus 로고    scopus 로고
    • Quality control in the bacterial periplasm
    • Duguay A.R., and Silhavy T.J. Quality control in the bacterial periplasm. Biochim Biophys Acta 1694 (2004) 121-134
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 121-134
    • Duguay, A.R.1    Silhavy, T.J.2
  • 13
    • 0024727149 scopus 로고
    • E subunit of Escherichia coli RNA polymerase-a second alternate σ factor involved in high-temperature gene expression
    • E subunit of Escherichia coli RNA polymerase-a second alternate σ factor involved in high-temperature gene expression. Genes Dev 3 (1989) 1462-1471
    • (1989) Genes Dev , vol.3 , pp. 1462-1471
    • Erickson, J.W.1    Gross, C.A.2
  • 14
    • 0023367975 scopus 로고
    • Regulation of the promoters and transcripts of rpoH, the Escherichia coli heat shock regulatory gene
    • Erickson J.W., Vaughn V., Walter W.A., Neidhardt F.C., and Gross C.A. Regulation of the promoters and transcripts of rpoH, the Escherichia coli heat shock regulatory gene. Genes Dev 1 (1987) 419-432
    • (1987) Genes Dev , vol.1 , pp. 419-432
    • Erickson, J.W.1    Vaughn, V.2    Walter, W.A.3    Neidhardt, F.C.4    Gross, C.A.5
  • 15
    • 0027425230 scopus 로고
    • Production and fluorescence-activated cell sorting of Escherichia coli expressing a functional antibody fragment on the external surface
    • Francisco J.A., Campbell R., Iverson B.L., and Georgiou G. Production and fluorescence-activated cell sorting of Escherichia coli expressing a functional antibody fragment on the external surface. Proc Natl Acad Sci USA 90 (1993) 10444-10448
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10444-10448
    • Francisco, J.A.1    Campbell, R.2    Iverson, B.L.3    Georgiou, G.4
  • 16
    • 0026594374 scopus 로고
    • Transport and anchoring of β-lactamase to the external surface of Escherichia coli
    • Francisco J.A., Earhart C.F., and Georgiou G. Transport and anchoring of β-lactamase to the external surface of Escherichia coli. Proc Natl Acad Sci USA 89 (1992) 2713-2717
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2713-2717
    • Francisco, J.A.1    Earhart, C.F.2    Georgiou, G.3
  • 17
    • 0029983637 scopus 로고    scopus 로고
    • Display of β-lactamase on the Escherichia coli surface: outer membrane phenotypes conferred by Lpp'-OmpA'-β-lactamase Fusions
    • Georgiou G., Stephens D., Stathopoulos L.C., Poetschke H.L., Mendenhall J., and Earhart C.F. Display of β-lactamase on the Escherichia coli surface: outer membrane phenotypes conferred by Lpp'-OmpA'-β-lactamase Fusions. Protein Eng 9 (1996) 239-247
    • (1996) Protein Eng , vol.9 , pp. 239-247
    • Georgiou, G.1    Stephens, D.2    Stathopoulos, L.C.3    Poetschke, H.L.4    Mendenhall, J.5    Earhart, C.F.6
  • 18
    • 29144519709 scopus 로고    scopus 로고
    • The extracytoplasmic adaptor protein CpxP is degraded with substrate by DegP
    • Isaac D.D., Pinkner J.S., Hultgren S.J., and Silhavy T.J. The extracytoplasmic adaptor protein CpxP is degraded with substrate by DegP. Proc Natl Acad Sci USA 102 (2005) 17775-17779
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17775-17779
    • Isaac, D.D.1    Pinkner, J.S.2    Hultgren, S.J.3    Silhavy, T.J.4
  • 19
    • 0346243935 scopus 로고    scopus 로고
    • YaeL proteolysis of RseA is controlled by the PDZ domain of YaeL and a Gln-rich region of RseA
    • Kanehara K.K., and Ito A.Y. YaeL proteolysis of RseA is controlled by the PDZ domain of YaeL and a Gln-rich region of RseA. EMBO J 22 (2003) 6389-6398
    • (2003) EMBO J , vol.22 , pp. 6389-6398
    • Kanehara, K.K.1    Ito, A.Y.2
  • 20
  • 22
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH
