메뉴 건너뛰기




Volumn 106, Issue 51, 2009, Pages 21555-21560

Lethal factor unfolding is the most force-dependent step of anthrax toxin translocation

Author keywords

Mechanical unfolding; Transition state structure; Unfolding pathway

Indexed keywords

ANTHRAX TOXIN; PHENYLALANINE;

EID: 76049107424     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0905880106     Document Type: Article
Times cited : (53)

References (29)
  • 1
    • 5344269437 scopus 로고    scopus 로고
    • Sculpting the proteomewith AAA(+) proteases and disassembly machines
    • Sauer RT, et al. (2004) Sculpting the proteomewith AAA(+) proteases and disassembly machines. Cell 119:9-18.
    • (2004) Cell , vol.119 , pp. 9-18
    • Sauer, R.T.1
  • 2
    • 0037308999 scopus 로고    scopus 로고
    • Protein unfolding - an important process in vivo?
    • MatouschekA
    • MatouschekA(2003) Protein unfolding - an important process in vivo? Curr Opin Struct Biol 13:98-109.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 98-109
  • 3
    • 10044281903 scopus 로고    scopus 로고
    • Protein translocation through anthrax toxin channels formed in planar lipid bilayers
    • Zhang S, Udho E, Wu Z, Collier RJ, Finkelstein A (2004) Protein translocation through anthrax toxin channels formed in planar lipid bilayers. Biophys J 87:3842-3849.
    • (2004) Biophys J , vol.87 , pp. 3842-3849
    • Zhang, S.1    Udho, E.2    Wu, Z.3    Collier, R.J.4    Finkelstein, A.5
  • 4
    • 29444456231 scopus 로고    scopus 로고
    • Protein translocation through the anthrax toxin transmembrane pore is driven by a proton gradient
    • Krantz BA, Finkelstein A, Collier RJ (2006) Protein translocation through the anthrax toxin transmembrane pore is driven by a proton gradient. J Mol Biol 355:968-979.
    • (2006) J Mol Biol , vol.355 , pp. 968-979
    • Krantz, B.A.1    Finkelstein, A.2    Collier, R.J.3
  • 5
    • 0022515029 scopus 로고
    • Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
    • Eilers M, Schatz G (1986) Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria. Nature 322:228-232.
    • (1986) Nature , vol.322 , pp. 228-232
    • Eilers, M.1    Schatz, G.2
  • 7
    • 0035875890 scopus 로고    scopus 로고
    • Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine
    • Burton RE, Siddiqui SM, Kim YI, Baker TA, Sauer RT (2001) Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine. EMBO J 20:3092-3100.
    • (2001) EMBO J , vol.20 , pp. 3092-3100
    • Burton, R.E.1    Siddiqui, S.M.2    Kim, Y.I.3    Baker, T.A.4    Sauer, R.T.5
  • 8
    • 0042329502 scopus 로고    scopus 로고
    • Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine
    • Kenniston JA, Baker TA, Fernandez JM, Sauer RT (2003) Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine. Cell 114:511-520.
    • (2003) Cell , vol.114 , pp. 511-520
    • Kenniston, J.A.1    Baker, T.A.2    Fernandez, J.M.3    Sauer, R.T.4
  • 9
    • 0037059032 scopus 로고    scopus 로고
    • Submolecular cooperativity produces multi-state protein unfolding and refolding
    • Englander SW, Mayne L, Rumbley JN (2002) Submolecular cooperativity produces multi-state protein unfolding and refolding. Biophys Chem 101-102:57-65.
    • (2002) Biophys Chem , vol.101-102 , pp. 57-65
    • Englander, S.W.1    Mayne, L.2    Rumbley, J.N.3
  • 10
    • 0029643523 scopus 로고
    • Protein folding intermediates studied by native state hydrogen exchange
    • Bai Y, Sosnick TR, Mayne L, Englander SW (1995) Protein folding intermediates studied by native state hydrogen exchange. Science 269:192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 11
    • 34447291354 scopus 로고    scopus 로고
