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Volumn 97, Issue 5, 2015, Pages 822-831

Regulated intramembrane proteolysis of the virulence activator TcpP in Vibrio cholerae is initiated by the tail-specific protease (Tsp)

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; METALLOPROTEINASE; PROTEIN TCPH; PROTEIN TCPP; PROTEIN TCPPA172; PROTEIN TCPPI174; PROTEIN TSP; PROTEIN YAEL; PROTEINASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; VIRULENCE FACTOR; BACTERIAL PROTEIN; C-TERMINAL PROCESSING PEPTIDASE; DNA BINDING PROTEIN; TCPP PROTEIN, VIBRIO CHOLERAE;

EID: 84940466998     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.13069     Document Type: Article
Times cited : (26)

References (38)
  • 1
    • 84930367653 scopus 로고    scopus 로고
    • Proteolysis of virulence regulator ToxR is associated with entry of Vibrio cholerae into a dormant state
    • Almagro-Moreno, S., Kim, T.K., Skorupski, K., and Taylor, R.K. (2015) Proteolysis of virulence regulator ToxR is associated with entry of Vibrio cholerae into a dormant state. PLoS Genet 11: e1005145.
    • (2015) PLoS Genet , vol.11 , pp. e1005145
    • Almagro-Moreno, S.1    Kim, T.K.2    Skorupski, K.3    Taylor, R.K.4
  • 2
    • 84905381153 scopus 로고    scopus 로고
    • The Prc and RseP proteases control bacterial cell-surface signalling activity
    • Bastiaansen, K.C., Ibanez, A., Ramos, J.L., Bitter, W., and Llamas, M.A. (2014) The Prc and RseP proteases control bacterial cell-surface signalling activity. Environ Microbiol 16: 2433-2443.
    • (2014) Environ Microbiol , vol.16 , pp. 2433-2443
    • Bastiaansen, K.C.1    Ibanez, A.2    Ramos, J.L.3    Bitter, W.4    Llamas, M.A.5
  • 3
    • 10044288424 scopus 로고    scopus 로고
    • TcpH influences virulence gene expression in Vibrio cholerae by inhibiting degradation of the transcription activator TcpP
    • Beck, N.A., Krukonis, E.S., and DiRita, V.J. (2004) TcpH influences virulence gene expression in Vibrio cholerae by inhibiting degradation of the transcription activator TcpP. J Bacteriol 186: 8309-8316.
    • (2004) J Bacteriol , vol.186 , pp. 8309-8316
    • Beck, N.A.1    Krukonis, E.S.2    DiRita, V.J.3
  • 4
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans
    • Brown, M.S., Ye, J., Rawson, R.B., and Goldstein, J.L. (2000) Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell 100: 391-398.
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 5
    • 47249101480 scopus 로고    scopus 로고
    • A defined transposon mutant library and its use in identifying motility genes in Vibrio cholerae
    • Cameron, D.E., Urbach, J.M., and Mekalanos, J.J. (2008) A defined transposon mutant library and its use in identifying motility genes in Vibrio cholerae. Proc Natl Acad Sci USA 105: 8736-8741.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 8736-8741
    • Cameron, D.E.1    Urbach, J.M.2    Mekalanos, J.J.3
  • 6
    • 79952146175 scopus 로고    scopus 로고
    • Signal integration by DegS and RseB governs the sigmaE-mediated envelope stress response in Escherichia coli
    • Chaba, R., Alba, B.M., Guo, M.S., Sohn, J., Ahuja, N., Sauer, R.T., and Gross, C.A. (2011) Signal integration by DegS and RseB governs the sigmaE-mediated envelope stress response in Escherichia coli. Proc Natl Acad Sci USA 108: 2106-2111.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 2106-2111
    • Chaba, R.1    Alba, B.M.2    Guo, M.S.3    Sohn, J.4    Ahuja, N.5    Sauer, R.T.6    Gross, C.A.7
  • 7
    • 84860557951 scopus 로고    scopus 로고
    • Proteolytic regulation of alginate overproduction in Pseudomonas aeruginosa
    • Damron, F.H., and Goldberg, J.B. (2012) Proteolytic regulation of alginate overproduction in Pseudomonas aeruginosa. Mol Microbiol 84: 595-607.
    • (2012) Mol Microbiol , vol.84 , pp. 595-607
    • Damron, F.H.1    Goldberg, J.B.2
  • 8
    • 0026098804 scopus 로고
    • Periplasmic interaction between two membrane regulatory proteins, ToxR and ToxS, results in signal transduction and transcriptional activation
    • DiRita, V.J., and Mekalanos, J.J. (1991) Periplasmic interaction between two membrane regulatory proteins, ToxR and ToxS, results in signal transduction and transcriptional activation. Cell 64: 29-37.
