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Volumn 10, Issue 1, 2009, Pages

Ser170 of Bacillus thuringiensis Cry1Ab -endotoxin becomes anchored in a hydrophobic moiety upon insertion of this protein into Manduca sexta brush border membranes

Author keywords

[No Author keywords available]

Indexed keywords

CRY1AB DELTA ENDOTOXIN; CRY1AB TOXIN; LEUCINE; MUTANT PROTEIN; SERINE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; ENDOTOXIN; HEMOLYSIN; INSECTICIDAL CRYSTAL PROTEIN, BACILLUS THURINGIENSIS; ION;

EID: 70449432621     PISSN: None     EISSN: 14712091     Source Type: Journal    
DOI: 10.1186/1471-2091-10-25     Document Type: Article
Times cited : (10)

References (27)
  • 2
    • 4244144005 scopus 로고
    • The crystal -endotoxins of Bacillus thuringiensis: Models for their mechanism of action on the insect gut
    • 10.1002/bies.950150706
    • The crystal -endotoxins of Bacillus thuringiensis: models for their mechanism of action on the insect gut. BH Knowles JAT Dow, BioEssays 1993 15 469 476 10.1002/bies.950150706
    • (1993) BioEssays , vol.15 , pp. 469-476
    • Knowles, B.H.1    Dow, J.A.T.2
  • 3
    • 0030785699 scopus 로고    scopus 로고
    • Restriction of intramolecular movements within the Cry1aA toxin molecule of Bacillus thuringiensis through disulfide bond engineering
    • DOI 10.1016/S0014-5793(97)00626-1, PII S0014579397006261
    • Restriction of intramolecular movements within the CrylAa toxin molecule of Bacillus thuringiensis through disulfide bond engineering. JL Schwartz M Juteau P Grochulski M Cygler G Préfontaine R Brousseau L Masson, FEBS Letts 1997 410 397 402 10.1016/S0014-5793(97)00626-1 (Pubitemid 27304104)
    • (1997) FEBS Letters , vol.410 , Issue.2-3 , pp. 397-402
    • Schwartz, J.-L.1    Juteau, M.2    Grochulski, P.3    Cygler, M.4    Prefontaine, G.5    Brousseau, R.6    Masson, L.7
  • 4
    • 0029619216 scopus 로고
    • Bacillus thuringiensis CryIA(a) insecticidal toxin: Crystal structure and channel formation
    • 10.1006/jmbi.1995.0630. 7490762
    • Bacillus thuringiensis CryIA(a) insecticidal toxin: crystal structure and channel formation. P Grochulski L Masson S Borisova M Pusztai-Carey JL Schwartz R Brousseau M Cygler, J Mol Biol 1995 254 447 464 10.1006/jmbi.1995.0630 7490762
    • (1995) J Mol Biol , vol.254 , pp. 447-464
    • Grochulski, P.1    Masson, L.2    Borisova, S.3    Pusztai-Carey, M.4    Schwartz, J.L.5    Brousseau, R.6    Cygler, M.7
  • 5
    • 0026050639 scopus 로고
    • Crystal structure of insecticidal -endotoxin from Bacillus thuringiensis at 2.5 resolution
    • 10.1038/353815a0. 1658659
    • Crystal structure of insecticidal -endotoxin from Bacillus thuringiensis at 2.5 resolution. J Li J Carroll DJ Ellar, Nature 1991 353 815 821 10.1038/353815a0 1658659
    • (1991) Nature , vol.353 , pp. 815-821
    • Li, J.1    Carroll, J.2    Ellar, D.J.3
  • 6
    • 0035957098 scopus 로고    scopus 로고
    • Role of -Helix Seven of Bacillus thuringiensis Cry1Ab -Endotoxin in Membrane Insertion, Structural Stability, and Ion Channel Activity
    • 10.1021/bi0022240. 11327876
    • Role of -Helix Seven of Bacillus thuringiensis Cry1Ab -Endotoxin in Membrane Insertion, Structural Stability, and Ion Channel Activity. EP Alcantara O Alzate MK Lee A Curtiss DH Dean, Biochemistry 2001 40 2540 2547 10.1021/bi0022240 11327876
    • (2001) Biochemistry , vol.40 , pp. 2540-2547
    • Alcantara, E.P.1    Alzate, O.2    Lee, M.K.3    Curtiss, A.4    Dean, D.H.5
  • 8
    • 0040358826 scopus 로고    scopus 로고
    • Bivalent sequential binding model of a Bacillus thuringiensis toxin to gypsy moth aminopeptidase N receptor
    • 10.1074/jbc.275.19.14423. 10799525
    • Bivalent sequential binding model of a Bacillus thuringiensis toxin to gypsy moth aminopeptidase N receptor. JL Jenkins MK Lee AP Valaitis A Curtiss DH Dean, J Biol Chem 2000 275 14423 14431 10.1074/jbc.275.19.14423 10799525
    • (2000) J Biol Chem , vol.275 , pp. 14423-14431
    • Jenkins, J.L.1    Lee, M.K.2    Valaitis, A.P.3    Curtiss, A.4    Dean, D.H.5
  • 9
    • 0029007022 scopus 로고
    • Single amino acid changes in domain II of Bacillus thuringiensis CryIAb -endotoxin affect irreversible binding to Manduca sexta midgut membrane vesicles
