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Volumn 243, Issue 1-2, 1997, Pages 400-407

Spectroscopic studies of the C-terminal secretion signal of the Serratia marcescens haem acquisition protein (HasA) in various membrane-mimetic environments

Author keywords

Liposome; Micelle; Peptide structure; Secretion; Trifluoroethanol

Indexed keywords

ABC TRANSPORTER; BINDING PROTEIN; METALLOPROTEINASE; SIGNAL PEPTIDE;

EID: 0031020832     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.0400a.x     Document Type: Article
Times cited : (18)

References (42)
  • 1
    • 0026669327 scopus 로고
    • Secretion across the bacterial outer membrane
    • Wandersman, C. (1992) Secretion across the bacterial outer membrane, Trends Genet. 8, 317-321.
    • (1992) Trends Genet. , vol.8 , pp. 317-321
    • Wandersman, C.1
  • 2
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley, A. P. (1993) The complete general secretory pathway in gram-negative bacteria, Microbiol. Rev. 57, 50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 3
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C. F. (1992) ABC transporters: from microorganisms to man, Annu. Rev. Cell. Biol. 8, 67-113.
    • (1992) Annu. Rev. Cell. Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 4
    • 0027458116 scopus 로고
    • ATP-dependent transport systems in bacteria and humans: Relevance to cystic fibrosis and multidrug resistance
    • Doige, C. A. & Ames, F. L. G. (1993) ATP-dependent transport systems in bacteria and humans: relevance to cystic fibrosis and multidrug resistance, Annu. Rev. Microbiol. 47, 291-319.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 291-319
    • Doige, C.A.1    Ames, F.L.G.2
  • 5
    • 0028318241 scopus 로고
    • A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria
    • Dinh, T., Paulsen, I. T. & Saier, M. H. J. (1994) A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria, J. Bacteriol. 176, 3825-3831.
    • (1994) J. Bacteriol. , vol.176 , pp. 3825-3831
    • Dinh, T.1    Paulsen, I.T.2    Saier, M.H.J.3
  • 6
    • 0345384691 scopus 로고
    • A carboxyl-terminal four-amino acid motif is required for secretion of the metalloprotease PrtG through the Erwinia chrysanthemi protease secretion pathway
    • Ghigo, J.-M. & Wandersman, C. (1994) A carboxyl-terminal four-amino acid motif is required for secretion of the metalloprotease PrtG through the Erwinia chrysanthemi protease secretion pathway, J. Biol. Chem. 269, 1-7.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1-7
    • Ghigo, J.-M.1    Wandersman, C.2
  • 7
    • 0028285221 scopus 로고
    • C-terminal secretion signal of an Erwinia chrysanthemi protease secreted by a signal peptide-independent pathway: Proton NMR and CD conformational studies in membrane-mimetic environments
    • Wolff, N., Ghigo, J.-M., Delepelaire, P., Wandersman, C. & Delepierre, M. (1994) C-terminal secretion signal of an Erwinia chrysanthemi protease secreted by a signal peptide-independent pathway: proton NMR and CD conformational studies in membrane-mimetic environments, Biochemistry 33, 6792-6801.
    • (1994) Biochemistry , vol.33 , pp. 6792-6801
    • Wolff, N.1    Ghigo, J.-M.2    Delepelaire, P.3    Wandersman, C.4    Delepierre, M.5
  • 8
    • 0028170732 scopus 로고
    • Iron acquisition from heme and hemoglobin by a Serratia marcescens extracellular protein
    • Létoffé, S., Ghigo, J.-M. & Wandersman, C. (1994) Iron acquisition from heme and hemoglobin by a Serratia marcescens extracellular protein, Proc. Natl Acad. Sci. USA 91, 9876-9880.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9876-9880
    • Létoffé, S.1    Ghigo, J.-M.2    Wandersman, C.3
  • 9
    • 0025372570 scopus 로고
    • TolC, an Escherichia coli outer membrane protein required for hemolysin secretion
    • Wandersman, C. & Delepelaire, P. (1990) TolC, an Escherichia coli outer membrane protein required for hemolysin secretion, Proc. Natl Acad. Sci. USA 87, 4776-4780.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4776-4780
    • Wandersman, C.1    Delepelaire, P.2
  • 10
    • 0018476871 scopus 로고
    • Prediction of β-turns
    • Chou, P. Y. & Fasman, G. D. (1979) Prediction of β-turns, Biophys. J. 26, 367-384.
    • (1979) Biophys. J. , vol.26 , pp. 367-384
    • Chou, P.Y.1    Fasman, G.D.2
  • 11
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier, J., Osguthorpe, D. J. & Robson, B. (1978) Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins, J. Mol. Biol. 120, 97-120.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 12
    • 0000929505 scopus 로고
    • The hydrophobic moment detects periodicity in protein hydrophobicity
    • Eisenberg, D., Weiss, R. M. & Terwilliger, T. C. (1984) The hydrophobic moment detects periodicity in protein hydrophobicity, Proc. Natl Acad. Sci. USA 81, 140-144.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 140-144
