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Volumn 287, Issue 29, 2012, Pages 24534-24543

Monomer-monomer interactions propagate structural transitions necessary for pore formation by the cholesterol-dependent cytolysins

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE-BOUND; MONOMER STRUCTURES; MONOMER-MONOMER INTERACTIONS; POINT MUTATIONS; PORE FORMATION; SELF-ASSEMBLING; STRUCTURAL CHANGE; STRUCTURAL INFORMATION; STRUCTURAL TRANSITIONS;

EID: 84863799473     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.380139     Document Type: Article
Times cited : (48)

References (30)
  • 1
    • 84857650341 scopus 로고    scopus 로고
    • Membrane assembly of the cholesterol-dependent cytolysin pore complex V
    • Hotze, E. M., and Tweten, R. K. (2012) Membrane assembly of the cholesterol-dependent cytolysin pore complex V. Biochim. Biophys. Acta 1818, 1028-1038
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 1028-1038
    • Hotze, E.M.1    Tweten, R.K.2
  • 3
    • 4444291857 scopus 로고    scopus 로고
    • Vertical collapse of a cytolysin prepore moves its transmembrane β-hairpins to the membrane
    • DOI 10.1038/sj.emboj.7600350
    • Czajkowsky, D. M., Hotze, E. M., Shao, Z., and Tweten, R. K. (2004) Vertical collapse of a cytolysin prepore moves its transmembrane β-hairpins to the membrane. EMBO J. 23, 3206-3215 (Pubitemid 39209145)
    • (2004) EMBO Journal , vol.23 , Issue.16 , pp. 3206-3215
    • Czajkowsky, D.M.1    Hotze, E.M.2    Shao, Z.3    Tweten, R.K.4
  • 4
    • 0033636662 scopus 로고    scopus 로고
    • Mechanism of membrane insertion of a multimeric β-barrel protein: Perfringolysin O creates a pore using ordered and coupled conformational changes
    • Heuck, A. P., Hotze, E. M., Tweten, R. K., and Johnson, A. E. (2000) Mechanism of membrane insertion of a multimeric β-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes. Mol. Cell 6, 1233-1242
    • (2000) Mol. Cell , vol.6 , pp. 1233-1242
    • Heuck, A.P.1    Hotze, E.M.2    Tweten, R.K.3    Johnson, A.E.4
  • 5
    • 0036830653 scopus 로고    scopus 로고
    • Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin
    • Ramachandran, R., Heuck, A. P., Tweten, R. K., and Johnson, A. E. (2002) Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin. Nat. Struct. Biol. 9, 823-827 (Pubitemid 35257781)
    • (2002) Nature Structural Biology , vol.9 , Issue.11 , pp. 823-827
    • Ramachandran, R.1    Heuck, A.P.2    Tweten, R.K.3    Johnson, A.E.4
  • 6
    • 38049125626 scopus 로고    scopus 로고
    • Structural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions
    • Soltani, C. E., Hotze, E. M., Johnson, A. E., and Tweten, R. K. (2007) Structural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions. Proc. Natl. Acad. Sci. U.S.A. 104, 20226-20231
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 20226-20231
    • Soltani, C.E.1    Hotze, E.M.2    Johnson, A.E.3    Tweten, R.K.4
  • 7
    • 3543016107 scopus 로고    scopus 로고
    • Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit β-strand alignment
    • DOI 10.1038/nsmb793
    • Ramachandran, R., Tweten, R. K., and Johnson, A. E. (2004) Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit β-strand alignment. Nat. Struct. Mol. Biol. 11, 697-705 (Pubitemid 39014494)
    • (2004) Nature Structural and Molecular Biology , vol.11 , Issue.8 , pp. 697-705
    • Ramachandran, R.1    Tweten, R.K.2    Johnson, A.E.3
  • 8
    • 0033615736 scopus 로고    scopus 로고
    • The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins
    • DOI 10.1016/S0092-8674(00)81660-8
    • Shatursky, O., Heuck, A. P., Shepard, L. A., Rossjohn, J., Parker, M. W., Johnson, A. E., and Tweten, R. K. (1999) The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins. Cell 99, 293-299 (Pubitemid 29519908)
