메뉴 건너뛰기




Volumn 54, Issue 5, 2009, Pages 565-569

Translocation of botulinum neurotoxin light chain protease by the heavy chain protein-conducting channel

Author keywords

Channels; Chaperone; Membranes; Neurotoxicity; Protein translocation

Indexed keywords

BOTULINUM TOXIN; BOTULINUM TOXIN A; BOTULINUM TOXIN E; PROTEINASE; SNARE PROTEIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25;

EID: 68849127717     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2008.11.018     Document Type: Article
Times cited : (51)

References (34)
  • 1
    • 24344470084 scopus 로고    scopus 로고
    • Structural analysis of botulinum neurotoxin serotype F light chain: implications on substrate binding and inhibitor design
    • Agarwal R., Binz T., and Swaminathan S. Structural analysis of botulinum neurotoxin serotype F light chain: implications on substrate binding and inhibitor design. Biochemistry 44 (2005) 11758-11765
    • (2005) Biochemistry , vol.44 , pp. 11758-11765
    • Agarwal, R.1    Binz, T.2    Swaminathan, S.3
  • 2
    • 2542517864 scopus 로고    scopus 로고
    • Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212 → Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway
    • Agarwal R., Eswaramoorthy S., Kumaran D., Binz T., and Swaminathan S. Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212 → Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway. Biochemistry 43 (2004) 6637-6644
    • (2004) Biochemistry , vol.43 , pp. 6637-6644
    • Agarwal, R.1    Eswaramoorthy, S.2    Kumaran, D.3    Binz, T.4    Swaminathan, S.5
  • 3
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: preparing the next generation of molecular biologists
    • Alberts B. The cell as a collection of protein machines: preparing the next generation of molecular biologists. Cell 92 (1998) 291-294
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1
  • 4
    • 33644859288 scopus 로고    scopus 로고
    • Structure of botulinum neurotoxin type D light chain at 1.65 A resolution: repercussions for VAMP-2 substrate specificity
    • Arndt J.W., Chai Q., Christian T., and Stevens R.C. Structure of botulinum neurotoxin type D light chain at 1.65 A resolution: repercussions for VAMP-2 substrate specificity. Biochemistry 45 (2006) 3255-3262
    • (2006) Biochemistry , vol.45 , pp. 3255-3262
    • Arndt, J.W.1    Chai, Q.2    Christian, T.3    Stevens, R.C.4
  • 5
    • 22244456750 scopus 로고    scopus 로고
    • Crystal structure of botulinum neurotoxin type G light chain: serotype divergence in substrate recognition
    • Arndt J.W., Yu W., Bi F., and Stevens R.C. Crystal structure of botulinum neurotoxin type G light chain: serotype divergence in substrate recognition. Biochemistry 44 (2005) 9574-9580
    • (2005) Biochemistry , vol.44 , pp. 9574-9580
    • Arndt, J.W.1    Yu, W.2    Bi, F.3    Stevens, R.C.4
  • 7
    • 11144341950 scopus 로고    scopus 로고
    • Substrate recognition strategy for botulinum neurotoxin serotype A
    • Breidenbach M.A., and Brunger A.T. Substrate recognition strategy for botulinum neurotoxin serotype A. Nature 432 (2004) 925-929
    • (2004) Nature , vol.432 , pp. 925-929
    • Breidenbach, M.A.1    Brunger, A.T.2
  • 8
    • 34848840291 scopus 로고    scopus 로고
    • Botulinum neurotoxin heavy chain belt as an intramolecular chaperone for the light chain
    • Brunger A.T., Breidenbach M.A., Jin R., Fischer A., Santos J.S., and Montal M. Botulinum neurotoxin heavy chain belt as an intramolecular chaperone for the light chain. PLoS Pathog 3 (2007) 1191-1194
    • (2007) PLoS Pathog , vol.3 , pp. 1191-1194
    • Brunger, A.T.1    Breidenbach, M.A.2    Jin, R.3    Fischer, A.4    Santos, J.S.5    Montal, M.6
  • 9
  • 10
    • 34248213125 scopus 로고    scopus 로고
    • Mechanism of substrate recognition by botulinum neurotoxin serotype A