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 13
    • 0028447768 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters
    • Munoz, V. & Serrano, L. (1994) Elucidating the folding problem of helical peptides using empirical parameters, Nat. Struct. Biol. 1, 399-409.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 399-409
    • Munoz, V.1    Serrano, L.2
  • 14
    • 0028873081 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides
    • Munoz, V. & Serrano, L. (1995) Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides, J. Mol. Biol. 245, 275-296.
    • (1995) J. Mol. Biol. , vol.245 , pp. 275-296
    • Munoz, V.1    Serrano, L.2
  • 15
    • 0028834210 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence
    • Munoz, V. & Serrano, L. (1995) Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence, J. Mol. Biol. 245, 297-308.
    • (1995) J. Mol. Biol. , vol.245 , pp. 297-308
    • Munoz, V.1    Serrano, L.2
  • 16
    • 0015550508 scopus 로고
    • Experimental differential light-scattering correction to the circular dichroism of bacteriophage T2
    • Dorman, B. P. & Maestre, M. F. (1973) Experimental differential light-scattering correction to the circular dichroism of bacteriophage T2, Proc. Nat Acad. Sci. USA 70, 255-259.
    • (1973) Proc. Nat Acad. Sci. USA , vol.70 , pp. 255-259
    • Dorman, B.P.1    Maestre, M.F.2
  • 17
    • 0000367088 scopus 로고
    • Two points calibration of circular dichrometer with D-10-camphorsulfoic acid
    • Chen, G. C. & Yang, J. T. (1977) Two points calibration of circular dichrometer with D-10-camphorsulfoic acid, Anal Lett. 10, 1195-1207.
    • (1977) Anal Lett. , vol.10 , pp. 1195-1207
    • Chen, G.C.1    Yang, J.T.2
  • 18
    • 0016169865 scopus 로고
    • Determination of the helix and beta form of proteins in aqueous solution by circular dichroism
    • Chen, Y.-H., Yang, J. T. & Chau, K. H. (1974) Determination of the helix and beta form of proteins in aqueous solution by circular dichroism, Biochemistry 13, 3350-3359.
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.-H.1    Yang, J.T.2    Chau, K.H.3
  • 19
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang, J. T., Wu, C.-S. C. & Martinez, H. M. (1986) Calculation of protein conformation from circular dichroism, Methods Enzymol. 130, 209-269.
    • (1986) Methods Enzymol. , vol.130 , pp. 209-269
    • Yang, J.T.1    Wu, C.-S.C.2    Martinez, H.M.3
  • 20
    • 0026254055 scopus 로고
    • Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water
    • Scholtz, J. M., Qian, H., York, E. J., Steward, J. M. & Baldwin, R. L. (1991) Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water, Biopolymers 31, 1463-1470.
    • (1991) Biopolymers , vol.31 , pp. 1463-1470
    • Scholtz, J.M.1    Qian, H.2    York, E.J.3    Steward, J.M.4    Baldwin, R.L.5
  • 21
    • 0019604334 scopus 로고
    • A fluorimetric method for the estimation of the critical micelle concentration of surfactants
    • De Vendittis, E., Palumbo, G., Parlato, G. & Bocchini, V. (1981) A fluorimetric method for the estimation of the critical micelle concentration of surfactants, Anal. Biochem. 115, 278-286.
    • (1981) Anal. Biochem. , vol.115 , pp. 278-286
    • De Vendittis, E.1    Palumbo, G.2    Parlato, G.3    Bocchini, V.4
  • 24
    • 2642628181 scopus 로고
    • A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants
    • States, D. J., Haberkorn, R. A. & Ruben, D. J. (1982) A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants, J. Magn. Reson. 48, 286-292.
    • (1982) J. Magn. Reson. , vol.48 , pp. 286-292
    • States, D.J.1    Haberkorn, R.A.2    Ruben, D.J.3
  • 25
    • 0000244937 scopus 로고
    • P. COSY, a sensitive alternative for double-quantum-filtered COSY
    • Marion, D. & Bax, A. (1988) P. COSY, a sensitive alternative for double-quantum-filtered COSY, J. Magn. Reson. 80, 528-533.
    • (1988) J. Magn. Reson. , vol.80 , pp. 528-533
    • Marion, D.1    Bax, A.2
  • 26
    • 0005963761 scopus 로고
    • Multiple quantum filters for elucidating NMR coupling networks
    • Piantini, U., Sorensen, O. W. & Ernst, R. R. (1982) multiple quantum filters for elucidating NMR coupling networks, J. Am. Chem. Soc. 104, 6800-6801.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 6800-6801
    • Piantini, U.1    Sorensen, O.W.2    Ernst, R.R.3
  • 28
    • 0024282849 scopus 로고
    • Clean TOCSY for 1H spin system identification in macromolecules
    • Griesinger, C., Otting, G., Wüthrich, K. & Ernst, R. R. (1988) clean TOCSY for 1H spin system identification in macromolecules, J. Am. Chem. Soc. 110, 7870-7872.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 7870-7872
    • Griesinger, C.1    Otting, G.2    Wüthrich, K.3    Ernst, R.R.4
  • 29