    • Anthrax Toxin: Receptor-Binding, Internalization, Pore Formation, and Translocation
    • Young JA, Collier RJ (2007) Anthrax Toxin: Receptor-Binding, Internalization, Pore Formation, and Translocation Annu Rev Biochem 76:243-265.
    • (2007) Annu Rev Biochem , vol.76 , pp. 243-265
    • Young, J.A.1    Collier, R.J.2
  • 12
    • 7944221639 scopus 로고    scopus 로고
    • Acid-induced unfolding of the amino-terminal domains of the lethal and edema factors of anthrax toxin
    • Krantz BA, Trivedi AD, Cunningham K, Christensen KA, Collier RJ (2004) Acid-induced unfolding of the amino-terminal domains of the lethal and edema factors of anthrax toxin. J Mol Biol 344:739-756.
    • (2004) J Mol Biol , vol.344 , pp. 739-756
    • Krantz, B.A.1    Trivedi, A.D.2    Cunningham, K.3    Christensen, K.A.4    Collier, R.J.5
  • 13
    • 23044508996 scopus 로고    scopus 로고
    • Aphenylalanine clamp catalyzes protein translocation through the anthrax toxin pore
    • Krantz BA, et al. (2005)Aphenylalanine clamp catalyzes protein translocation through the anthrax toxin pore. Science 309:777-781.
    • (2005) Science , vol.309 , pp. 777-781
    • Krantz, B.A.1
  • 14
    • 0015879604 scopus 로고
    • Ionic blockage of sodium channels in nerve
    • Woodhull AM (1973) Ionic blockage of sodium channels in nerve. J Gen Physiol 61:687-708.
    • (1973) J Gen Physiol , vol.61 , pp. 687-708
    • Woodhull, A.M.1
  • 15
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • Matouschek A, Kellis JT, Jr, Serrano L, Fersht AR (1989) Mapping the transition state and pathway of protein folding by protein engineering. Nature 340:122-126.
    • (1989) Nature , vol.340 , pp. 122-126
    • Matouschek, A.1    Kellis Jr, J.T.2    Serrano, L.3    Fersht, A.R.4
  • 16
    • 0037169549 scopus 로고    scopus 로고
    • Mapping the anthrax protective antigen binding site on the lethal and edema factors
    • Lacy DB, Mourez M, Fouassier A, Collier RJ (2002) Mapping the anthrax protective antigen binding site on the lethal and edema factors. J Biol Chem 277:3006-3010.
    • (2002) J Biol Chem , vol.277 , pp. 3006-3010
    • Lacy, D.B.1    Mourez, M.2    Fouassier, A.3    Collier, R.J.4
  • 17
    • 28044436994 scopus 로고    scopus 로고
    • A model of anthrax toxin lethal factor bound to protective antigen
    • Lacy DB, et al. (2005) A model of anthrax toxin lethal factor bound to protective antigen. Proc Natl Acad Sci USA 102:16409-16414.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16409-16414
    • Lacy, D.B.1
  • 18
    • 0030322783 scopus 로고    scopus 로고
    • Double mutant cycles; a powerful tool for analyzing protein structure and function
    • Horovitz A (1996) Double mutant cycles; a powerful tool for analyzing protein structure and function. Folding Design 1:R121-R126.
    • (1996) Folding Design , vol.1
    • Horovitz, A.1
  • 19
    • 43749107950 scopus 로고    scopus 로고
    • Mechanical biochemistry of proteins one molecule at a time
    • Oberhauser AF, Carrion-Vazquez M (2008) Mechanical biochemistry of proteins one molecule at a time. J Biol Chem 283:6617-6621.
    • (2008) J Biol Chem , vol.283 , pp. 6617-6621
    • Oberhauser, A.F.1    Carrion-Vazquez, M.2
  • 20
    • 0036221085 scopus 로고    scopus 로고
    • Protein unfolding by the mitochondrial membrane potential
    • Huang S, Ratliff KS, Matouschek A (2002) Protein unfolding by the mitochondrial membrane potential. Nat Struct Biol 9:301-307.
    • (2002) Nat Struct Biol , vol.9 , pp. 301-307
    • Huang, S.1    Ratliff, K.S.2    Matouschek, A.3
  • 21
    • 2942694473 scopus 로고    scopus 로고
    • The force exerted by the membrane potential during protein import into the mitochondrial matrix