    • (1991) Cell , vol.64 , pp. 29-37
    • DiRita, V.J.1    Mekalanos, J.J.2
  • 9
    • 7544239890 scopus 로고    scopus 로고
    • Fine-tuning of the Escherichia coli sigmaE envelope stress response relies on multiple mechanisms to inhibit signal-independent proteolysis of the transmembrane anti-sigma factor, RseA
    • Grigorova, I.L., Chaba, R., Zhong, H.J., Alba, B.M., Rhodius, V., Herman, C., and Gross, C.A. (2004) Fine-tuning of the Escherichia coli sigmaE envelope stress response relies on multiple mechanisms to inhibit signal-independent proteolysis of the transmembrane anti-sigma factor, RseA. Genes Dev 18: 2686-2697.
    • (2004) Genes Dev , vol.18 , pp. 2686-2697
    • Grigorova, I.L.1    Chaba, R.2    Zhong, H.J.3    Alba, B.M.4    Rhodius, V.5    Herman, C.6    Gross, C.A.7
  • 10
    • 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
  • 11
    • 0030825248 scopus 로고    scopus 로고
    • Pentapeptide scanning mutagenesis: random insertion of a variable five amino acid cassette in a target protein
    • Hallet, B., Sherratt, D.J., and Hayes, F. (1997) Pentapeptide scanning mutagenesis: random insertion of a variable five amino acid cassette in a target protein. Nucleic Acids Res 25: 1866-1867.
    • (1997) Nucleic Acids Res , vol.25 , pp. 1866-1867
    • Hallet, B.1    Sherratt, D.J.2    Hayes, F.3
  • 12
    • 0024450646 scopus 로고
    • Genetic analyses of processing involving C-terminal cleavage in penicillin-binding protein 3 of Escherichia coli
    • Hara, H., Nishimura, Y., Kato, J., Suzuki, H., Nagasawa, H., Suzuki, A., and Hirota, Y. (1989) Genetic analyses of processing involving C-terminal cleavage in penicillin-binding protein 3 of Escherichia coli. J Bacteriol 171: 5882-5889.
    • (1989) J Bacteriol , vol.171 , pp. 5882-5889
    • Hara, H.1    Nishimura, Y.2    Kato, J.3    Suzuki, H.4    Nagasawa, H.5    Suzuki, A.6    Hirota, Y.7
  • 13
    • 0025832094 scopus 로고
    • Cloning, mapping, and characterization of the Escherichia coli prc gene, which is involved in C-terminal processing of penicillin-binding protein 3
    • Hara, H., Yamamoto, Y., Higashitani, A., Suzuki, H., and Nishimura, Y. (1991) Cloning, mapping, and characterization of the Escherichia coli prc gene, which is involved in C-terminal processing of penicillin-binding protein 3. J Bacteriol 173: 4799-4813.
    • (1991) J Bacteriol , vol.173 , pp. 4799-4813
    • Hara, H.1    Yamamoto, Y.2    Higashitani, A.3    Suzuki, H.4    Nishimura, Y.5
  • 14
    • 0031930690 scopus 로고    scopus 로고
    • TcpP protein is a positive regulator of virulence gene expression in Vibrio cholerae
    • Hase, C.C., and Mekalanos, J.J. (1998) TcpP protein is a positive regulator of virulence gene expression in Vibrio cholerae. Proc Natl Acad Sci USA 95: 730-734.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 730-734
    • Hase, C.C.1    Mekalanos, J.J.2
  • 15
    • 35348985928 scopus 로고    scopus 로고
    • Regulation of the sigmaE stress response by DegS: how the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress
    • Hasselblatt, H., Kurzbauer, R., Wilken, C., Krojer, T., Sawa, J., Kurt, J., etal. (2007) Regulation of the sigmaE stress response by DegS: how the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress. Genes Dev 21: 2659-2670.
    • (2007) Genes Dev , vol.21 , pp. 2659-2670
    • Hasselblatt, H.1    Kurzbauer, R.2    Wilken, C.3    Krojer, T.4    Sawa, J.5    Kurt, J.6
  • 16
    • 0034957021 scopus 로고    scopus 로고
    • Isolation and characterization of a temperature-sensitive generalized transducing bacteriophage for Vibrio cholerae
    • Hava, D.L., and Camilli, A. (2001) Isolation and characterization of a temperature-sensitive generalized transducing bacteriophage for Vibrio cholerae. J Microbiol Methods 46: 217-225.
