메뉴 건너뛰기




Volumn 74, Issue 24, 2008, Pages 7821-7823

Influence of high pressure on the dimerization of ToxR, a protein involved in bacterial signal transduction

Author keywords

[No Author keywords available]

Indexed keywords

DIMERIZATION; ESCHERICHIA COLI; HYDROSTATIC PRESSURE; LIPID BILAYERS; PROTEINS;

EID: 57449116328     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02028-08     Document Type: Article
Times cited : (17)

References (20)
  • 1
    • 0037171122 scopus 로고    scopus 로고
    • High pressure effects on biological macromolecules: From structural changes to alteration of cellular processes
    • Balny, C., P. Masson, and K. Heremans. 2002. High pressure effects on biological macromolecules: from structural changes to alteration of cellular processes. Biochim. Biophys. Acta 1595:3-10.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 3-10
    • Balny, C.1    Masson, P.2    Heremans, K.3
  • 2
    • 0037171156 scopus 로고    scopus 로고
    • Pressure effects on in vivo microbial processes
    • Bartlett, D. H. 2002. Pressure effects on in vivo microbial processes. Biochim. Biophys. Acta 1595:367-381.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 367-381
    • Bartlett, D.H.1
  • 3
    • 0035117042 scopus 로고    scopus 로고
    • RNA arbitrarily primed PCR survey of genes regulated by ToxR in the deep-sea bacterium Photobacterium profundum strain SS9
    • Bidle, K. A., and D. H. Bartlett. 2001. RNA arbitrarily primed PCR survey of genes regulated by ToxR in the deep-sea bacterium Photobacterium profundum strain SS9. J. Bacteriol. 183:1688-1693.
    • (2001) J. Bacteriol , vol.183 , pp. 1688-1693
    • Bidle, K.A.1    Bartlett, D.H.2
  • 4
    • 0037171151 scopus 로고    scopus 로고
    • Pressure effects on intra- and intermolecular interactions within proteins
    • Boonyaratanakornkit, B. B., C. B. Park, and D. S. Clark. 2002. Pressure effects on intra- and intermolecular interactions within proteins. Biochim. Biophys. Acta 1595:235-249.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 235-249
    • Boonyaratanakornkit, B.B.1    Park, C.B.2    Clark, D.S.3
  • 5
    • 0028001591 scopus 로고
    • Analysis of membrane protein interaction: ToxR can dimerize the amino terminus of phage lambda repressor
    • Dziejman, M., and J. J. Mekalanos. 1994. Analysis of membrane protein interaction: ToxR can dimerize the amino terminus of phage lambda repressor. Mol. Microbiol. 13:485-494.
    • (1994) Mol. Microbiol , vol.13 , pp. 485-494
    • Dziejman, M.1    Mekalanos, J.J.2
  • 6
    • 0035824509 scopus 로고    scopus 로고
    • In vitro selection of membrane-spanning leucine zipper protein-protein interaction motifs using POSSYCCAT
    • Gurezka, R., and D. Langosch. 2001. In vitro selection of membrane-spanning leucine zipper protein-protein interaction motifs using POSSYCCAT. J. Biol. Chem. 276:45580-45587.
    • (2001) J. Biol. Chem , vol.276 , pp. 45580-45587
    • Gurezka, R.1    Langosch, D.2
  • 7
    • 0038690115 scopus 로고    scopus 로고
    • Characterization of the pressure-induced intermediate and unfolded state of red-shifted green fluorescent protein: A static and kinetic FTIR, UV/VIS and fluorescence spectroscopy study
    • Herberhold, H., S. Marchal, R. Lange, C. H. Scheyhing, R. F. Vogel, and R. Winter. 2003. Characterization of the pressure-induced intermediate and unfolded state of red-shifted green fluorescent protein: a static and kinetic FTIR, UV/VIS and fluorescence spectroscopy study. J. Mol. Biol. 330:1153-1164.
    • (2003) J. Mol. Biol , vol.330 , pp. 1153-1164
    • Herberhold, H.1    Marchal, S.2    Lange, R.3    Scheyhing, C.H.4    Vogel, R.F.5    Winter, R.6
  • 9
    • 0027952334 scopus 로고
    • Dimerization of Bence Jones proteins: Linking the rate of transcription from an Escherichia coli promoter to the association constant of REIV
    • Kolmar, H., C. Frisch, G. Kleemann, K. Gotze, F. J. Stevens, and H. J. Fritz. 1994. Dimerization of Bence Jones proteins: linking the rate of transcription from an Escherichia coli promoter to the association constant of REIV. Biol. Chem. Hoppe-Seyler 375:61-70.
    • (1994) Biol. Chem. Hoppe-Seyler , vol.375 , pp. 61-70
    • Kolmar, H.1    Frisch, C.2    Kleemann, G.3    Gotze, K.4    Stevens, F.J.5    Fritz, H.J.6
  • 10
    • 0029115282 scopus 로고
    • Membrane insertion of the bacterial signal transduction protein ToxR and requirements of transcription activation studied by modular replacement of different protein substructures
    • Kolmar, H., F. Hennecke, K. Gotze, B. Janzer, B. Vogt, F. Mayer, and H. J. Fritz. 1995. Membrane insertion of the bacterial signal transduction protein ToxR and requirements of transcription activation studied by modular replacement of different protein substructures. EMBO J. 14:3895-3904.