    • (1999) Cell , vol.99 , Issue.3 , pp. 293-299
    • Shatursky, O.1    Heuck, A.P.2    Shepard, L.A.3    Rossjohn, J.4    Parker, M.W.5    Johnson, A.E.6    Tweten, R.K.7
  • 9
    • 0032514655 scopus 로고    scopus 로고
    • Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: An α-helical to β-sheet transition identified by fluorescence spectroscopy
    • DOI 10.1021/bi981452f
    • Shepard, L. A., Heuck, A. P., Hamman, B. D., Rossjohn, J., Parker, M. W., Ryan, K. R., Johnson, A. E., and Tweten, R. K. (1998) Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: an α-helical to β-sheet transition identified by fluorescence spectroscopy. Biochemistry 37, 14563-14574 (Pubitemid 28489065)
    • (1998) Biochemistry , vol.37 , Issue.41 , pp. 14563-14574
    • Shepard, L.A.1    Heuck, A.P.2    Hamman, B.D.3    Rossjohn, J.4    Parker, M.W.5    Ryan, K.R.6    Johnson, A.E.7    Tweten, R.K.8
  • 10
    • 0030592696 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of a thiol-activated cytolysin
    • DOI 10.1016/S0014-5793(96)01200-8, PII S0014579396012008
    • Feil, S. C., Rossjohn, J., Rohde, K., Tweten, R. K., and Parker, M. W. (1996) Crystallization and preliminary x-ray analysis of a thiol-activated cytolysin. FEBS Lett. 397, 290-292 (Pubitemid 26414035)
    • (1996) FEBS Letters , vol.397 , Issue.2-3 , pp. 290-292
    • Feil, S.C.1    Rossjohn, J.2    Rohde, K.3    Tweten, R.K.4    Parker, M.W.5
  • 11
    • 0030666371 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
    • Rossjohn, J., Feil, S. C., McKinstry, W. J., Tweten, R. K., and Parker, M. W. (1997) Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell 89, 685-692 (Pubitemid 27516171)
    • (1997) Cell , vol.89 , Issue.5 , pp. 685-692
    • Rossjohn, J.1    Feil, S.C.2    McKinstry, W.J.3    Tweten, R.K.4    Parker, M.W.5
  • 12
    • 33947163269 scopus 로고    scopus 로고
    • Structures of Perfringolysin O Suggest a Pathway for Activation of Cholesterol-dependent Cytolysins
    • DOI 10.1016/j.jmb.2007.01.042, PII S0022283607000824
    • Rossjohn, J., Polekhina, G., Feil, S. C., Morton, C. J., Tweten, R. K., and Parker, M. W. (2007) Structures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysins. J. Mol. Biol. 367, 1227-1236 (Pubitemid 46413267)
    • (2007) Journal of Molecular Biology , vol.367 , Issue.5 , pp. 1227-1236
    • Rossjohn, J.1    Polekhina, G.2    Feil, S.C.3    Morton, C.J.4    Tweten, R.K.5    Parker, M.W.6
  • 13
    • 0037192791 scopus 로고    scopus 로고
    • Monomer-monomer interactions drive the prepore to pore conversion of a β-barrel-forming cholesterol-dependent cytolysin
    • DOI 10.1074/jbc.M111039200
    • Hotze, E. M., Heuck, A. P., Czajkowsky, D. M., Shao, Z., Johnson, A. E., and Tweten, R. K. (2002) Monomer-monomer interactions drive the prepore to pore conversion of aβ-barrel-forming cholesterol-dependent cytolysin. J. Biol. Chem. 277, 11597-11605 (Pubitemid 34952932)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.13 , pp. 11597-11605
    • Hotze, E.M.1    Heuck, A.P.2    Czajkowsky, D.M.3    Shao, Z.4    Johnson, A.E.5    Tweten, R.K.6
  • 14
    • 34447536854 scopus 로고    scopus 로고
    • Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysin
    • DOI 10.1074/jbc.M701173200
    • Soltani, C. E., Hotze, E. M., Johnson, A. E., and Tweten, R. K. (2007) Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysin. J. Biol. Chem. 282, 15709-15716 (Pubitemid 47093275)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.21 , pp. 15709-15716
    • Soltani, C.E.1    Hotze, E.M.2    Johnson, A.E.3    Tweten, R.K.4
  • 15
    • 14844287849 scopus 로고    scopus 로고
