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Volumn 10, Issue 1, 2003, Pages 13-18

Translocation of botulinum neurotoxin light chain protease through the heavy chain channel

Author keywords

[No Author keywords available]

Indexed keywords

BOTULINUM TOXIN A; CHAPERONE; CLOSTRIDIUM TOXIN; MEMBRANE PROTEIN; PROTEINASE;

EID: 0037222077     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb879     Document Type: Article
Times cited : (285)

References (35)
  • 1
    • 0026497466 scopus 로고
    • Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin
    • Schiavo, G. et al. Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin. Nature 359, 832-835 (1992).
    • (1992) Nature , vol.359 , pp. 832-835
    • Schiavo, G.1
  • 3
    • 0027219725 scopus 로고
    • Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25
    • Blasi, J. et al. Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25. Nature 365, 160-163 (1993).
    • (1993) Nature , vol.365 , pp. 160-163
    • Blasi, J.1
  • 4
    • 0027413655 scopus 로고
    • SNAP receptors implicated in vesicle targeting and fusion
    • Sollner, T. et al. SNAP receptors implicated in vesicle targeting and fusion. Nature 362, 318-324 (1993).
    • (1993) Nature , vol.362 , pp. 318-324
    • Sollner, T.1
  • 5
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • Sutton, R.B., Fasshauer, D., Jahn, R. & Brunger, A.T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution. Nature 395, 347-353 (1998).
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 6
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn, R. & Sudhof, T.C. Membrane fusion and exocytosis. Annu. Rev. Biochem. 68, 863-911 (1999).
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 863-911
    • Jahn, R.1    Sudhof, T.C.2
  • 7
    • 0028906375 scopus 로고
    • Quantitative measurement of intraorganelle pH in the endosomal-lysosomal pathway in neurons by using ratiometric imaging with pyranine
    • Overly, C.C., Lee, K.D., Berthiaume, E. & Hollenbeck, P.J. Quantitative measurement of intraorganelle pH in the endosomal-lysosomal pathway in neurons by using ratiometric imaging with pyranine. Proc. Natl. Acad. Sci. USA 92, 3156-3160 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3156-3160
    • Overly, C.C.1    Lee, K.D.2    Berthiaume, E.3    Hollenbeck, P.J.4
  • 9
    • 0031712779 scopus 로고    scopus 로고
    • Crystal structure of botulinum neurotoxin type A and implications for toxicity
    • Lacy, D.B., Tepp, W., Cohen, A.C., DasGupta, B.R. & Stevens, R.C. Crystal structure of botulinum neurotoxin type A and implications for toxicity. Nat. Struct. Biol. 5, 898-902 (1998).
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 898-902
    • Lacy, D.B.1    Tepp, W.2    Cohen, A.C.3    DasGupta, B.R.4    Stevens, R.C.5
  • 10
    • 0033884053 scopus 로고    scopus 로고
    • Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B
    • Swaminathan, S. & Eswaramoorthy, S. Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B. Nat. Struct. Biol. 7, 693-699 (2000).
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 693-699
    • Swaminathan, S.1    Eswaramoorthy, S.2
  • 11
    • 0020069806 scopus 로고
    • Insertion of diphtheria toxin into and across membranes: Role of phosphoinositide asymmetry
    • Donovan, J.J., Simon, M.I. & Montal, M. Insertion of diphtheria toxin into and across membranes: Role of phosphoinositide asymmetry. Nature 298, 669-672 (1982).
    • (1982) Nature , vol.298 , pp. 669-672
    • Donovan, J.J.1    Simon, M.I.2    Montal, M.3
  • 12
    • 0023903076 scopus 로고
    • Characterization of the channel properties of tetanus toxin in planar lipid bilayers
    • Gambale, F. & Montal, M. Characterization of the channel properties of tetanus toxin in planar lipid bilayers. Biophys. J. 53, 771-783 (1988).
    • (1988) Biophys. J. , vol.53 , pp. 771-783
    • Gambale, F.1    Montal, M.2
  • 13
    • 0029115961 scopus 로고
    • Formation of ion channels in lipid bilayers by a peptide with the predicted transmembrane sequence of botulinum neurotoxin A
    • Oblatt-Montal, M., Yamazaki, M., Nelson, R. & Montal, M. Formation of ion channels in lipid bilayers by a peptide with the predicted transmembrane sequence of botulinum neurotoxin A. Protein Sci. 4, 1490-1497 (1995).
    • (1995) Protein Sci. , vol.4 , pp. 1490-1497
    • Oblatt-Montal, M.1    Yamazaki, M.2    Nelson, R.3    Montal, M.4
  • 14
    • 0345570658 scopus 로고
    • Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: Relevance to translocation of proteins across membranes
    • Hoch, D.H. et al. Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: Relevance to translocation of proteins across membranes. Proc. Natl. Acad. Sci. USA 82, 1692-1696 (1985).
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1692-1696
    • Hoch, D.H.1
  • 15
    • 0023662110 scopus 로고
    • The N-terminal half of the heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayers
    • Blaustein, R.O., Germann, W.J., Finkelstein, A. & DasGupta, B.R. The N-terminal half of the heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayers. FEBS Lett. 226, 115-120 (1987).
    • (1987) FEBS Lett. , vol.226 , pp. 115-120
    • Blaustein, R.O.1    Germann, W.J.2    Finkelstein, A.3    DasGupta, B.R.4
  • 16
    • 0031840854 scopus 로고    scopus 로고
    • Gating and permeability of ion channels produced by botulinum toxin types A and E in PC12 cell membranes
    • Sheridan, R.E. Gating and permeability of ion channels produced by botulinum toxin types A and E in PC12 cell membranes. Toxicon 36, 703-717 (1998).
    • (1998) Toxicon , vol.36 , pp. 703-717
    • Sheridan, R.E.1
  • 17
    • 0000483941 scopus 로고    scopus 로고
    • Translocation of the catalytic domain of diphtheria toxin across planar phospholipid bilayers by its own T domain
    • Oh, K.J., Senzel, L., Collier, R.J. & Finkelstein, A. Translocation of the catalytic domain of diphtheria toxin across planar phospholipid bilayers by its own T domain. Proc. Natl. Acad. Sci. USA 96, 8467-8470 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8467-8470
    • Oh, K.J.1    Senzel, L.2    Collier, R.J.3    Finkelstein, A.4
  • 18
    • 0031042584 scopus 로고    scopus 로고
    • A novel method for structure-based prediction of ion channel conductance properties
    • Smart, O.S., Breed, J., Smith, G.R. & Sansom, M.S. A novel method for structure-based prediction of ion channel conductance properties. Biophys. J. 72, 1109-1126 (1997).
    • (1997) Biophys. J. , vol.72 , pp. 1109-1126
    • Smart, O.S.1    Breed, J.2    Smith, G.R.3    Sansom, M.S.4
  • 19
    • 0027312063 scopus 로고
    • Inhibition of a reductive function of the plasma membrane by bacitracin and antibodies against protein disulfide-isomerase
    • Mandel, R., Ryser, H.J., Ghani, F., Wu, M. & Peak, D. Inhibition of a reductive function of the plasma membrane by bacitracin and antibodies against protein disulfide-isomerase. Proc. Natl. Acad. Sci. USA 90, 4112-4116 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4112-4116
    • Mandel, R.1    Ryser, H.J.2    Ghani, F.3    Wu, M.4    Peak, D.5
  • 20
    • 0033680802 scopus 로고    scopus 로고
    • Structure of the molecular chaperone prefoldin: Unique interaction of multiple coiled coil tentacles with unfolded proteins
    • Siegert, R., Leroux, M.R., Scheufler, C., Hartl, F.U. & Moarefi, I. Structure of the molecular chaperone prefoldin: Unique interaction of multiple coiled coil tentacles with unfolded proteins. Cell 103, 621-632 (2000).
    • (2000) Cell , vol.103 , pp. 621-632
    • Siegert, R.1    Leroux, M.R.2    Scheufler, C.3    Hartl, F.U.4    Moarefi, I.5
  • 21
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • Tsai, B., Rodighiero, C., Lencer, W.I. & Rapoport, T.A. Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell 104, 937-948 (2001).
    • (2001) Cell , vol.104 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 22
    • 0035499438 scopus 로고    scopus 로고
    • Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion
    • Stebbins, C.E. & Galan, J.E. Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Nature 414, 77-81 (2001).
    • (2001) Nature , vol.414 , pp. 77-81
    • Stebbins, C.E.1    Galan, J.E.2
  • 23
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov, I.N. & Bourne, P.E. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11, 739-747 (1998).
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 24
    • 0033532355 scopus 로고    scopus 로고
    • Interaction of diphtheria toxin T domain with molten globule-like proteins and its implications for translocation
    • Ren, J. et al. Interaction of diphtheria toxin T domain with molten globule-like proteins and its implications for translocation. Science 284, 955-957 (1999).
    • (1999) Science , vol.284 , pp. 955-957
    • Ren, J.1
  • 25
    • 0035798359 scopus 로고    scopus 로고
    • Architecture of the protein-conducting channel associated with the translating 805 ribosome