    • (2001) J Microbiol Methods , vol.46 , pp. 217-225
    • Hava, D.L.1    Camilli, A.2
  • 17
    • 0023701409 scopus 로고
    • Lipid modification of Escherichia coli penicillin-binding protein 3
    • Hayashi, S., Hara, H., Suzuki, H., and Hirota, Y. (1988) Lipid modification of Escherichia coli penicillin-binding protein 3. J Bacteriol 170: 5392-5395.
    • (1988) J Bacteriol , vol.170 , pp. 5392-5395
    • Hayashi, S.1    Hara, H.2    Suzuki, H.3    Hirota, Y.4
  • 18
    • 72049093490 scopus 로고    scopus 로고
    • Two proteolytic modules are involved in regulated intramembrane proteolysis of Bacillus subtilis RsiW
    • Heinrich, J., Hein, K., and Wiegert, T. (2009) Two proteolytic modules are involved in regulated intramembrane proteolysis of Bacillus subtilis RsiW. Mol Microbiol 74: 1412-1426.
    • (2009) Mol Microbiol , vol.74 , pp. 1412-1426
    • Heinrich, J.1    Hein, K.2    Wiegert, T.3
  • 19
    • 0030063988 scopus 로고    scopus 로고
    • Sequence determinants of C-terminal substrate recognition by the Tsp protease
    • Keiler, K.C., and Sauer, R.T. (1996) Sequence determinants of C-terminal substrate recognition by the Tsp protease. J Biol Chem 271: 2589-2593.
    • (1996) J Biol Chem , vol.271 , pp. 2589-2593
    • Keiler, K.C.1    Sauer, R.T.2
  • 20
    • 0029115371 scopus 로고
    • C-terminal specific protein degradation: activity and substrate specificity of the Tsp protease
    • Keiler, K.C., Silber, K.R., Downard, K.M., Papayannopoulous, I.A., Biemann, K., and Sauer, R.T. (1995) C-terminal specific protein degradation: activity and substrate specificity of the Tsp protease. Protein Sci 4: 1507-1515.
    • (1995) Protein Sci , vol.4 , pp. 1507-1515
    • Keiler, K.C.1    Silber, K.R.2    Downard, K.M.3    Papayannopoulous, I.A.4    Biemann, K.5    Sauer, R.T.6
  • 21
    • 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
  • 22
    • 0032798521 scopus 로고    scopus 로고
    • A Vibrio cholerae LysR homolog, AphB, cooperates with AphA at the tcpPH promoter to activate expression of the ToxR virulence cascade
    • Kovacikova, G., and Skorupski, K. (1999) A Vibrio cholerae LysR homolog, AphB, cooperates with AphA at the tcpPH promoter to activate expression of the ToxR virulence cascade. J Bacteriol 181: 4250-4256.
    • (1999) J Bacteriol , vol.181 , pp. 4250-4256
    • Kovacikova, G.1    Skorupski, K.2
  • 23
    • 0031566431 scopus 로고    scopus 로고
    • Structural relationships in the OmpR family of winged-helix transcription factors
    • Martinez-Hackert, E., and Stock, A.M. (1997) Structural relationships in the OmpR family of winged-helix transcription factors. J Mol Biol 269: 301-312.
    • (1997) J Mol Biol , vol.269 , pp. 301-312
    • Martinez-Hackert, E.1    Stock, A.M.2
  • 24
    • 28044455049 scopus 로고    scopus 로고
    • Degradation of the membrane-localized virulence activator TcpP by the YaeL protease in Vibrio cholerae
    • Matson, J.S., and DiRita, V.J. (2005) Degradation of the membrane-localized virulence activator TcpP by the YaeL protease in Vibrio cholerae. Proc Natl Acad Sci USA 102: 16403-16408.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16403-16408
    • Matson, J.S.1    DiRita, V.J.2
  • 25
    • 36749079251 scopus 로고    scopus 로고
    • Regulatory networks controlling Vibrio cholerae virulence gene expression
    • Matson, J.S., Withey, J.H., and DiRita, V.J. (2007) Regulatory networks controlling Vibrio cholerae virulence gene expression. Infect Immun 75: 5542-5549.
    • (2007) Infect Immun , vol.75 , pp. 5542-5549
    • Matson, J.S.1    Withey, J.H.2    DiRita, V.J.3
  • 26
  • 27
    • 0037047379 scopus 로고    scopus 로고
    • Parallel quorum sensing systems converge to regulate virulence in Vibrio cholerae
    • Miller, M.B., Skorupski, K., Lenz, D.H., Taylor, R.K., and Bassler, B.L. (2002) Parallel quorum sensing systems converge to regulate virulence in Vibrio cholerae. Cell 110: 303-314.