    • (Ménez, A., ed) John Wiley & Sons, West Sussex, England
    • Hotze, E., and Tweten, R. K. (2002) in Perspectives in Molecular Toxinology (Ménez, A., ed) pp. 23-37, John Wiley & Sons, West Sussex, England
    • (2002) Perspectives in Molecular Toxinology , pp. 23-37
    • Hotze, E.1    Tweten, R.K.2
  • 16
    • 0035896507 scopus 로고    scopus 로고
    • Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane β-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 disulfide trapping synchronizes the insertion of the transmembrane β-sheet from a prepore intermediate. J. Biol. Chem. 276, 8261-8268
    • (2001) J. Biol. Chem. , vol.276 , pp. 8261-8268
    • Hotze, E.M.1    Wilson-Kubalek, E.M.2    Rossjohn, J.3    Parker, M.W.4    Johnson, A.E.5    Tweten, R.K.6
  • 17
    • 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 β-hairpins
    • DOI 10.1021/bi000436r
    • 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 β-hairpins. Biochemistry 39, 10284-10293 (Pubitemid 30663051)
    • (2000) Biochemistry , vol.39 , Issue.33 , pp. 10284-10293
    • Shepard, L.A.1    Shatursky, O.2    Johnson, A.E.3    Tweten, R.K.4
  • 18
    • 0028988973 scopus 로고
    • Interaction of θ-toxin (perfringolysin O), a cholesterol-binding cytolysin, with liposomal membranes: Change in the aromatic side chains upon binding and insertion
    • Nakamura, M., Sekino, N., Iwamoto, M., and Ohno-Iwashita, Y. (1995) Interaction of θ-toxin (perfringolysin O), a cholesterol-binding cytolysin, with liposomal membranes: change in the aromatic side chains upon binding and insertion. Biochemistry 34, 6513-6520
    • (1995) Biochemistry , vol.34 , pp. 6513-6520
    • Nakamura, M.1    Sekino, N.2    Iwamoto, M.3    Ohno-Iwashita, Y.4
  • 21
    • 34548670476 scopus 로고    scopus 로고
    • Structure of C8α-MACPF reveals mechanism of membrane attack in complement immune defense
    • DOI 10.1126/science.1147103
    • Hadders, M. A., Beringer, D. X., and Gros, P. (2007) Structure of C8α-MACPF reveals mechanism of membrane attack in complement immune defense. Science 317, 1552-1554 (Pubitemid 47417434)
    • (2007) Science , vol.317 , Issue.5844 , pp. 1552-1554
    • Hadders, M.A.1    Beringer, D.X.2    Gros, P.3
  • 24
    • 43049094015 scopus 로고    scopus 로고
    • Crystal structure of the MACPF domain of human complement protein C8α in complex with the C8γ subunit
    • Slade, D. J., Lovelace, L. L., Chruszcz, M., Minor, W., Lebioda, L., and Sodetz, J. M. (2008) Crystal structure of the MACPF domain of human complement protein C8α in complex with the C8γ subunit. J. Mol. Biol. 379, 331-342
    • (2008) J. Mol. Biol. , vol.379 , pp. 331-342
    • Slade, D.J.1    Lovelace, L.L.2    Chruszcz, M.3    Minor, W.4    Lebioda, L.5    Sodetz, J.M.6
  • 26
    • 79955953166 scopus 로고    scopus 로고
    • Structure of human C8 protein provides mechanistic insight into membrane pore formation by complement
    • Lovelace, L. L., Cooper, C. L., Sodetz, J. M., and Lebioda, L. (2011) Structure of human C8 protein provides mechanistic insight into membrane pore formation by complement. J. Biol. Chem. 286, 17585-17592
    • (2011) J. Biol. Chem. , vol.286 , pp. 17585-17592
    • Lovelace, L.L.1    Cooper, C.L.2    Sodetz, J.M.3    Lebioda, L.4
  • 27
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti, F., and Dobson, C. M. (2006) Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333-366 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 28
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti, F., and Dobson, C. M. (2009) Amyloid formation by globular proteins under native conditions. Nat. Chem. Biol. 5, 15-22
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.