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Volumn 44, Issue 11, 2005, Pages 4488-4498

Behavior of diphtheria toxin T domain containing substitutions that block normal membrane insertion at Pro345 and Leu307: Control of deep membrane insertion and coupling between deep insertion of hydrophobic subdomains

(2)  Zhao, Gang a   London, Erwin a  

a NONE

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENCE; HYDROPHOBICITY; LIPIDS; SUBSTITUTION REACTIONS; TOXICITY;

EID: 15544385169     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047705o     Document Type: Article
Times cited : (31)

References (46)
  • 2
    • 0028077637 scopus 로고
    • Refined structure of dimeric diphtheria toxin at 2.0 Å resolution
    • Bennett, M. J., Choe, S., and Eisenberg, D. (1994) Refined structure of dimeric diphtheria toxin at 2.0 Å resolution, Protein Sci. 3, 1444-1463.
    • (1994) Protein Sci. , vol.3 , pp. 1444-1463
    • Bennett, M.J.1    Choe, S.2    Eisenberg, D.3
  • 3
    • 0028908353 scopus 로고
    • Interaction of the isolated transmembrane domain of diphtheria toxin with membranes
    • Zhan, H., Oh, K. J., Shin, Y. K., Hubbell, W. L., and Collier, R. J. (1995) Interaction of the isolated transmembrane domain of diphtheria toxin with membranes, Biochemistry 34, 4856-4863.
    • (1995) Biochemistry , vol.34 , pp. 4856-4863
    • Zhan, H.1    Oh, K.J.2    Shin, Y.K.3    Hubbell, W.L.4    Collier, R.J.5
  • 4
    • 0030803672 scopus 로고    scopus 로고
    • Identification of shallow and deep membrane-penetrating forms of diphtheria toxin T domain that are regulated by protein concentration and bilayer width
    • Wang, Y., Malenbaum, S. E., Kachel, K., Zhan, H., Collier, R. J., and London, E. (1997) Identification of shallow and deep membrane-penetrating forms of diphtheria toxin T domain that are regulated by protein concentration and bilayer width, J. Biol. Chem. 272, 25091-25098.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25091-25098
    • Wang, Y.1    Malenbaum, S.E.2    Kachel, K.3    Zhan, H.4    Collier, R.J.5    London, E.6
  • 5
    • 0034878448 scopus 로고    scopus 로고
    • Understanding the mode of action of diphtheria toxin: A perspective on progress during the 20th century
    • Collier, R. J. (2001) Understanding the mode of action of diphtheria toxin: A perspective on progress during the 20th century, Toxicon 39, 1793-1803.
    • (2001) Toxicon , vol.39 , pp. 1793-1803
    • Collier, R.J.1
  • 6
    • 0025737882 scopus 로고
    • Insertion of diphtheria toxin B-fragment into the plasma membrane at low pH. Characterization and topology of inserted regions
    • Moskaug, J. O., Stenmark, H., and Olsnes, S. (1991) Insertion of diphtheria toxin B-fragment into the plasma membrane at low pH. Characterization and topology of inserted regions, J. Biol. Chem. 266, 2652-2659.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2652-2659
    • Moskaug, J.O.1    Stenmark, H.2    Olsnes, S.3
  • 7
    • 0345668477 scopus 로고    scopus 로고
    • The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex
    • Ratts, R., Zeng, H., Berg, E. A., Blue, C., McComb, M. E., Costello, C. E., vanderSpek, J. C., and Murphy, J. R. (2003) The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex, J. Cell Biol. 160, 1139-1150.
    • (2003) J. Cell Biol. , vol.160 , pp. 1139-1150
    • Ratts, R.1    Zeng, H.2    Berg, E.A.3    Blue, C.4    McComb, M.E.5    Costello, C.E.6    VanderSpek, J.C.7    Murphy, J.R.8
  • 8
    • 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
    • Oh, K. J., Zhan, H., Cui, C., Altenbach, C., Hubbell, W. L., and Collier, R. J. (1999) Conformation of the diphtheria toxin T domain in membranes; A site-directed spin-labeling study of the TH8 helix and TL5 loop, Biochemistry 38, 10336-10343.
    • (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
  • 9
    • 0033735495 scopus 로고    scopus 로고
    • The diphtheria toxin channel-forming T-domain translocates its own NH2-terminal region and the catalytic domain across planar phospholipid bilayers
    • Finkelstein, A., Oh, K. J., Senzel, L., Gordon, M., Blaustein, R. O., and Collier, R. J. (2000) The diphtheria toxin channel-forming T-domain translocates its own NH2-terminal region and the catalytic domain across planar phospholipid bilayers, Int. J. Med. Microbiol. 290, 435-440.