    • (1995) EMBO J , vol.14 , pp. 3895-3904
    • Kolmar, H.1    Hennecke, F.2    Gotze, K.3    Janzer, B.4    Vogt, B.5    Mayer, F.6    Fritz, H.J.7
  • 11
    • 0030575833 scopus 로고    scopus 로고
    • Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator
    • Langosch, D., B. Brosig, H. Kolmar, and H. J. Fritz. 1996. Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator. J. Mol. Biol. 263:525-530.
    • (1996) J. Mol. Biol , vol.263 , pp. 525-530
    • Langosch, D.1    Brosig, B.2    Kolmar, H.3    Fritz, H.J.4
  • 12
    • 0542390231 scopus 로고
    • Synthesis of cholera toxin is positively regulated at the transcriptional level by ToxR
    • Miller, V. L., and J. J. Mekalanos. 1984. Synthesis of cholera toxin is positively regulated at the transcriptional level by ToxR. Proc. Natl. Acad. Sci. USA 81:3471-3475.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3471-3475
    • Miller, V.L.1    Mekalanos, J.J.2
  • 13
    • 0023667819 scopus 로고
    • Cholera toxin transcriptional activator ToxR is a transmembrane DNA binding protein
    • Miller, V. L., R. K. Taylor, and J. J. Mekalanos. 1987. Cholera toxin transcriptional activator ToxR is a transmembrane DNA binding protein. Cell 48:271-279.
    • (1987) Cell , vol.48 , pp. 271-279
    • Miller, V.L.1    Taylor, R.K.2    Mekalanos, J.J.3
  • 14
    • 33745713605 scopus 로고    scopus 로고
    • Nicolini, C., J. Kraineva, M. Khurana, N. Periasamy, S. S. Funari, and R. Winter. 2006. Temperature and pressure effects on structural and conformational properties of POPC/SM/cholesterol model raft mixtures: a FT-IR, SAXS, DSC, PPC and Laurdan fluorescence spectroscopy study. Biochim. Biophys. Acta 1758:248-258.
    • Nicolini, C., J. Kraineva, M. Khurana, N. Periasamy, S. S. Funari, and R. Winter. 2006. Temperature and pressure effects on structural and conformational properties of POPC/SM/cholesterol model raft mixtures: a FT-IR, SAXS, DSC, PPC and Laurdan fluorescence spectroscopy study. Biochim. Biophys. Acta 1758:248-258.
  • 15
    • 0030059639 scopus 로고    scopus 로고
    • The ToxR protein of Vibrio cholerae forms homodimers and heterodimers
    • Ottemann, K. M., and J. J. Mekalanos. 1996. The ToxR protein of Vibrio cholerae forms homodimers and heterodimers. J. Bacteriol. 178:156-162.
    • (1996) J. Bacteriol , vol.178 , pp. 156-162
    • Ottemann, K.M.1    Mekalanos, J.J.2
  • 16
    • 0025742883 scopus 로고
    • Quantitation of lipid phases in phospholipid vesicles by the generalized polarization of Laurdan fluorescence
    • Parasassi, T., G. De Stasio, G. Ravagnan, R. M. Rusch, and E. Gratton. 1991. Quantitation of lipid phases in phospholipid vesicles by the generalized polarization of Laurdan fluorescence. Biophys. J. 60:179-189.
    • (1991) Biophys. J , vol.60 , pp. 179-189
    • Parasassi, T.1    De Stasio, G.2    Ravagnan, G.3    Rusch, R.M.4    Gratton, E.5
  • 17
    • 0017172644 scopus 로고
    • Protoplast formation in Escherichia coli
    • Weiss, R. L. 1976. Protoplast formation in Escherichia coli. J. Bacteriol. 128:668-670.
    • (1976) J. Bacteriol , vol.128 , pp. 668-670
    • Weiss, R.L.1
  • 18
    • 0031779823 scopus 로고    scopus 로고
    • Identification of a regulatory protein required for pressure-responsive gene expression in the deep sea bacterium Photobacterium species strain SS9
    • Welch, T. J., and D. H. Bartlett. 1998. Identification of a regulatory protein required for pressure-responsive gene expression in the deep sea bacterium Photobacterium species strain SS9. Mol. Microbiol. 27:977-985.
    • (1998) Mol. Microbiol , vol.27 , pp. 977-985
    • Welch, T.J.1    Bartlett, D.H.2
  • 19
    • 33847312741 scopus 로고    scopus 로고
    • Towards an understanding of the temperature/pressure configurational and free-energy landscape of biomolecules
    • Winter, R., D. Lopes, S. Grudzielanek, and K. Vogtt. 2007. Towards an understanding of the temperature/pressure configurational and free-energy landscape of biomolecules. J. Non-Equilib. Thermodyn. 32:41-97.
    • (2007) J. Non-Equilib. Thermodyn , vol.32 , pp. 41-97
    • Winter, R.1    Lopes, D.2    Grudzielanek, S.3    Vogtt, K.4
  • 20
    • 0014617497 scopus 로고
    • A study of the effects of hydrostatic pressure on macromolecular synthesis in Escherichia coli
    • Yayanos, A. A., and E. C. Pollard. 1969. A study of the effects of hydrostatic pressure on macromolecular synthesis in Escherichia coli. Biophys. J. 9:1464-1482.
    • (1969) Biophys. J , vol.9 , pp. 1464-1482
    • Yayanos, A.A.1    Pollard, E.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.