    • MatouschekA
    • Shariff K, Ghosal S, MatouschekA(2004) The force exerted by the membrane potential during protein import into the mitochondrial matrix. Biophys J 86:3647-3652.
    • (2004) Biophys J , vol.86 , pp. 3647-3652
    • Shariff, K.1    Ghosal, S.2
  • 22
    • 0024523836 scopus 로고
    • Anthrax toxin: Channelforming activity of protective antigen in planar phospholipid bilayers
    • Blaustein RO, Koehler TM, Collier RJ, Finkelstein A (1989) Anthrax toxin: Channelforming activity of protective antigen in planar phospholipid bilayers. Proc Natl Acad Sci USA 86:2209-2213.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2209-2213
    • Blaustein, R.O.1    Koehler, T.M.2    Collier, R.J.3    Finkelstein, A.4
  • 23
    • 10044247127 scopus 로고    scopus 로고
    • Evidence that translocation of anthrax toxin's lethal factor is initiated by entry of its N terminus into the protective antigen channel
    • Zhang S, Finkelstein A, Collier RJ (2004) Evidence that translocation of anthrax toxin's lethal factor is initiated by entry of its N terminus into the protective antigen channel. Proc Natl Acad Sci USA 101:16756-16761.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16756-16761
    • Zhang, S.1    Finkelstein, A.2    Collier, R.J.3
  • 24
    • 0042508740 scopus 로고    scopus 로고
    • The mechanical stability of ubiquitin is linkage dependent
    • Carrion-Vazquez M, et al. (2003) The mechanical stability of ubiquitin is linkage dependent. Nat Struct Biol 10:738-743.
    • (2003) Nat Struct Biol , vol.10 , pp. 738-743
    • Carrion-Vazquez, M.1
  • 25
    • 0042508741 scopus 로고    scopus 로고
    • Pulling geometry defines the mechanical resistance of a beta-sheet protein
    • Brockwell DJ, et al. (2003) Pulling geometry defines the mechanical resistance of a beta-sheet protein. Nat Struct Biol 10:731-737.
    • (2003) Nat Struct Biol , vol.10 , pp. 731-737
    • Brockwell, D.J.1
  • 26
    • 1642308732 scopus 로고    scopus 로고
    • Effects of local protein stability and the geometric position of the substrate degradation tag on the efficiency of ClpXP denaturation and degradation
    • Kenniston JA, Burton RE, Siddiqui SM, Baker TA, Sauer RT (2004) Effects of local protein stability and the geometric position of the substrate degradation tag on the efficiency of ClpXP denaturation and degradation. J Struct Biol 146:130-140.
    • (2004) J Struct Biol , vol.146 , pp. 130-140
    • Kenniston, J.A.1    Burton, R.E.2    Siddiqui, S.M.3    Baker, T.A.4    Sauer, R.T.5
  • 27
    • 1642307617 scopus 로고    scopus 로고
    • The folding pathway of barnase: The rate-limiting transition state and a hidden intermediate under native conditions
    • Vu ND, Feng H, Bai Y (2004) The folding pathway of barnase: The rate-limiting transition state and a hidden intermediate under native conditions. Biochemistry 43:3346-3356.
    • (2004) Biochemistry , vol.43 , pp. 3346-3356
    • Vu, N.D.1    Feng, H.2    Bai, Y.3
  • 28
    • 0030781431 scopus 로고    scopus 로고
    • Active unfolding of precursor proteins during mitochondrial protein import
    • Matouschek A, et al. (1997) Active unfolding of precursor proteins during mitochondrial protein import. EMBO J 16:6727-6736.
    • (1997) EMBO J , vol.16 , pp. 6727-6736
    • Matouschek, A.1
  • 29
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - a visualization system for exploratory research and analysis
    • Pettersen EF, et al. (2004) UCSF Chimera - a visualization system for exploratory research and analysis. J Comput Chem 25:1605-1612.
    • (2004) J Comput Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.