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Volumn 45, Issue 6, 2002, Pages 1485-1498

Controlling pore assembly of staphylococcal γ-haemolysin by low temperature and by disulphide bond formation in double-cysteine LukF mutants

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CYSTEINE; DISULFIDE; DODECYL SULFATE SODIUM; HEMOLYSIN;

EID: 0036033671     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2002.03125.x     Document Type: Article
Times cited : (32)

References (42)
  • 1
    • 0033576256 scopus 로고    scopus 로고
    • Streptolysin O: Inhibition of the conformational change during membrane binding of the monomer prevents oligomerization and pore formation
    • AbdelGhani, E.M., Weis, S., Walev, I., Kehoe, M., Bhakdi, S., and Palmer, M. (1999) Streptolysin O: inhibition of the conformational change during membrane binding of the monomer prevents oligomerization and pore formation. Biochemistry 38: 15204-15211.
    • (1999) Biochemistry , vol.38 , pp. 15204-15211
    • AbdelGhani, E.M.1    Weis, S.2    Walev, I.3    Kehoe, M.4    Bhakdi, S.5    Palmer, M.6
  • 2
    • 0000329969 scopus 로고
    • Cytolytic toxins of bacterial
    • Ajl, S., Kadis, S., and Montie, T.C., (eds) New York: Academic Press
    • Bernheimer, A.W. (1970) Cytolytic Toxins of Bacterial. Vol 1. In Microbial toxins. Ajl, S., Kadis, S., and Montie, T.C., (eds) New York: Academic Press, pp. 183-212.
    • (1970) Microbial Toxins , vol.1 , pp. 183-212
    • Bernheimer, A.W.1
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method of the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method of the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0030660558 scopus 로고    scopus 로고
    • Conformational changes in aerolysin during the transition from the water-soluble protoxin to the membrane channel
    • Cabiaux, V., Buckley, T., Wattiez, R., Ruysschaert, J.M., Parker, M. and Gisou van der Goot, F. (1997) Conformational changes in aerolysin during the transition from the water-soluble protoxin to the membrane channel. Biochemistry 36: 15224-15232.
    • (1997) Biochemistry , vol.36 , pp. 15224-15232
    • Cabiaux, V.1    Buckley, T.2    Wattiez, R.3    Ruysschaert, J.M.4    Parker, M.5    Gisou van der Goot, F.6
  • 5
    • 0031404458 scopus 로고    scopus 로고
    • Spontaneous oligomerization of a staphylococcal alpha-hemolysin conformationally constrained by removal of residues that form the transmembrane beta-barrel
    • Cheley, S., Malghani, M.S., Song, L., Hobaugh, M., Gouaux, J.E., Yang, J., and Bayley, H. (1997) Spontaneous oligomerization of a staphylococcal alpha-hemolysin conformationally constrained by removal of residues that form the transmembrane beta-barrel. Protein Eng 10: 1433-1443.
    • (1997) Protein Eng , vol.10 , pp. 1433-1443
    • Cheley, S.1    Malghani, M.S.2    Song, L.3    Hobaugh, M.4    Gouaux, J.E.5    Yang, J.6    Bayley, H.7
  • 6
    • 0032508971 scopus 로고    scopus 로고
    • The interaction of Staphylococcus aureus bi-component γ-hemolysins and leucocidins with cells and lipid membranes
    • Ferreras, M., Frank, H., Serra, M.D., Coli, D.A., Prevost, G., and Menestrina, G. (1998) The interaction of Staphylococcus aureus bi-component γ-hemolysins and leucocidins with cells and lipid membranes. Biochim Biophys Acta 1414: 108-126.
    • (1998) Biochim Biophys Acta , vol.1414 , pp. 108-126
    • Ferreras, M.1    Frank, H.2    Serra, M.D.3    Coli, D.A.4    Prevost, G.5    Menestrina, G.6
  • 7
    • 0028945654 scopus 로고
    • Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution
    • Funatsu, T., Harada, Y., Tokunaga, M., Saito, K., and Yanagida, T. (1995) Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature 374: 555-559.
    • (1995) Nature , vol.374 , pp. 555-559
    • Funatsu, T.1    Harada, Y.2    Tokunaga, M.3    Saito, K.4    Yanagida, T.5
  • 9
    • 0031877366 scopus 로고    scopus 로고
    • α-hemolysin from Staphylococcus aureus: An archetype of beta-barrel, channel-forming toxins
    • Gouaux, J.E. (1998) α-Hemolysin from Staphylococcus aureus: an archetype of beta-barrel, channel-forming toxins. J Struct Biol 121: 110-122.
