메뉴 건너뛰기




Volumn 287, Issue 30, 2012, Pages 24929-24940

Molecular characteristics of Clostridium perfringens TpeL toxin and consequences of mono-O-GlcNAcylation of Ras in living cells

Author keywords

[No Author keywords available]

Indexed keywords

CLOSTRIDIUM PERFRINGENS; CYSTEINE PROTEASE; ERK ACTIVATION; GLUCOSYLTRANSFERASES; HELA CELL; IN-VITRO; INOSITOL HEXAKISPHOSPHATE; LIVING CELL; MOLECULAR CHARACTERISTICS; PC12 CELLS; PHEOCHROMOCYTOMA; SAKURAI; TARGET CELLS; TOXIN CONCENTRATIONS; UDP-GLUCOSE;

EID: 84864105928     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.347773     Document Type: Article
Times cited : (55)

References (37)
  • 4
    • 0025824660 scopus 로고
    • Molecular genetics and pathogenesis of Clostridium perfringens
    • Rood, J. I., and Cole, S. T. (1991) Molecular genetics and pathogenesis of Clostridium perfringens. Microbiol. Rev. 55, 621-648 (Pubitemid 21895169)
    • (1991) Microbiological Reviews , vol.55 , Issue.4 , pp. 621-648
    • Rood, J.I.1    Cole, S.T.2
  • 5
    • 0031726607 scopus 로고    scopus 로고
    • Virulence genes of Clostridium perfringens
    • Rood, J. I. (1998) Virulence genes of Clostridium perfringens. Annu. Rev. Microbiol. 52, 333-360
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 333-360
    • Rood, J.I.1
  • 6
    • 0033105216 scopus 로고    scopus 로고
    • Clostridium perfringens: Toxinotype and genotype
    • DOI 10.1016/S0966-842X(98)01430-9, PII S0966842X98014309
    • Petit, L., Gibert, M., and Popoff, M. R. (1999) Clostridium perfringens: toxinotype and genotype. Trends Microbiol. 7, 104-110 (Pubitemid 29271996)
    • (1999) Trends in Microbiology , vol.7 , Issue.3 , pp. 104-110
    • Petit, L.1    Gibert, M.2    Popoff, M.R.3
  • 8
    • 34247229774 scopus 로고    scopus 로고
    • A novel toxin homologous to large clostridial cytotoxins found in culture supernatant of Clostridium perfringens type C
    • DOI 10.1099/mic.0.2006/002287-0
    • Amimoto, K., Noro, T., Oishi, E., and Shimizu, M. (2007) A novel toxin homologous to large clostridial cytotoxins found in culture supernatant of Clostridium perfringens type C. Microbiology 153, 1198-1206 (Pubitemid 46605818)
    • (2007) Microbiology , vol.153 , Issue.4 , pp. 1198-1206
    • Amimoto, K.1    Noro, T.2    Oishi, E.3    Shimizu, M.4
  • 9
    • 33947260554 scopus 로고    scopus 로고
    • Rho-glucosylating Clostridium difficile toxins A and B: New insights into structure and function
    • DOI 10.1093/glycob/cwm004
    • Jank, T., Giesemann, T., and Aktories, K. (2007) Rho-glucosylating Clostridium difficile toxins A and B: new insights into structure and function. Glycobiology 17, 15R-22R (Pubitemid 46432006)
    • (2007) Glycobiology , vol.17 , Issue.4
    • Jank, T.1    Giesemann, T.2    Aktories, K.3
  • 11
    • 17444366186 scopus 로고    scopus 로고
    • Clostridium difficile toxins: Mechanism of action and role in disease
    • DOI 10.1128/CMR.18.2.247-263.2005
    • Voth, D. E., and Ballard, J. D. (2005) Clostridium difficile toxins: mechanism of action and role in disease. Clin. Microbiol. Rev. 18, 247-263 (Pubitemid 40548293)
    • (2005) Clinical Microbiology Reviews , vol.18 , Issue.2 , pp. 247-263
    • Voth, D.E.1    Ballard, J.D.2
  • 12
    • 42749095602 scopus 로고    scopus 로고
    • Structure and mode of action of clostridial glucosylating toxins: The ABCD model
    • Jank, T., and Aktories, K. (2008) Structure and mode of action of clostridial glucosylating toxins: the ABCD model. Trends Microbiol. 16, 222-229
    • (2008) Trends Microbiol. , vol.16 , pp. 222-229
    • Jank, T.1    Aktories, K.2
  • 13
    • 0030891386 scopus 로고    scopus 로고
    • Localization of the glucosyltransferase activity of Clostridium difficile toxin B to the N-terminal part of the holotoxin
    • DOI 10.1074/jbc.272.17.11074
    • Hofmann, F., Busch, C., Prepens, U., Just, I., and Aktories, K. (1997) Localization of the glucosyltransferase activity of Clostridium difficile toxin B to the N-terminal part of the holotoxin. J. Biol. Chem. 272, 11074-11078 (Pubitemid 27184097)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.17 , pp. 11074-11078