    • Missiakas D., Betton J.-M., and Raina S. New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH. Mol Microbiol 21 (1996) 871-884
    • (1996) Mol Microbiol , vol.21 , pp. 871-884
    • Missiakas, D.1    Betton, J.-M.2    Raina, S.3
  • 23
    • 0030907038 scopus 로고    scopus 로고
    • Modulation of the Escherichia coli sigmaE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins
    • Missiakas D., Mayer M.P., Lemaire M., Georgrgopoulos C., and Raina S. Modulation of the Escherichia coli sigmaE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins. Mol Microbiol 24 (1997) 355-371
    • (1997) Mol Microbiol , vol.24 , pp. 355-371
    • Missiakas, D.1    Mayer, M.P.2    Lemaire, M.3    Georgrgopoulos, C.4    Raina, S.5
  • 24
    • 4544222062 scopus 로고    scopus 로고
    • Effects of lipoprotein overproduction on the induction of DegP (HtrA) involved in quality control in the Escherichia coli periplasm
    • Miyadai H., Tanaka-Masuda K., Matsuayama S., and Tokuda H. Effects of lipoprotein overproduction on the induction of DegP (HtrA) involved in quality control in the Escherichia coli periplasm. J Biol Chem 279 (2004) 39807-39813
    • (2004) J Biol Chem , vol.279 , pp. 39807-39813
    • Miyadai, H.1    Tanaka-Masuda, K.2    Matsuayama, S.3    Tokuda, H.4
  • 26
  • 27
    • 0028272057 scopus 로고
    • The dam and dcm strains of Escherichia coli-a review
    • Palmer B.R., and Marinus M.G. The dam and dcm strains of Escherichia coli-a review. Gene 143 (1994) 1-12
    • (1994) Gene , vol.143 , pp. 1-12
    • Palmer, B.R.1    Marinus, M.G.2
  • 28
    • 0025017436 scopus 로고
    • Biosynthesis and function of phospholipids in Escherichia coli
    • Raetz C.R.H., and Dowhan W. Biosynthesis and function of phospholipids in Escherichia coli. J Biol Chem 265 (1990) 1235-1238
    • (1990) J Biol Chem , vol.265 , pp. 1235-1238
    • Raetz, C.R.H.1    Dowhan, W.2
  • 29
    • 0028920231 scopus 로고
    • The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of Escherichia coli
    • Raina S., Missiakas D., and Georgopoulos C. The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of Escherichia coli. EMBO J 14 (1995) 1043-1055
    • (1995) EMBO J , vol.14 , pp. 1043-1055
    • Raina, S.1    Missiakas, D.2    Georgopoulos, C.3
  • 30
    • 0033106492 scopus 로고    scopus 로고
    • E and Cpx regulatory pathways: overlapping but distinct envelope stress responses
    • E and Cpx regulatory pathways: overlapping but distinct envelope stress responses. Curr Opin Microbiol 2 (1999) 159-165
    • (1999) Curr Opin Microbiol , vol.2 , pp. 159-165
    • Raivio, T.L.1    Silhavy, T.J.2
  • 31
    • 0030834844 scopus 로고    scopus 로고
    • Transduction of envelope stress in Escherichia coli by the Cpx two-component system
    • Raivio T.L., and Silhavy T.J. Transduction of envelope stress in Escherichia coli by the Cpx two-component system. J Bacteriol 179 (1997) 7724-7733
    • (1997) J Bacteriol , vol.179 , pp. 7724-7733
    • Raivio, T.L.1    Silhavy, T.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., and Pluckthun A. The periplasmic Escherichia coli peptidylprolyl cis, trans-isomerase FkpA-II. Isomerase-independent chaperone activity in vitro. J Biol Chem 275 (2000) 17106-17113
    • (2000) J Biol Chem , vol.275 , pp. 17106-17113
    • Ramm, K.1    Pluckthun, A.2
  • 33
    • 15744389448 scopus 로고    scopus 로고
    • Sensing external stress: watchdogs of the Escherichia coli cell envelope
    • Ruiz N., and Silhavy T.J. Sensing external stress: watchdogs of the Escherichia coli cell envelope. Curr Opin Microbiol 8 (2005) 122-126
    • (2005) Curr Opin Microbiol , vol.8 , pp. 122-126
    • Ruiz, N.1    Silhavy, T.J.2
  • 35