    • 7730254
    • Single amino acid changes in domain II of Bacillus thuringiensis CryIAb -endotoxin affect irreversible binding to Manduca sexta midgut membrane vesicles. F Rajamohan E Alcantara MK Lee XJ Chen A Curtiss DH Dean, J Bacteriol 1995 177 2276 2282 7730254
    • (1995) J Bacteriol , vol.177 , pp. 2276-2282
    • Rajamohan, F.1    Alcantara, E.2    Lee, M.K.3    Chen, X.J.4    Curtiss, A.5    Dean, D.H.6
  • 10
    • 0029141222 scopus 로고
    • Bacillus thuringiensis -endotoxin and larval Manduca sexta midgut brush-border membrane vesicles act synergistically to cause very large increases in the conductance of planar lipid bilayers
    • Bacillus thuringiensis -endotoxin and larval Manduca sexta midgut brush-border membrane vesicles act synergistically to cause very large increases in the conductance of planar lipid bilayers. FG Martin MG Wolfersberger, J Exper Biol 1995 198 91 96
    • (1995) J Exper Biol , vol.198 , pp. 91-96
    • Martin, F.G.1    Wolfersberger, M.G.2
  • 11
    • 0025361875 scopus 로고
    • Delta-endotoxins form cation-selective channels in planar lipid bilayers
    • 10.1016/0006-291X(90)90397-6. 1694077
    • Delta-endotoxins form cation-selective channels in planar lipid bilayers. SL Slatin CK Abrams L English, Biochem Biophys Res Commun 1990 169 765 772 10.1016/0006-291X(90)90397-6 1694077
    • (1990) Biochem Biophys Res Commun , vol.169 , pp. 765-772
    • Slatin, S.L.1    Abrams, C.K.2    English, L.3
  • 12
    • 0032514753 scopus 로고    scopus 로고
    • The structure and organization within the membrane of the helices composing the pore-forming domain of Bacillus thuringien sis -endotoxin are consistent with an "umbrella like" structure of the pore
    • 10.1073/pnas.95.21.12289. 9770479
    • The structure and organization within the membrane of the helices composing the pore-forming domain of Bacillus thuringien sis -endotoxin are consistent with an "umbrella like" structure of the pore. E Gazit PL Rocca MSP Sansom Y Shai, Proc Natl Acad Sci USA 1998 95 12289 12294 10.1073/pnas.95.21.12289 9770479
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12289-12294
    • Gazit, E.1    Rocca, P.L.2    Sansom, M.S.P.3    Shai, Y.4
  • 13
    • 0028984252 scopus 로고
    • The assembly and organization of the 5 and 7 helices from the pore-forming domain of Bacillus thuringiensis -endotoxin
    • 10.1074/jbc.270.6.2571. 7852320
    • The assembly and organization of the 5 and 7 helices from the pore-forming domain of Bacillus thuringiensis -endotoxin. E Gazit Y Shai, J Biol Chem 1995 270 2571 2578 10.1074/jbc.270.6.2571 7852320
    • (1995) J Biol Chem , vol.270 , pp. 2571-2578
    • Gazit, E.1    Shai, Y.2
  • 14
    • 0035830707 scopus 로고    scopus 로고
    • The role of a proline-induced broken-helix motif in -helix 2 of Bacillus thuringiensis -endotoxins
    • 10.1016/S0014-5793(01)02139-1. 11172813
    • The role of a proline-induced broken-helix motif in -helix 2 of Bacillus thuringiensis -endotoxins. S Arnold A Curtiss DH Dean O Alzate, FEBS Letters 2001 490 70 74 10.1016/S0014-5793(01)02139-1 11172813
    • (2001) FEBS Letters , vol.490 , pp. 70-74
    • Arnold, S.1    Curtiss, A.2    Dean, D.H.3    Alzate, O.4
  • 15
    • 0033774892 scopus 로고    scopus 로고
    • Incorporation of protease K into larval insect membrane vesicles does not result in disruption of integrity or function of the pore-forming Bacillus thuringiensis -endotoxin
    • 10.1128/AEM.66.10.4568-4570.2000. 11010919
    • Incorporation of protease K into larval insect membrane vesicles does not result in disruption of integrity or function of the pore-forming Bacillus thuringiensis -endotoxin. A Aronson, Appl Environ Microbiol 2000 66 4568 4570 10.1128/AEM.66.10.4568-4570.2000 11010919
    • (2000) Appl Environ Microbiol , vol.66 , pp. 4568-4570
    • Aronson, A.1
  • 16
    • 0032976138 scopus 로고    scopus 로고
    • Aggregation of Bacillus thuringiensis Cry1A toxins upon binding to target insect larval midgut vesicles
    • 10347034
    • Aggregation of Bacillus thuringiensis Cry1A toxins upon binding to target insect larval midgut vesicles. AI Aronson C Geng L Wu, Appl Environ Microbiol 1999 65 2503 2507 10347034