    • Hofmann, F.1    Busch, C.2    Prepens, U.3    Just, I.4    Aktories, K.5
  • 14
    • 34548472183 scopus 로고    scopus 로고
    • Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity
    • DOI 10.1074/jbc.M703062200
    • Egerer, M., Giesemann, T., Jank, T., Satchell, K. J., and Aktories, K. (2007) Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity. J. Biol. Chem. 282, 25314-25321 (Pubitemid 47372781)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.35 , pp. 25314-25321
    • Egerer, M.1    Giesemann, T.2    Jank, T.3    Fullner, S.K.J.4    Aktories, K.5
  • 15
    • 0025667927 scopus 로고
    • Clostridium difficile toxin A carries a C-terminal repetitive structure homologous to the carbohydrate binding region of streptococcal glycosyltransferases
    • von Eichel-Streiber, C., and Sauerborn, M. (1990) Clostridium difficile toxin A carries a C-terminal repetitive structure homologous to the carbohydrate binding region of streptococcal glycosyltransferases. Gene 96, 107-113
    • (1990) Gene , vol.96 , pp. 107-113
    • Von Eichel-Streiber, C.1    Sauerborn, M.2
  • 17
    • 79952418425 scopus 로고    scopus 로고
    • Structural determinants for membrane insertion, pore formation and translocation of Clostridium difficile toxin B
    • Genisyuerek, S., Papatheodorou, P., Guttenberg, G., Schubert, R., Benz, R., and Aktories, K. (2011) Structural determinants for membrane insertion, pore formation and translocation of Clostridium difficile toxin B. Mol. Microbiol. 79, 1643-1654
    • (2011) Mol. Microbiol. , vol.79 , pp. 1643-1654
    • Genisyuerek, S.1    Papatheodorou, P.2    Guttenberg, G.3    Schubert, R.4    Benz, R.5    Aktories, K.6
  • 20
    • 0029823945 scopus 로고    scopus 로고
    • Clostridium novyi α-toxin-catalyzed incorporation of GlcNAc into Rho subfamily proteins
    • DOI 10.1074/jbc.271.41.25173
    • Selzer, J., Hofmann, F., Rex, G., Wilm, M., Mann, M., Just, I., and Aktories, K. (1996) Clostridium novyi α-toxin-catalyzed incorporation of GlcNAc into Rho subfamily proteins. J. Biol. Chem. 271, 25173-25177 (Pubitemid 26337878)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.41 , pp. 25173-25177
    • Selzer, J.1    Hofmann, F.2    Rex, G.3    Wilm, M.4    Mann, M.5    Just, I.6    Aktories, K.7
  • 22
    • 0029925007 scopus 로고    scopus 로고
    • Inactivation of Ras by Clostridium sordellii lethal toxin-catalyzed glucosylation
    • DOI 10.1074/jbc.271.17.10149
    • Just, I., Selzer, J., Hofmann, F., Green, G. A., and Aktories, K. (1996) Inactivation of Ras by Clostridium sordellii lethal toxin-catalyzed glucosylation. J. Biol. Chem. 271, 10149-10153 (Pubitemid 26131577)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.17 , pp. 10149-10153
    • Just, I.1    Selzer, J.2    Hofmann, F.3    Green, G.A.4    Aktories, K.5
  • 24
    • 64349095054 scopus 로고    scopus 로고
    • Killing of rat basophilic leukemia cells by lethal toxin from Clostridium sordellii: Critical role of phosphatidylinositide 3′-OH kinase/Akt signaling
    • Dreger, S. C., Schulz, F., Huelsenbeck, J., Gerhard, R., Hofmann, F., Just, I., and Genth, H. (2009) Killing of rat basophilic leukemia cells by lethal toxin from Clostridium sordellii: critical role of phosphatidylinositide 3′-OH kinase/Akt signaling. Biochemistry 48, 1785-1792
    • (2009) Biochemistry , vol.48 , pp. 1785-1792
    • Dreger, S.C.1    Schulz, F.2    Huelsenbeck, J.3    Gerhard, R.4    Hofmann, F.5    Just, I.6    Genth, H.7
  • 25
    • 27844548024 scopus 로고    scopus 로고
    • Change of the donor substrate specificity of clostridium difficile toxin B by site-directed mutagenesis
    • DOI 10.1074/jbc.M506836200
    • Jank, T., Reinert, D. J., Giesemann, T., Schulz, G. E., and Aktories, K. (2005) Change of the donor substrate specificity of Clostridium difficile toxin B by site-directed mutagenesis. J. Biol. Chem. 280, 37833-37838 (Pubitemid 41642394)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.45 , pp. 37833-37838
    • Jank, T.1    Reinert, D.J.2    Giesemann, T.3    Schulz, G.E.4    Aktories, K.5