    • (1998) J Struct Biol , vol.121 , pp. 110-122
    • Gouaux, J.E.1
  • 10
    • 0031454754 scopus 로고    scopus 로고
    • α-hemolysin, γ-hemolysin, and leukocidin from Staphylococcus aureus: Distant in sequence but similar in structure
    • Gouaux, J.E., Hobaugh, M.R., and Song, L. (1997) α-Hemolysin, γ-hemolysin, and leukocidin from Staphylococcus aureus: distant in sequence but similar in structure. Protein Sci 6: 2631-2635.
    • (1997) Protein Sci , vol.6 , pp. 2631-2635
    • Gouaux, J.E.1    Hobaugh, M.R.2    Song, L.3
  • 11
    • 0035896507 scopus 로고    scopus 로고
    • Arresting pore formation of a cholesterol-dependent cytolysin by disulphide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate
    • Hotze, E.M., Wilson-Kubalek, E.M., Rossjohn, J., Parker, M.W., Johnson, A.E., and Tweten, R.K. (2001) Arresting pore formation of a cholesterol-dependent cytolysin by disulphide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate. J Biol Chem 276: 8261-82688.
    • (2001) J Biol Chem , vol.276 , pp. 8261-82688
    • Hotze, E.M.1    Wilson-Kubalek, E.M.2    Rossjohn, J.3    Parker, M.W.4    Johnson, A.E.5    Tweten, R.K.6
  • 12
    • 0032559298 scopus 로고    scopus 로고
    • Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin
    • Ishijima, A., Kojima, H., Funatsu, T., Tokunaga, M., Higuchi, H., Tanaka, H., and Yanagida, Y. (1998) Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin. Cell 23: 161-171.
    • (1998) Cell , vol.23 , pp. 161-171
    • Ishijima, A.1    Kojima, H.2    Funatsu, T.3    Tokunaga, M.4    Higuchi, H.5    Tanaka, H.6    Yanagida, Y.7
  • 13
    • 0027418490 scopus 로고
    • The two staphylococcal bi-component toxins, leukocidin and γ-hemolysin, share one component in common
    • Kamio, Y., Rahman, A., Nariya, H., Ozawa, T., and Izaki, K. (1993) The two staphylococcal bi-component toxins, leukocidin and γ-hemolysin, share one component in common. FEBS 321: 15-18.
    • (1993) FEBS , vol.321 , pp. 15-18
    • Kamio, Y.1    Rahman, A.2    Nariya, H.3    Ozawa, T.4    Izaki, K.5
  • 14
    • 0031148369 scopus 로고    scopus 로고
    • Sequential binding of Staphylococcal γ-hemolysin to human erythrocytes and complex formation of the hemolysin on the cell surface
    • Kaneko, J., Ozawa, T., Tomita, T., and Kamio, Y. (1997) Sequential binding of Staphylococcal γ-hemolysin to human erythrocytes and complex formation of the hemolysin on the cell surface. Biosci Biotech Biochem 61: 846-851.
    • (1997) Biosci Biotech Biochem , vol.61 , pp. 846-851
    • Kaneko, J.1    Ozawa, T.2    Tomita, T.3    Kamio, Y.4
  • 15
    • 0032109375 scopus 로고    scopus 로고
    • An N-terminal region of LukF of staphylococcal leukocidin/gamma-hemolysin crucial for the biological activity of the toxin
    • Kaneko, J., Mascarenas, A.L., Huda, M.N., Tomita, T., and Kamio, Y. (1998) An N-terminal region of LukF of staphylococcal leukocidin/gamma-hemolysin crucial for the biological activity of the toxin. Biosci Biotechnol Biochem 62: 1465-1467.
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 1465-1467
    • Kaneko, J.1    Mascarenas, A.L.2    Huda, M.N.3    Tomita, T.4    Kamio, Y.5
  • 16
    • 0033586795 scopus 로고    scopus 로고
    • Outer membrane protein A of Escherichia coli inserts and folds into lipid bilayers by a concerted mechanism
    • Kleinschmidt, J.H., den Blaauwen, T., Driessen, A.J., and Tamm, L.K. (1999) Outer membrane protein A of Escherichia coli inserts and folds into lipid bilayers by a concerted mechanism. Biochemistry 38: 5006-5016.