    • (2000) Int. J. Med. Microbiol. , vol.290 , pp. 435-440
    • Finkelstein, A.1    Oh, K.J.2    Senzel, L.3    Gordon, M.4    Blaustein, R.O.5    Collier, R.J.6
  • 11
    • 0031714548 scopus 로고    scopus 로고
    • The diphtheria toxin channel-forming T domain translocates its own NH2-terminal region across planar bilayers
    • Senzel, L., Huynh, P. D., Jakes, K. S., Collier, R. J., and Finkelstein, A. (1998) The diphtheria toxin channel-forming T domain translocates its own NH2-terminal region across planar bilayers, J. Gen. Physiol. 112, 317-324.
    • (1998) J. Gen. Physiol. , vol.112 , pp. 317-324
    • Senzel, L.1    Huynh, P.D.2    Jakes, K.S.3    Collier, R.J.4    Finkelstein, A.5
  • 12
    • 0030900233 scopus 로고    scopus 로고
    • Structure-function relationship of the ion channel formed by diphtheria toxin in vero cell membranes
    • Lanzrein, M., Falnes, P. O., Sand, O., and Olsnes, S. (1997) Structure-function relationship of the ion channel formed by diphtheria toxin in vero cell membranes, J. Membr. Biol. 156, 141-148.
    • (1997) J. Membr. Biol. , vol.156 , pp. 141-148
    • Lanzrein, M.1    Falnes, P.O.2    Sand, O.3    Olsnes, S.4
  • 13
    • 0033532355 scopus 로고    scopus 로고
    • Interaction of diphtheria toxin T domain with molten globule-like proteins and its implications for translocation
    • Ren, J., Kachel, K., Kim, H., Malenbaum, S. E., Collier, R. J., and London, E. (1999) Interaction of diphtheria toxin T domain with molten globule-like proteins and its implications for translocation, Science 284, 955-957.
    • (1999) Science , vol.284 , pp. 955-957
    • Ren, J.1    Kachel, K.2    Kim, H.3    Malenbaum, S.E.4    Collier, R.J.5    London, E.6
  • 14
    • 0031719786 scopus 로고    scopus 로고
    • The effects of helix breaking mutations in the diphtheria toxin transmembrane domain helix layers of the fusion toxin DAB389IL-2
    • Hu, H. Y., Huynh, P. D., Murphy, J. R., and vanderSpek, J. C. (1998) The effects of helix breaking mutations in the diphtheria toxin transmembrane domain helix layers of the fusion toxin DAB389IL-2, Protein Eng. 11, 811-817.
    • (1998) Protein Eng. , vol.11 , pp. 811-817
    • Hu, H.Y.1    Huynh, P.D.2    Murphy, J.R.3    VanderSpek, J.C.4
  • 15
    • 0027222607 scopus 로고
    • Membrane translocation and channel-forming activities of diphtheria toxin are blocked by replacing isoleucine 364 with lysine
    • Cabiaux, V., Mindell, J., and Collier, R. J. (1993) Membrane translocation and channel-forming activities of diphtheria toxin are blocked by replacing isoleucine 364 with lysine, Infect. Immun. 61, 2200-2202.