    • Beckmann, R. et al. Architecture of the protein-conducting channel associated with the translating 805 ribosome. Cell 107, 361-372 (2001).
    • (2001) Cell , vol.107 , pp. 361-372
    • Beckmann, R.1
  • 26
    • 0037043724 scopus 로고    scopus 로고
    • Three-dimensional structure of the bacterial protein-translocation complex SecYEG
    • Breyton, C., Haase, W., Rapoport, T.A., Kuhlbrandt, W. & Collinson, I. Three-dimensional structure of the bacterial protein-translocation complex SecYEG. Nature 418, 662-665 (2002).
    • (2002) Nature , vol.418 , pp. 662-665
    • Breyton, C.1    Haase, W.2    Rapoport, T.A.3    Kuhlbrandt, W.4    Collinson, I.5
  • 27
    • 0035190910 scopus 로고    scopus 로고
    • A presequence- and voltage-sensitive channel of the mitochondrial preprotein translocase formed by Tim 23
    • Truscott, K.N. et al. A presequence- and voltage-sensitive channel of the mitochondrial preprotein translocase formed by Tim23. Nat. Struct. Biol. 8, 1074-1082 (2001).
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 1074-1082
    • Truscott, K.N.1
  • 28
    • 0035997027 scopus 로고    scopus 로고
    • The chloroplast protein import channel toc75: Pore properties and interaction with transit peptides
    • Hinnah, S.C., Wagner, R., Sveshnikova, N., Harrer, R. & Soil, J. The chloroplast protein import channel toc75: Pore properties and interaction with transit peptides. Biophys. J. 83, 899-911 (2002).
    • (2002) Biophys. J. , vol.83 , pp. 899-911
    • Hinnah, S.C.1    Wagner, R.2    Sveshnikova, N.3    Harrer, R.4    Soil, J.5
  • 29
    • 0037013850 scopus 로고    scopus 로고
    • The preprotein conducting channel at the inner envelope membrane of plastids
    • Heins, L. et al. The preprotein conducting channel at the inner envelope membrane of plastids. EMBO J. 21, 2616-2625 (2002).
    • (2002) EMBO J. , vol.21 , pp. 2616-2625
    • Heins, L.1
  • 30
    • 0016379265 scopus 로고
    • Formation of bimolecular membranes from lipid monolayers
    • Montal, M. Formation of bimolecular membranes from lipid monolayers. Methods Enzymol. 32, 545-554 (1974).
    • (1974) Methods Enzymol. , vol.32 , pp. 545-554
    • Montal, M.1
  • 31
    • 0033486255 scopus 로고    scopus 로고
    • High-level expression, purification, and characterization of recombinant type A botulinum neurotoxin light chain
    • Li, L. & Singh, B.R. High-level expression, purification, and characterization of recombinant type A botulinum neurotoxin light chain. Protein Expr. Purif. 17, 339-344 (1999).
    • (1999) Protein Expr. Purif. , vol.17 , pp. 339-344
    • Li, L.1    Singh, B.R.2
  • 32
    • 0035916282 scopus 로고    scopus 로고
    • Thermal stabilization of the catalytic domain of botulinum neurotoxin E by phosphorylation of a single tyrosine residue
    • Blanes-Mira, C. et al. Thermal stabilization of the catalytic domain of botulinum neurotoxin E by phosphorylation of a single tyrosine residue. Biochemistry 40, 2234-2242 (2001).
    • (2001) Biochemistry , vol.40 , pp. 2234-2242
    • Blanes-Mira, C.1
  • 33
    • 0036156870 scopus 로고    scopus 로고
    • Development and validation of a quantitative ELISA for the measurement of PSA concentration
    • Acevedo, B. et al. Development and validation of a quantitative ELISA for the measurement of PSA concentration. Clin. Chim. Acta 317, 55-63 (2002).
    • (2002) Clin. Chim. Acta , vol.317 , pp. 55-63
    • Acevedo, B.1
  • 34
    • 0032545285 scopus 로고    scopus 로고
    • Assembly of a ternary complex by the predicted minimal coiled-coil-forming domains of syntaxin, SNAP-25, and synaptobrevin. A circular dichroism study
    • Canaves, J.M. & Montal, M. Assembly of a ternary complex by the predicted minimal coiled-coil-forming domains of syntaxin, SNAP-25, and synaptobrevin. A circular dichroism study. J. Biol. Chem. 273, 34214-34221 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 34214-34221
    • Canaves, J.M.1    Montal, M.2
  • 35
    • 0039842494 scopus 로고    scopus 로고
    • Spectroscopic analysis of pH-induced changes in the molecular features of type A botulinum neurotoxin light chain
    • Li, L. & Singh, B.R. Spectroscopic analysis of pH-induced changes in the molecular features of type A botulinum neurotoxin light chain. Biochemistry 39, 6466-6474 (2000).
    • (2000) Biochemistry , vol.39 , pp. 6466-6474
    • Li, L.1    Singh, B.R.2


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