    • 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., Normand B.V.L., Kahn R., Betton J.M., and Bentley G.A. Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. J Mol Biol 335 (2004) 595-608
    • (2004) J Mol Biol , vol.335 , pp. 595-608
    • Saul, F.A.1    Arie, J.P.2    Normand, B.V.L.3    Kahn, R.4    Betton, J.M.5    Bentley, G.A.6
  • 36
    • 11844279155 scopus 로고    scopus 로고
    • Functional solubilization of aggregation-prone HIV envelope proteins by covalent fusion with chaperone modules
    • Scholz C., Schaarschmidt P., Engel A.M., Andres H., Schmitt U., and Faatz E. Functional solubilization of aggregation-prone HIV envelope proteins by covalent fusion with chaperone modules. J Mol Biol 345 (2005) 1229-1241
    • (2005) J Mol Biol , vol.345 , pp. 1229-1241
    • Scholz, C.1    Schaarschmidt, P.2    Engel, A.M.3    Andres, H.4    Schmitt, U.5    Faatz, E.6
  • 37
    • 0342710346 scopus 로고    scopus 로고
    • Bacterial surface display: trends and progress
    • Stahl S., and Uhlen M. Bacterial surface display: trends and progress. Trends Biotechnol 15 (1997) 185-192
    • (1997) Trends Biotechnol , vol.15 , pp. 185-192
    • Stahl, S.1    Uhlen, M.2
  • 38
    • 0029916414 scopus 로고    scopus 로고
    • Characterization of Escherichia coli expressing an Lpp'OmpA(46-159)-PhoA fusion protein localized in the outer membrane
    • Stathopoulos C., Georgiou G., and Earhart C.F. Characterization of Escherichia coli expressing an Lpp'OmpA(46-159)-PhoA fusion protein localized in the outer membrane. Appl Microbiol Biotechnol 45 (1996) 112-119
    • (1996) Appl Microbiol Biotechnol , vol.45 , pp. 112-119
    • Stathopoulos, C.1    Georgiou, G.2    Earhart, C.F.3
  • 39
    • 0344953579 scopus 로고    scopus 로고
    • OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain
    • Walsh N.P., Alba B.M., Bose B., Gross C.A., and Sauer R.T. OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain. Cell 113 (2003) 61-71
    • (2003) Cell , vol.113 , pp. 61-71
    • Walsh, N.P.1    Alba, B.M.2    Bose, B.3    Gross, C.A.4    Sauer, R.T.5
  • 40
    • 0032721432 scopus 로고    scopus 로고
    • Wilhelm STJ, Jaeger KE. A novel lipolytic enzyme located in the outer membrane of Pseudomonas aeruginosa. J Bacteriol 1999;181:6977-86.
    • Wilhelm STJ, Jaeger KE. A novel lipolytic enzyme located in the outer membrane of Pseudomonas aeruginosa. J Bacteriol 1999;181:6977-86.
  • 41
    • 0024594736 scopus 로고
    • Quantitative evaluation of Escherichia coli host strains for tolerance to cytosine methylation in plasmid and phage recombinants
    • Woodcock D.M., Crowther P.J., Doherty J., Jefferson S., Decruz E., Noyerweidner M., et al. Quantitative evaluation of Escherichia coli host strains for tolerance to cytosine methylation in plasmid and phage recombinants. Nucleic Acids Res 17 (1989) 3469-3478
    • (1989) Nucleic Acids Res , vol.17 , pp. 3469-3478
    • Woodcock, D.M.1    Crowther, P.J.2    Doherty, J.3    Jefferson, S.4    Decruz, E.5    Noyerweidner, M.6
  • 42
    • 33947585117 scopus 로고    scopus 로고
    • Effect of heat-shock proteins for relieving physiological stress and enhancing the production of penicillin acylase in Escherichia coli
    • Wu M.S., Pan K.L., and Chou C.P. Effect of heat-shock proteins for relieving physiological stress and enhancing the production of penicillin acylase in Escherichia coli. Biotechnol Bioeng 96 (2007) 956-966
    • (2007) Biotechnol Bioeng , vol.96 , pp. 956-966
    • Wu, M.S.1    Pan, K.L.2    Chou, C.P.3
  • 43
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C., Vieira J., and Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33 (1985) 103-119
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.