    • (1993) Infect. Immun. , vol.61 , pp. 2200-2202
    • Cabiaux, V.1    Mindell, J.2    Collier, R.J.3
  • 16
    • 0026752616 scopus 로고
    • Replacement of negative by positive charges in the presumed membrane-inserted part of diphtheria toxin B fragment. Effect on membrane translocation and on formation of cation channels
    • Falnes, P. O., Madshus, I. H., Sandvig, K., and Olsnes, S. (1992) Replacement of negative by positive charges in the presumed membrane-inserted part of diphtheria toxin B fragment. Effect on membrane translocation and on formation of cation channels, J. Biol. Chem. 267, 12284-12290.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12284-12290
    • Falnes, P.O.1    Madshus, I.H.2    Sandvig, K.3    Olsnes, S.4
  • 17
    • 0027478576 scopus 로고
    • The role of proline 345 in diphtheria toxin translocation
    • Johnson, V. G., Nicholls, P. J., Habig, W. H., and Youle, R. J. (1993) The role of proline 345 in diphtheria toxin translocation, J. Biol. Chem. 268, 3514-3519.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3514-3519
    • Johnson, V.G.1    Nicholls, P.J.2    Habig, W.H.3    Youle, R.J.4
  • 18
    • 0027989890 scopus 로고
    • Mutational analysis of the helical hairpin region of diphtheria toxin transmembrane domain
    • Silverman, J. A., Mindell, J. A., Finkelstein, A., Shen, W. H., and Collier, R. J. (1994) Mutational analysis of the helical hairpin region of diphtheria toxin transmembrane domain, J. Biol. Chem. 269, 22524-22532.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22524-22532
    • Silverman, J.A.1    Mindell, J.A.2    Finkelstein, A.3    Shen, W.H.4    Collier, R.J.5
  • 19
    • 0032939820 scopus 로고    scopus 로고
    • Effects of mutations in proline 345 on insertion of diphtheria toxin into model membranes
    • Zhan, H., Elliott, J. L., Shen, W. H., Huynh, P. D., Finkelstein, A., and Collier, R. J. (1999) Effects of mutations in proline 345 on insertion of diphtheria toxin into model membranes, J. Membr. Biol. 167, 173-181.
    • (1999) J. Membr. Biol. , vol.167 , pp. 173-181
    • Zhan, H.1    Elliott, J.L.2    Shen, W.H.3    Huynh, P.D.4    Finkelstein, A.5    Collier, R.J.6
  • 21
    • 0028001091 scopus 로고
    • Intermediates in translocation of diphtheria toxin across the plasma membrane
    • Madshus, I. H., Wiedlocha, A., and Sandvig, K. (1994) Intermediates in translocation of diphtheria toxin across the plasma membrane, J. Biol. Chem. 269, 4648-4652.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4648-4652
    • Madshus, I.H.1    Wiedlocha, A.2    Sandvig, K.3
  • 22
    • 0028235219 scopus 로고
    • Reaction of diphtheria toxin channels with sulfhydryl-specific reagents: Observation of chemical reactions at the single molecule level
    • Mindell, J. A., Zhan, H., Huynh, P. D., Collier, R. J., and Finkelstein, A. (1994) Reaction of diphtheria toxin channels with sulfhydryl-specific reagents: Observation of chemical reactions at the single molecule level, Proc. Natl. Acad. Sci. U.S.A. 91, 5272-5276.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 5272-5276
    • Mindell, J.A.1    Zhan, H.2    Huynh, P.D.3    Collier, R.J.4    Finkelstein, A.5
  • 23
    • 0028144832 scopus 로고
    • Dynamic transitions of the transmembrane domain of diphtheria toxin: Bisulfide trapping and fluorescence proximity studies
    • Zhan, H., Choe, S., Huynh, P. D., Finkelstein, A., Eisenberg, D., and Collier, R. J. (1994) Dynamic transitions of the transmembrane domain of diphtheria toxin: Bisulfide trapping and fluorescence proximity studies, Biochemistry 33, 11254-11263.
    • (1994) Biochemistry , vol.33 , pp. 11254-11263
    • Zhan, H.1    Choe, S.2    Huynh, P.D.3    Finkelstein, A.4    Eisenberg, D.5    Collier, R.J.6
  • 24
    • 0001350946 scopus 로고    scopus 로고
    • Organization of diphtheria toxin T domain in bilayers: A site-directed spin labeling study
    • Oh, K. J., Zhan, H., Cui, C., Hideg, K., Collier, R. J., and Hubbell, W. L. (1996) Organization of diphtheria toxin T domain in bilayers: A site-directed spin labeling study, Science 273, 810-812.