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar, A., Ernst, R. R. & Wüthrich, K. (1980) A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules, Biochem. Biophys. Res. Commun. 95, 1-6.
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 31
    • 0029207339 scopus 로고
    • 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG
    • 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG, J. Biomol. NMR 5, 14-24.
    • (1995) J. Biomol. NMR , vol.5 , pp. 14-24
    • Merutka, G.1    Dyson, H.J.2    Wright, P.E.3
  • 32
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart, D. S., Sykes, B. D. & Richards, F. M. (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy, Biochemistry 31, 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 33
    • 0022424027 scopus 로고
    • Specificity of lipid-protein interactions as determined by spectroscopic techniques
    • Devaux, P. F. & Seigneuret, M. (1985) Specificity of lipid-protein interactions as determined by spectroscopic techniques, Biochim. Biophys. Acta. 822, 63-125.
    • (1985) Biochim. Biophys. Acta , vol.822 , pp. 63-125
    • Devaux, P.F.1    Seigneuret, M.2
  • 34
    • 0025917093 scopus 로고
    • Stereochemical analysis of interaction of signal peptide with phospholipids at the initiation of protein translocation across the membrane
    • Kajava, A. V., Bogdanov, M. V. & Nesmeyanova, M. A. (1991) Stereochemical analysis of interaction of signal peptide with phospholipids at the initiation of protein translocation across the membrane, J. Biomol. Struct. & Dyn., 143-157.
    • (1991) J. Biomol. Struct. & Dyn. , pp. 143-157
    • Kajava, A.V.1    Bogdanov, M.V.2    Nesmeyanova, M.A.3
  • 35
    • 0026585803 scopus 로고
    • Effects of temperature variation and phenethyl alcohol addition on acyl chain order and lipid organization in Escherichia coli derived membrane systems. A 2H- and 31P-NMR study
    • Killian, J. A., Fabrie, C. H. J. P., Baart, W. & De Kruijff, B. (1992) Effects of temperature variation and phenethyl alcohol addition on acyl chain order and lipid organization in Escherichia coli derived membrane systems. A 2H- and 31P-NMR study, Biochem. Biophys. Acta 1105, 253-262.
    • (1992) Biochem. Biophys. Acta , vol.1105 , pp. 253-262
    • Killian, J.A.1    Fabrie, C.H.J.P.2    Baart, W.3    De Kruijff, B.4
  • 36
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. & Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein, J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 37
    • 0029023510 scopus 로고
    • Structural analysis and comparison of the C-terminal transport signal domains of hemolysin A and leukotoxin A
    • Yin, Y., Zhang, F., Ling, V. & Arrowsmith, C. H. (1995) Structural analysis and comparison of the C-terminal transport signal domains of hemolysin A and leukotoxin A, FEBS Lett. 366, 1-5.
    • (1995) FEBS Lett. , vol.366 , pp. 1-5
    • Yin, Y.1    Zhang, F.2    Ling, V.3    Arrowsmith, C.H.4
  • 38
    • 0028936779 scopus 로고
    • Secretion and circular dichroism analysis of the C-terminal signal peptides of HlyA and LktA
    • Zhang, F., Yin, Y., Arrowsmith, C. H. & Ling, V. (1995) Secretion and circular dichroism analysis of the C-terminal signal peptides of HlyA and LktA, Biochemistry 34, 4193-4201.
    • (1995) Biochemistry , vol.34 , pp. 4193-4201
    • Zhang, F.1    Yin, Y.2    Arrowsmith, C.H.3    Ling, V.4
  • 39
    • 0025297583 scopus 로고
    • The signal peptide
    • Von Heijne, G. (1990) The signal peptide, J. Membrane Biol. 115, 195-201.
    • (1990) J. Membrane Biol. , vol.115 , pp. 195-201
    • Von Heijne, G.1
  • 40
    • 0029056415 scopus 로고
    • Protein secretion by hybrid bacterial ABC-transporters: Specific functions of the membrane ATPase and the membrane fusion protein
    • Binet, R. & Wandersman, C. (1995) Protein secretion by hybrid bacterial ABC-transporters: specific functions of the membrane ATPase and the membrane fusion protein, EMBO J. 14, 2298-2306.
    • (1995) EMBO J. , vol.14 , pp. 2298-2306
    • Binet, R.1    Wandersman, C.2
  • 41
    • 0028051797 scopus 로고
    • PrtD, the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system, exhibits a secretion signal-regulated ATPase activity
    • Delepelaire, P. (1994) PrtD, the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system, exhibits a secretion signal-regulated ATPase activity, J. Biol. Chem. 45, 27952-27957.
    • (1994) J. Biol. Chem. , vol.45 , pp. 27952-27957
    • Delepelaire, P.1
  • 42
    • 0028023120 scopus 로고
    • Secretion of the Serratia marcescens HasA protein by an ABC transporter
    • Létoffé, S., Ghigo, J.-M. & Wandersman, C. (1994) Secretion of the Serratia marcescens HasA protein by an ABC transporter, J. Bacteriol. 176, 5372-5377.
    • (1994) J. Bacteriol. , vol.176 , pp. 5372-5377
    • Létoffé, S.1    Ghigo, J.-M.2    Wandersman, C.3


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