    • Chen S., Kim J.J., and Barbieri J.T. Mechanism of substrate recognition by botulinum neurotoxin serotype A. J. Biol. Chem. 282 (2007) 9621-9627
    • (2007) J. Biol. Chem. , vol.282 , pp. 9621-9627
    • Chen, S.1    Kim, J.J.2    Barbieri, J.T.3
  • 11
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., and Wright P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6 (2005) 197-208
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 12
  • 13
    • 33747174022 scopus 로고    scopus 로고
    • Characterization of Clostridial botulinum neurotoxin channels in neuroblastoma cells
    • Fischer A., and Montal M. Characterization of Clostridial botulinum neurotoxin channels in neuroblastoma cells. Neurotox. Res. 9 (2006) 93-100
    • (2006) Neurotox. Res. , vol.9 , pp. 93-100
    • Fischer, A.1    Montal, M.2
  • 14
    • 35748961106 scopus 로고    scopus 로고
    • Crucial role of the disulfide bridge between botulinum neurotoxin light and heavy chains in protease translocation across membranes
    • Fischer A., and Montal M. Crucial role of the disulfide bridge between botulinum neurotoxin light and heavy chains in protease translocation across membranes. J. Biol. Chem. 282 (2007) 29604-29611
    • (2007) J. Biol. Chem. , vol.282 , pp. 29604-29611
    • Fischer, A.1    Montal, M.2
  • 15
    • 34547509346 scopus 로고    scopus 로고
    • Single molecule detection of intermediates during botulinum neurotoxin translocation across membranes
    • Fischer A., and Montal M. Single molecule detection of intermediates during botulinum neurotoxin translocation across membranes. Proc. Natl. Acad. Sci. U S A 104 (2007) 10447-10452
    • (2007) Proc. Natl. Acad. Sci. U S A , vol.104 , pp. 10447-10452
    • Fischer, A.1    Montal, M.2
  • 18
    • 0033887403 scopus 로고    scopus 로고
    • Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution
    • Hanson M.A., and Stevens R.C. Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution. Nat. Struct. Biol. 7 (2000) 687-692
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 687-692
    • Hanson, M.A.1    Stevens, R.C.2
  • 19
    • 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., Romero-Mira M., Ehrlich B.E., Finkelstein A., DasGupta B.R., and Simpson L.L. 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 (1985) 1692-1696
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1692-1696
    • Hoch, D.H.1    Romero-Mira, M.2    Ehrlich, B.E.3    Finkelstein, A.4    DasGupta, B.R.5    Simpson, L.L.6
  • 20
    • 33845871995 scopus 로고    scopus 로고
    • Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity
    • Jin R., Rummel A., Binz T., and Brunger A.T. Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity. Nature 444 (2006) 1092-1095
    • (2006) Nature , vol.444 , pp. 1092-1095
    • Jin, R.1    Rummel, A.2    Binz, T.3    Brunger, A.T.4
  • 21
    • 34548688418 scopus 로고    scopus 로고
    • Structural and biochemical studies of botulinum neurotoxin serotype C1 light chain protease: implications for dual substrate specificity
    • Jin R., Sikorra S., Stegmann C.M., Pich A., Binz T., and Brunger A.T. Structural and biochemical studies of botulinum neurotoxin serotype C1 light chain protease: implications for dual substrate specificity. Biochemistry 46 (2007) 10685-10693
    • (2007) Biochemistry , vol.46 , pp. 10685-10693
    • Jin, R.1    Sikorra, S.2    Stegmann, C.M.3    Pich, A.4    Binz, T.5    Brunger, A.T.6
  • 22
    • 0037222077 scopus 로고    scopus 로고
    • Translocation of botulinum neurotoxin light chain protease through the heavy chain channel
    • Koriazova L.K., and Montal M. Translocation of botulinum neurotoxin light chain protease through the heavy chain channel. Nat. Struct. Biol. 10 (2003) 13-18
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 13-18
    • Koriazova, L.K.1    Montal, M.2
  • 23
    • 29444456231 scopus 로고    scopus 로고
    • Protein translocation through the anthrax toxin transmembrane pore is driven by a proton gradient