    • (1996) Science , vol.273 , pp. 810-812
    • Oh, K.J.1    Zhan, H.2    Cui, C.3    Hideg, K.4    Collier, R.J.5    Hubbell, W.L.6
  • 26
    • 0032483451 scopus 로고    scopus 로고
    • Identifying transmembrane states and defining the membrane insertion boundaries of hydrophobic helices in membrane-inserted diphtheria toxin T domain
    • Kachel, K., Ren, J., Collier, R. J., and London, E. (1998) Identifying transmembrane states and defining the membrane insertion boundaries of hydrophobic helices in membrane-inserted diphtheria toxin T domain, J. Biol. Chem. 273, 22950-22956.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22950-22956
    • Kachel, K.1    Ren, J.2    Collier, R.J.3    London, E.4
  • 27
    • 0037053367 scopus 로고    scopus 로고
    • Topography of helices 5-7 in membrane-inserted diphtheria toxin T domain: Identification and insertion boundaries of two hydrophobic sequences that do not form a stable transmembrane hairpin
    • Rosconi, M. P., and London, E. (2002) Topography of helices 5-7 in membrane-inserted diphtheria toxin T domain: Identification and insertion boundaries of two hydrophobic sequences that do not form a stable transmembrane hairpin, J. Biol. Chem. 277, 16517-16527.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16517-16527
    • Rosconi, M.P.1    London, E.2
  • 28
    • 3142667679 scopus 로고    scopus 로고
    • Analyzing topography of membrane-inserted diphtheria toxin T domain using BODIPY-streptavidin: At low pH, helices 8 and 9 form a transmembrane hairpin but helices 5-7 form stable nonclassical inserted segments on the cis side of the bilayer
    • Rosconi, M. P., Zhao, G., and London, E. (2004) Analyzing topography of membrane-inserted diphtheria toxin T domain using BODIPY-streptavidin: At low pH, helices 8 and 9 form a transmembrane hairpin but helices 5-7 form stable nonclassical inserted segments on the cis side of the bilayer, Biochemistry 43, 9127-9139.
    • (2004) Biochemistry , vol.43 , pp. 9127-9139
    • Rosconi, M.P.1    Zhao, G.2    London, E.3
  • 30
    • 0026581661 scopus 로고
    • Refined structure of the pore-forming domain of colicin a at 2.4 Å resolution
    • Parker, M. W., Postma, J. P., Pattus, F., Tucker, A. D., and Tsernoglou, D. (1992) Refined structure of the pore-forming domain of colicin A at 2.4 Å resolution, J. Mol. Biol. 224, 639-657.
    • (1992) J. Mol. Biol. , vol.224 , pp. 639-657
    • Parker, M.W.1    Postma, J.P.2    Pattus, F.3    Tucker, A.D.4    Tsernoglou, D.5
  • 32
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 0037465698 scopus 로고    scopus 로고
    • Using a novel dual fluorescence quenching assay for measurement of tryptophan depth within lipid bilayers to determine hydrophobic α-helix locations within membranes
    • Caputo, G. A., and London, E. (2003) Using a novel dual fluorescence quenching assay for measurement of tryptophan depth within lipid bilayers to determine hydrophobic α-helix locations within membranes, Biochemistry 42, 3265-3274.
    • (2003) Biochemistry , vol.42 , pp. 3265-3274
    • Caputo, G.A.1    London, E.2
  • 34
    • 13544273837 scopus 로고    scopus 로고
    • Topography of diptheria toxin A chain inserted into lipid vesicles
    • Hayashibara, M., and London, E. (2005) Topography of diptheria toxin A chain inserted into lipid vesicles, Biochemistry 44, 2183-2196.
    • (2005) Biochemistry , vol.44 , pp. 2183-2196
    • Hayashibara, M.1    London, E.2
  • 35
    • 0030738720 scopus 로고    scopus 로고
    • Transmembrane orientation of hydrophobic α-helices is regulated both by the relationship of helix length to bilayer thickness and by the cholesterol concentration
    • Ren, J., Lew, S., Wang, Z., and London, E. (1997) Transmembrane orientation of hydrophobic α-helices is regulated both by the relationship of helix length to bilayer thickness and by the cholesterol concentration, Biochemistry 36, 10213-10220.
    • (1997) Biochemistry , vol.36 , pp. 10213-10220
    • Ren, J.1    Lew, S.2    Wang, Z.3    London, E.4
  • 36
    • 0015927357 scopus 로고
    • Single bilayer liposomes prepared without sonication
    • Batzri, S., and Korn, E. D. (1973) Single bilayer liposomes prepared without sonication, Biochim. Biophys. Acta 298, 1015-1019.