    • (1999) Appl Environ Microbiol , vol.65 , pp. 2503-2507
    • Aronson, A.I.1    Geng, C.2    Wu, L.3
  • 17
    • 0013646256 scopus 로고
    • Mode of action of -endotoxin from Bacillus thuringiensis var. aizawai
    • Washington, D. C: American Chemical Society Clark JM
    • Mode of action of -endotoxin from Bacillus thuringiensis var. aizawai. M Himeno H Ihara, Molecular Action of Insecticides on Ion Channels Washington, D. C: American Chemical Society, Clark JM, 1995
    • (1995) Molecular Action of Insecticides on Ion Channels
    • Himeno, M.1    Ihara, H.2
  • 18
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • 10.1038/78956. 10966640
    • Identifying conformational changes with site-directed spin labeling. WL Hubbell DS Cafiso C Altenbach, Nat Struct Biol 2000 7 735 739 10.1038/78956 10966640
    • (2000) Nat Struct Biol , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 20
    • 0024974071 scopus 로고
    • Structural studies on transmembrane proteins. 2. Spin labeling of bacteriorhodopsin mutants at unique cysteines
    • 10.1021/bi00445a042. 2558712
    • Structural studies on transmembrane proteins. 2. Spin labeling of bacteriorhodopsin mutants at unique cysteines. C Altenbach SL Flitsch HG Khorana WL Hubbell, Biochemistry 1989 28 7806 7812 10.1021/bi00445a042 2558712
    • (1989) Biochemistry , vol.28 , pp. 7806-7812
    • Altenbach, C.1    Flitsch, S.L.2    Khorana, H.G.3    Hubbell, W.L.4
  • 21
    • 0028346566 scopus 로고
    • A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: Application to spin-labeled mutants of bacteriorhodopsin
    • 10.1073/pnas.91.5.1667. 8127863
    • A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: application to spin-labeled mutants of bacteriorhodopsin. C Altenbach DA Greenhalgh HG Khorana WL Hubbell, Proc Natl Acad Sci USA 1994 91 1667 1671 10.1073/pnas.91.5.1667 8127863
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1667-1671
    • Altenbach, C.1    Greenhalgh, D.A.2    Khorana, H.G.3    Hubbell, W.L.4
  • 23
    • 0000704357 scopus 로고    scopus 로고
    • Conformation of the diphtheria toxin T domain in membranes: A site-directed spin labeling study of the TH8 helix and TL5 loop
    • 10.1021/bi990520a. 10441127
    • Conformation of the diphtheria toxin T domain in membranes: a site-directed spin labeling study of the TH8 helix and TL5 loop. KJ Oh H Zhan C Cui C Altenbach WL Hubbell RJ Collier, Biochemistry 1999 38 10336 10343 10.1021/bi990520a 10441127
    • (1999) Biochemistry , vol.38 , pp. 10336-10343
    • Oh, K.J.1    Zhan, H.2    Cui, C.3    Altenbach, C.4    Hubbell, W.L.5    Collier, R.J.6
  • 24
    • 0033527563 scopus 로고    scopus 로고
    • Helix 4 of the Bacillus thuringiensis Cry1Aa toxin lines the lumen of the ion channel
    • 10.1074/jbc.274.45.31996. 10542230
    • Helix 4 of the Bacillus thuringiensis Cry1Aa toxin lines the lumen of the ion channel. L Masson BE Tabashnik YB Liu R Brousseau JL Schwartz, J Biol Chem 1999 274 31996 32000 10.1074/jbc.274.45.31996 10542230
    • (1999) J Biol Chem , vol.274 , pp. 31996-32000
    • Masson, L.1    Tabashnik, B.E.2    Liu, Y.B.3    Brousseau, R.4    Schwartz, J.L.5
  • 26
    • 33751008673 scopus 로고    scopus 로고
    • Effects of disulfide bridges in domain i of Bacillus thuringiensis Cry1Aa -endotoxin on ion-channel formation in biological membranes
    • 10.1021/bi061474z. 17087513
    • Effects of disulfide bridges in domain I of Bacillus thuringiensis Cry1Aa -endotoxin on ion-channel formation in biological membranes. O Alzate T You M Claybon C Osorio A Curtiss DH Dean, Biochemistry 2006 45 13597 13605 10.1021/bi061474z 17087513
    • (2006) Biochemistry , vol.45 , pp. 13597-13605
    • Alzate, O.1    You, T.2    Claybon, M.3    Osorio, C.4    Curtiss, A.5    Dean, D.H.6
  • 27
    • 0025613473 scopus 로고
    • Isolation, voltage clamping, and flux measurements in lepidopteran midgut
    • Isolation, voltage clamping, and flux measurements in lepidopteran midgut. WR Harvey DN Crawford DD Spaeth, Methods in Enzymology 1990 192 599 608
    • (1990) Methods in Enzymology , vol.192 , pp. 599-608
    • Harvey, W.R.1    Crawford, D.N.2    Spaeth, D.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.