    • Krantz B.A., Finkelstein A., and Collier R.J. Protein translocation through the anthrax toxin transmembrane pore is driven by a proton gradient. J. Mol. Biol. 355 (2006) 968-979
    • (2006) J. Mol. Biol. , vol.355 , pp. 968-979
    • Krantz, B.A.1    Finkelstein, A.2    Collier, R.J.3
  • 24
    • 0031282024 scopus 로고    scopus 로고
    • Recombinant expression and purification of the botulinum neurotoxin type A translocation domain
    • Lacy D.B., and Stevens R.C. Recombinant expression and purification of the botulinum neurotoxin type A translocation domain. Protein Expr. Purif. 11 (1997) 195-200
    • (1997) Protein Expr. Purif. , vol.11 , pp. 195-200
    • Lacy, D.B.1    Stevens, R.C.2
  • 25
    • 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., and Stevens R.C. Crystal structure of botulinum neurotoxin type A and implications for toxicity. Nat. Struct. Biol. 5 (1998) 898-902
    • (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
  • 26
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • Rapoport T.A. Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature 450 (2007) 663-669
    • (2007) Nature , vol.450 , pp. 663-669
    • Rapoport, T.A.1
  • 27
    • 39349112321 scopus 로고    scopus 로고
    • Presynaptic neurotoxins with enzymatic activities
    • Rossetto O., and Montecucco C. Presynaptic neurotoxins with enzymatic activities. Handb. Exp. Pharmacol. (2008) 129-170
    • (2008) Handb. Exp. Pharmacol. , pp. 129-170
    • Rossetto, O.1    Montecucco, C.2
  • 29
    • 2342510157 scopus 로고    scopus 로고
    • Crystal structure of Clostridium botulinum neurotoxin protease in a product-bound state: evidence for noncanonical zinc protease activity
    • Segelke B., Knapp M., Kadkhodayan S., Balhorn R., and Rupp B. Crystal structure of Clostridium botulinum neurotoxin protease in a product-bound state: evidence for noncanonical zinc protease activity. Proc. Natl. Acad. Sci. USA 101 (2004) 6888-6893
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6888-6893
    • Segelke, B.1    Knapp, M.2    Kadkhodayan, S.3    Balhorn, R.4    Rupp, B.5
  • 30
    • 34248594822 scopus 로고    scopus 로고
    • Structures of Clostridium botulinum neurotoxin serotype A light chain complexed with small-molecule inhibitors highlight active-site flexibility
    • Silvaggi N.R., Boldt G.E., Hixon M.S., Kennedy J.P., Tzipori S., Janda K.D., and Allen K.N. Structures of Clostridium botulinum neurotoxin serotype A light chain complexed with small-molecule inhibitors highlight active-site flexibility. Chem. Biol. 14 (2007) 533-542
    • (2007) Chem. Biol. , vol.14 , pp. 533-542
    • Silvaggi, N.R.1    Boldt, G.E.2    Hixon, M.S.3    Kennedy, J.P.4    Tzipori, S.5    Janda, K.D.6    Allen, K.N.7
  • 31
    • 1342323663 scopus 로고    scopus 로고
    • Identification of the major steps in botulinum toxin action
    • Simpson L.L. Identification of the major steps in botulinum toxin action. Annu. Rev. Pharmacol. Toxicol. 44 (2004) 167-193
    • (2004) Annu. Rev. Pharmacol. Toxicol. , vol.44 , pp. 167-193
    • Simpson, L.L.1
  • 32
    • 0033884053 scopus 로고    scopus 로고
    • Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B
    • Swaminathan S., and Eswaramoorthy S. Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B. Nat. Struct. Biol. 7 (2000) 693-699
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 693-699
    • Swaminathan, S.1    Eswaramoorthy, S.2
  • 34
    • 34447291354 scopus 로고    scopus 로고
    • Anthrax toxin: receptor binding, internalization, pore formation, and translocation
    • Young J.A., and Collier R.J. Anthrax toxin: receptor binding, internalization, pore formation, and translocation. Annu. Rev. Biochem. 76 (2007) 243-265
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 243-265
    • Young, J.A.1    Collier, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.