    • (1973) Biochim. Biophys. Acta , vol.298 , pp. 1015-1019
    • Batzri, S.1    Korn, E.D.2
  • 37
    • 0026329398 scopus 로고
    • Self-translocation of diphtheria toxin across model membranes
    • Jiang, J. X., Chung, L. A., and London, E. (1991) Self-translocation of diphtheria toxin across model membranes, J. Biol. Chem. 266, 24003-24010.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24003-24010
    • Jiang, J.X.1    Chung, L.A.2    London, E.3
  • 38
    • 0032509153 scopus 로고    scopus 로고
    • Breaking the camel's back: Proline-induced turns in a model transmembrane helix
    • Nilsson, I., and von Heijne, G. (1998) Breaking the camel's back: Proline-induced turns in a model transmembrane helix, J. Mol. Biol. 284, 1185-1189.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1185-1189
    • Nilsson, I.1    Von Heijne, G.2
  • 39
    • 0033527670 scopus 로고    scopus 로고
    • Turns in transmembrane helices: Determination of the minimal length of a "helical hairpin" and derivation of a fine-grained turn propensity scale
    • Monne, M., Nilsson, I., Elofsson, A., and von Heijne, G. (1999) Turns in transmembrane helices: Determination of the minimal length of a "helical hairpin" and derivation of a fine-grained turn propensity scale, J. Mol. Biol. 293, 807-814.
    • (1999) J. Mol. Biol. , vol.293 , pp. 807-814
    • Monne, M.1    Nilsson, I.2    Elofsson, A.3    Von Heijne, G.4
  • 40
    • 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., and Finkelstein, A. (1999) Translocation of the catalytic domain of diphtheria toxin across planar phospholipid bilayers by its own T domain, Proc. Natl. Acad. Sci. U.S.A. 96, 8467-8470.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 8467-8470
    • Oh, K.J.1    Senzel, L.2    Collier, R.J.3    Finkelstein, A.4
  • 41
    • 0028269946 scopus 로고
    • Structure-function relationships in diphtheria toxin channels: I. Determining a minimal channel-forming domain
    • Silverman, J. A., Mindell, J. A., Zhan, H., Finkelstein, A., and Collier, R. J. (1994) Structure-function relationships in diphtheria toxin channels: I. Determining a minimal channel-forming domain, J. Membr. Biol 137, 17-28.
    • (1994) J. Membr. Biol , vol.137 , pp. 17-28
    • Silverman, J.A.1    Mindell, J.A.2    Zhan, H.3    Finkelstein, A.4    Collier, R.J.5
  • 42
    • 0033215457 scopus 로고    scopus 로고
    • Diphtheria toxin forms pores of different sizes depending on its concentration in membranes: Probable relationship to oligomerization
    • Sharpe, J. C., and London, E. (1999) Diphtheria toxin forms pores of different sizes depending on its concentration in membranes: Probable relationship to oligomerization, J. Membr. Biol. 171, 209-221.
    • (1999) J. Membr. Biol. , vol.171 , pp. 209-221
    • Sharpe, J.C.1    London, E.2
  • 43
    • 0028983351 scopus 로고
    • Imaging of endosome fusion in BHK fibroblasts based on a novel fluorimetric avidin-biotin binding assay
    • Emans, N., Biwersi, J., and Verkman, A. S. (1995) Imaging of endosome fusion in BHK fibroblasts based on a novel fluorimetric avidin-biotin binding assay, Biophys. J. 69, 716-728.
    • (1995) Biophys. J. , vol.69 , pp. 716-728
    • Emans, N.1    Biwersi, J.2    Verkman, A.S.3
  • 44
    • 0030886648 scopus 로고    scopus 로고
    • Probing the structure of the diphtheria toxin channel. Reactivity in planar lipid bilayer membranes of cysteine-substituted mutant channels with methanethiosulfonate derivatives
    • Huynh, P. D., Cui, C., Zhan, H., Oh, K. J., Collier, R. J., and Finkelstein, A. (1997) Probing the structure of the diphtheria toxin channel. Reactivity in planar lipid bilayer membranes of cysteine-substituted mutant channels with methanethiosulfonate derivatives, J. Gen. Physiol. 110, 229-242.
    • (1997) J. Gen. Physiol. , vol.110 , pp. 229-242
    • Huynh, P.D.1    Cui, C.2    Zhan, H.3    Oh, K.J.4    Collier, R.J.5    Finkelstein, A.6
  • 45
    • 0028297567 scopus 로고
    • Structure-function relationships in diphtheria toxin channels: III. Residues which affect the cis pH dependence of channel conductance
    • Mindell, J. A., Silverman, J. A., Collier, R. J., and Finkelstein, A. (1994) Structure-function relationships in diphtheria toxin channels: III. Residues which affect the cis pH dependence of channel conductance, J. Membr. Biol 137, 45-57.
    • (1994) J. Membr. Biol , vol.137 , pp. 45-57
    • Mindell, J.A.1    Silverman, J.A.2    Collier, R.J.3    Finkelstein, A.4
  • 46
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein, J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2


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