    • (1999) Biochemistry , vol.38 , pp. 5006-5016
    • Kleinschmidt, J.H.1    Den Blaauwen, T.2    Driessen, A.J.3    Tamm, L.K.4
  • 18
    • 0034869444 scopus 로고    scopus 로고
    • Mode of action of beta-barrel pore-forming toxins of the staphylococcal alpha-hemolysin family
    • Menestrina, G., Serra, M.D., and Prevost, G. (2001) Mode of action of beta-barrel pore-forming toxins of the staphylococcal alpha-hemolysin family. Toxicon 39: 1661-1672.
    • (2001) Toxicon , vol.39 , pp. 1661-1672
    • Menestrina, G.1    Serra, M.D.2    Prevost, G.3
  • 19
    • 0035942992 scopus 로고    scopus 로고
    • The Staphylococcal leukocidin bicomponent toxin forms large ionic channels
    • Miles, G., Cheley, S., Braha, O., and Bayley, H. (2001) The Staphylococcal leukocidin bicomponent toxin forms large ionic channels. Biochemistry 40: 8514-8522.
    • (2001) Biochemistry , vol.40 , pp. 8514-8522
    • Miles, G.1    Cheley, S.2    Braha, O.3    Bayley, H.4
  • 20
    • 0033543208 scopus 로고    scopus 로고
    • Anthrax protective antigen: Prepore-to-pore conversion
    • Miller, C.J., Elliott, J.L., and Collier, R.J. (1999) Anthrax protective antigen: prepore-to-pore conversion. Biochemistry 38: 10432-10441.
    • (1999) Biochemistry , vol.38 , pp. 10432-10441
    • Miller, C.J.1    Elliott, J.L.2    Collier, R.J.3
  • 21
    • 85007863356 scopus 로고
    • Improved method for purification of leukocidin and γ-hemolysin components from Staphylococcus aureus
    • Nariya, H., Asami, I., Ozawa, T., Beppu, Y., Izaki, K., and Kamio, Y. (1993) Improved method for purification of leukocidin and γ-hemolysin components from Staphylococcus aureus. Biosci Biotech Biochem 57: 2198-2199.
    • (1993) Biosci Biotech Biochem , vol.57 , pp. 2198-2199
    • Nariya, H.1    Asami, I.2    Ozawa, T.3    Beppu, Y.4    Izaki, K.5    Kamio, Y.6
  • 22
    • 0032932083 scopus 로고    scopus 로고
    • Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel
    • Olson, R., Nariya, H., Yokota, K., Kamio, Y., and Gouaux, E. (1999) Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel. Nature Struct Biol 6: 134-140.
    • (1999) Nature Struct Biol , vol.6 , pp. 134-140
    • Olson, R.1    Nariya, H.2    Yokota, K.3    Kamio, Y.4    Gouaux, E.5
  • 23
    • 0030043134 scopus 로고    scopus 로고
    • Aerolysin: The ins and outs of a model channel-forming toxin
    • Parker, M., Gisou van der Goot, F., and Buckley, J.T. (1998) Aerolysin: the ins and outs of a model channel-forming toxin. Mol Microbiol 19: 205-212.
    • (1998) Mol Microbiol , vol.19 , pp. 205-212
    • Parker, M.1    Gisou van der Goot, F.2    Buckley, J.T.3
  • 24
    • 0033103175 scopus 로고    scopus 로고
    • The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins
    • Pedelacq, J.D., Maveyraud, L., Prevost, G., Baba-Moussa, L., Gonzalez, A., Courcelle, E., et al. (1999) The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins. Structure Fold Des 7: 277-287.
    • (1999) Structure Fold Des , vol.7 , pp. 277-287
    • Pedelacq, J.D.1    Maveyraud, L.2    Prevost, G.3    Baba-Moussa, L.4    Gonzalez, A.5    Courcelle, E.6
  • 25
    • 23544437172 scopus 로고    scopus 로고
    • The bi-component staphylococcal leucotoxins and γ-hemolysins (toxins)
    • Alouf, J.E., and Freer, J.H., (eds). London: Academic Press
    • Prevost, G. (1999) The bi-component staphylococcal leucotoxins and γ-hemolysins (toxins). In Bacterial Protein Toxins: a Comprehensive Sourcebook. Alouf, J.E., and Freer, J.H., (eds). London: Academic Press.