    • (2002) Cell , vol.110 , pp. 303-314
    • Miller, M.B.1    Skorupski, K.2    Lenz, D.H.3    Taylor, R.K.4    Bassler, B.L.5
  • 28
    • 0024439293 scopus 로고
    • Determination of the cleavage site involved in C-terminal processing of penicillin-binding protein 3 of Escherichia coli
    • Nagasawa, H., Sakagami, Y., Suzuki, A., Suzuki, H., Hara, H., and Hirota, Y. (1989) Determination of the cleavage site involved in C-terminal processing of penicillin-binding protein 3 of Escherichia coli. J Bacteriol 171: 5890-5893.
    • (1989) J Bacteriol , vol.171 , pp. 5890-5893
    • Nagasawa, H.1    Sakagami, Y.2    Suzuki, A.3    Suzuki, H.4    Hara, H.5    Hirota, Y.6
  • 29
    • 84864544883 scopus 로고    scopus 로고
    • Different mutations in mucA gene of Pseudomonas aeruginosa mucoid strains in cystic fibrosis patients and their effect on algU gene expression
    • Pulcrano, G., Iula, D.V., Raia, V., Rossano, F., and Catania, M.R. (2012) Different mutations in mucA gene of Pseudomonas aeruginosa mucoid strains in cystic fibrosis patients and their effect on algU gene expression. New Microbiol 35: 295-305.
    • (2012) New Microbiol , vol.35 , pp. 295-305
    • Pulcrano, G.1    Iula, D.V.2    Raia, V.3    Rossano, F.4    Catania, M.R.5
  • 30
    • 34249950054 scopus 로고    scopus 로고
    • Regulated proteolysis controls mucoid conversion in Pseudomonas aeruginosa
    • Qiu, D., Eisinger, V.M., Rowen, D.W., and Yu, H.D. (2007) Regulated proteolysis controls mucoid conversion in Pseudomonas aeruginosa. Proc Natl Acad Sci USA 104: 8107-8112.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8107-8112
    • Qiu, D.1    Eisinger, V.M.2    Rowen, D.W.3    Yu, H.D.4
  • 34
    • 0029926274 scopus 로고    scopus 로고
    • Positive selection vectors for allelic exchange
    • Skorupski, K., and Taylor, R.K. (1996) Positive selection vectors for allelic exchange. Gene 169: 47-52.
    • (1996) Gene , vol.169 , pp. 47-52
    • Skorupski, K.1    Taylor, R.K.2
  • 35
    • 70349779534 scopus 로고    scopus 로고
    • OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism
    • Sohn, J., Grant, R.A., and Sauer, R.T. (2009) OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism. Structure 17: 1411-1421.
    • (2009) Structure , vol.17 , pp. 1411-1421
    • Sohn, J.1    Grant, R.A.2    Sauer, R.T.3
  • 36
    • 0019206171 scopus 로고
    • On the process of cellular division in Escherichia coli: isolation and characterization of penicillin-binding proteins 1a, 1b, and 3
    • Tamura, T., Suzuki, H., Nishimura, Y., Mizoguchi, J., and Hirota, Y. (1980) On the process of cellular division in Escherichia coli: isolation and characterization of penicillin-binding proteins 1a, 1b, and 3. Proc Natl Acad Sci USA 77: 4499-4503.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 4499-4503
    • Tamura, T.1    Suzuki, H.2    Nishimura, Y.3    Mizoguchi, J.4    Hirota, Y.5
  • 37
    • 84856569623 scopus 로고    scopus 로고
    • Chemical biology approaches reveal conserved features of a C-terminal processing PDZ protease
    • Weski, J., Meltzer, M., Spaan, L., Monig, T., Oeljeklaus, J., Hauseke, P., etal. (2012) Chemical biology approaches reveal conserved features of a C-terminal processing PDZ protease. Chembiochem 13: 402-408.
    • (2012) Chembiochem , vol.13 , pp. 402-408
    • Weski, J.1    Meltzer, M.2    Spaan, L.3    Monig, T.4    Oeljeklaus, J.5    Hauseke, P.6
  • 38
    • 33749181103 scopus 로고    scopus 로고
    • Cell wall-inhibitory antibiotics activate the alginate biosynthesis operon in Pseudomonas aeruginosa: roles of sigma (AlgT) and the AlgW and Prc proteases
    • Wood, L.F., Leech, A.J., and Ohman, D.E. (2006) Cell wall-inhibitory antibiotics activate the alginate biosynthesis operon in Pseudomonas aeruginosa: roles of sigma (AlgT) and the AlgW and Prc proteases. Mol Microbiol 62: 412-426.
    • (2006) Mol Microbiol , vol.62 , pp. 412-426
    • Wood, L.F.1    Leech, A.J.2    Ohman, D.E.3


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