    • (1999) Bacterial Protein Toxins: A Comprehensive Sourcebook
    • Prevost, G.1
  • 28
    • 0030881601 scopus 로고    scopus 로고
    • The propeptide of Clostridium septicum alpha toxin functions as an intramolecular chaperone and is a potent inhibitor of alpha toxin-dependent cytolysis
    • Sellman, B.R., and Tweten, R.K. (1997) The propeptide of Clostridium septicum alpha toxin functions as an intramolecular chaperone and is a potent inhibitor of alpha toxin-dependent cytolysis. Mol Microbiol 25: 429-440.
    • (1997) Mol Microbiol , vol.25 , pp. 429-440
    • Sellman, B.R.1    Tweten, R.K.2
  • 29
    • 0034702810 scopus 로고    scopus 로고
    • The mechanism of pore assembly for a cholesterol-dependent cytolysin: Formation of a large prepore complex precedes the insertion of the transmembrane beta-hairpins
    • Shepard, L.A., Shatursky, O., Johnson, A.E., and Tweten, R.K. (2000) The mechanism of pore assembly for a cholesterol-dependent cytolysin: formation of a large prepore complex precedes the insertion of the transmembrane beta-hairpins. Biochemistry 39: 10284-10293.
    • (2000) Biochemistry , vol.39 , pp. 10284-10293
    • Shepard, L.A.1    Shatursky, O.2    Johnson, A.E.3    Tweten, R.K.4
  • 30
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • Song, L., Hobaugh, M.R., Shustak, C., Cheyley, A., Bayley, H., and Gaoux, E. (1996) Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore. Science 274: 1859-1866.
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheyley, A.4    Bayley, H.5    Gaoux, E.6
  • 31
    • 0030740555 scopus 로고    scopus 로고
    • Assembly of Staphylococcus aureus γ-hemolysin into a pore-forming ring-shaped complex on the surface of human erythrocytes
    • Sugawara, N., Tomita, T., and Kamio, Y. (1997) Assembly of Staphylococcus aureus γ-hemolysin into a pore-forming ring-shaped complex on the surface of human erythrocytes. FEBS 410: 333-337.
    • (1997) FEBS , vol.410 , pp. 333-337
    • Sugawara, N.1    Tomita, T.2    Kamio, Y.3
  • 32
    • 0027510074 scopus 로고
    • Sequencing of leukocidin R from Staphylococcus aureus P83 suggests that staphylococcal leucocidins and γ-hemolysin are members of a single two-component family of toxins
    • Supersac, G., Prevost, G., and Piemont, Y. (1993) Sequencing of leukocidin R from Staphylococcus aureus P83 suggests that staphylococcal leucocidins and γ-hemolysin are members of a single two-component family of toxins. Infection Immunity 61: 580-587.
    • (1993) Infection Immunity , vol.61 , pp. 580-587
    • Supersac, G.1    Prevost, G.2    Piemont, Y.3
  • 33
    • 0035980137 scopus 로고    scopus 로고
    • Structure and assembly of β-barrel membrane proteins
    • Tamm, L.K., Arora, A., and Kleinschmidt, J.H. (2001) Structure and assembly of β-barrel membrane proteins. J Biol Chem 276: 32399-32402.
    • (2001) J Biol Chem , vol.276 , pp. 32399-32402
    • Tamm, L.K.1    Arora, A.2    Kleinschmidt, J.H.3
  • 34
    • 0031126533 scopus 로고    scopus 로고
    • Molecular biology of the pore-forming cytolysins from Staphylococcus aureus α-hemolysins and γ-hemolysins and leukocidin
    • Tomita, T., and Kamio, Y. (1997) Molecular biology of the pore-forming cytolysins from Staphylococcus aureus α-hemolysins and γ-hemolysins and leukocidin. Biosci Biotechnol Biochem 61: 565-572.
    • (1997) Biosci Biotechnol Biochem , vol.61 , pp. 565-572
    • Tomita, T.1    Kamio, Y.2
  • 35
    • 0029000140 scopus 로고
    • Correct oligomerization is a prerequisite for insertion of the central molecular domain of staphylococcal alpha-toxin into the lipid bilayer
    • Valeva, A., Palmer, M., Hilgert, K., Kehoe, M., and Bhakdi, S. (1995) Correct oligomerization is a prerequisite for insertion of the central molecular domain of staphylococcal alpha-toxin into the lipid bilayer. Biochim Biophys Acta 1236: 213-218.
    • (1995) Biochim Biophys Acta , vol.1236 , pp. 213-218
    • Valeva, A.1    Palmer, M.2    Hilgert, K.3    Kehoe, M.4    Bhakdi, S.5
  • 36
    • 0029924449 scopus 로고    scopus 로고
    • Molecular architecture of a toxin pore: A 15 residue sequence lines the transmembrane channel of Staphylococcal alpha-toxin
    • Valeva, A., Weisser, A., Walker, B., Kehoe, M., Bayley, H., Bhakdi, S., et al. (1996) Molecular architecture of a toxin pore: a 15 residue sequence lines the transmembrane channel of Staphylococcal alpha-toxin. EMBO J 15: 1857-1864.
    • (1996) EMBO J , vol.15 , pp. 1857-1864
    • Valeva, A.1    Weisser, A.2    Walker, B.3    Kehoe, M.4    Bayley, H.5    Bhakdi, S.6
  • 37
    • 0030735356 scopus 로고    scopus 로고
    • Staphylococcal alpha-toxin: Formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages
    • Valeva, A., Palmer, M., and Bhakdi, S. (1997a) Staphylococcal alpha-toxin: formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages. Biochemistry 36: 13298-13304.
    • (1997) Biochemistry , vol.36 , pp. 13298-13304
    • Valeva, A.1    Palmer, M.2    Bhakdi, S.3
  • 38
    • 0030779852 scopus 로고    scopus 로고
    • Transmembrane β-barrel of staphylococcal α-toxin forms in sensitive but not in resistant cells
    • Valeva, A., Walev, I., Pinkernell, M., Walker, B., Bayley, H., Palmer, M., et al. (1997b) Transmembrane β-barrel of staphylococcal α-toxin forms in sensitive but not in resistant cells. Proc Nati Acad Sci USA 94: 11607-11611.
    • (1997) Proc Nati Acad Sci USA , vol.94 , pp. 11607-11611
    • Valeva, A.1    Walev, I.2    Pinkernell, M.3    Walker, B.4    Bayley, H.5    Palmer, M.6
  • 39
    • 0035805604 scopus 로고    scopus 로고
    • Membrane insertion of the heptameric Staphylococcal alpha-toxin pore. A domino-like structural transition that is allosterically modulated by the target cell membrane
    • Valeva, A., Schnabel, R., Walev, I., Boukhallouk, F., Bhakdi, S., and Palmer, M. (2001) Membrane insertion of the heptameric Staphylococcal alpha-toxin pore. A domino-like structural transition that is allosterically modulated by the target cell membrane. J Biol Chem 276: 14835-14341.
    • (2001) J Biol Chem , vol.276 , pp. 14835-14341
    • Valeva, A.1    Schnabel, R.2    Walev, I.3    Boukhallouk, F.4    Bhakdi, S.5    Palmer, M.6
  • 40
    • 0026785678 scopus 로고
    • Assembly of the oligomeric membrane pore formed by staphylococcal alpha-hemolysin examined by truncation mutagenesis
    • Walker, B., Krishnasastry, M., Zorn, L., and Bayley, H. (1992) Assembly of the oligomeric membrane pore formed by staphylococcal alpha-hemolysin examined by truncation mutagenesis. J Biol Chem 267: 21782-21786.
    • (1992) J Biol Chem , vol.267 , pp. 21782-21786
    • Walker, B.1    Krishnasastry, M.2    Zorn, L.3    Bayley, H.4
  • 41
    • 0029240394 scopus 로고
    • An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch
    • Walker, B., Braha, O., Cheley, S., and Bayley, H. (1995) An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch. Chem Biol 2: 99-105.
    • (1995) Chem Biol , vol.2 , pp. 99-105
    • Walker, B.1    Braha, O.2    Cheley, S.3    Bayley, H.4
  • 42
    • 0034576095 scopus 로고    scopus 로고
    • Tyrosine72 residue at the bottom of rim domain in LukF is crucial for the sequential binding of the staphylococcal γ-hemolysin to human erythrocyte
    • Yokota, K., and Kamio, Y. (2000) Tyrosine72 residue at the bottom of rim domain in LukF is crucial for the sequential binding of the staphylococcal γ-hemolysin to human erythrocyte. Biosci Biotech Biochem 64: 2744-2747.
    • (2000) Biosci Biotech Biochem , vol.64 , pp. 2744-2747
    • Yokota, K.1    Kamio, Y.2


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