  • 26
    • 23644460027 scopus 로고    scopus 로고
    • Structural basis for the function of Clostridium difficile toxin B
    • DOI 10.1016/j.jmb.2005.06.071, PII S0022283605007552
    • Reinert, D. J., Jank, T., Aktories, K., and Schulz, G. E. (2005) Structural basis for the function of Clostridium difficile toxin B. J. Mol. Biol. 351, 973-981 (Pubitemid 41133445)
    • (2005) Journal of Molecular Biology , vol.351 , Issue.5 , pp. 973-981
    • Reinert, D.J.1    Jank, T.2    Aktories, K.3    Schulz, G.E.4
  • 28
    • 56649108115 scopus 로고    scopus 로고
    • Expression of recombinant Clostridium difficile toxin A and B in Bacillus megaterium
    • Yang, G., Zhou, B., Wang, J., He, X., Sun, X., Nie, W., Tzipori, S., and Feng, H. (2008) Expression of recombinant Clostridium difficile toxin A and B in Bacillus megaterium. BMC. Microbiol. 8, 192
    • (2008) BMC. Microbiol. , vol.8 , pp. 192
    • Yang, G.1    Zhou, B.2    Wang, J.3    He, X.4    Sun, X.5    Nie, W.6    Tzipori, S.7    Feng, H.8
  • 29
    • 77957667396 scopus 로고    scopus 로고
    • Inositol hexakisphosphate-induced autoprocessing of large bacterial protein toxins
    • Egerer, M., and Satchell, K. J. (2010) Inositol hexakisphosphate-induced autoprocessing of large bacterial protein toxins. PLoS. Pathog. 6, e1000942
    • (2010) PLoS. Pathog. , vol.6
    • Egerer, M.1    Satchell, K.J.2
  • 30
    • 79955414006 scopus 로고    scopus 로고
    • Inositol hexakisphosphate-dependent processing of Clostridium sordellii lethal toxin and Clostridium novyi α-toxin
    • Guttenberg, G., Papatheodorou, P., Genisyuerek, S., Lü, W., Jank, T., Einsle, O., and Aktories, K. (2011) Inositol hexakisphosphate-dependent processing of Clostridium sordellii lethal toxin and Clostridium novyi α-toxin. J. Biol. Chem. 286, 14779-14786
    • (2011) J. Biol. Chem. , vol.286 , pp. 14779-14786
    • Guttenberg, G.1    Papatheodorou, P.2    Genisyuerek, S.3    Lü, W.4    Jank, T.5    Einsle, O.6    Aktories, K.7
  • 31
  • 32
    • 0037205044 scopus 로고    scopus 로고
    • Signaling pathways for PC12 cell differentiation: Making the right connections
    • DOI 10.1126/science.1071552
    • Vaudry, D., Stork, P. J., Lazarovici, P., and Eiden, L. E. (2002) Signaling pathways for PC12 cell differentiation: making the right connections. Science 296, 1648-1649 (Pubitemid 34579153)
    • (2002) Science , vol.296 , Issue.5573 , pp. 1648-1649
    • Vaudry, D.1    Stork, P.J.S.2    Lazarovici, P.3    Eiden, L.E.4
  • 34
    • 0242414631 scopus 로고    scopus 로고
    • Cellular uptake of Clostridium difficile toxin B. Translocation of the N-terminal catalytic domain into the cytosol of eukaryotic cells
    • DOI 10.1074/jbc.M307540200
    • Pfeifer, G., Schirmer, J., Leemhuis, J., Busch, C., Meyer, D. K., Aktories, K., and Barth, H. (2003) Cellular uptake of Clostridium difficile toxin B. Translocation of the N-terminal catalytic domain into the cytosol of eukaryotic cells. J. Biol. Chem. 278, 44535-44541 (Pubitemid 37377206)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.45 , pp. 44535-44541
    • Pfeifer, G.1    Schirmer, J.2    Leemhuis, J.3    Busch, C.4    Meyer, D.K.5    Aktories, K.6    Barth, H.7
  • 35
    • 0032584665 scopus 로고    scopus 로고
    • A common motif of eukaryotic glycosyltransferases is essential for the enzyme activity of large clostridial cytotoxins
    • DOI 10.1074/jbc.273.31.19566
    • Busch, C., Hofmann, F., Selzer, J., Munro, S., Jeckel, D., and Aktories, K. (1998) A common motif of eukaryotic glycosyltransferases is essential for the enzyme activity of large clostridial cytotoxins. J. Biol. Chem. 273, 19566-19572 (Pubitemid 28367010)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.31 , pp. 19566-19572
    • Busch, C.1    Hofmann, F.2    Selzer, J.3    Munro, S.4    Jeckel, D.5    Aktories, K.6
  • 36
    • 70349451546 scopus 로고    scopus 로고
    • Distinct kinetics of (H/K/N)Ras glucosylation and Rac1 glucosylation catalyzed by Clostridium sordellii lethal toxin
    • Huelsenbeck, S. C., Klose, I., Reichenbach, M., Huelsenbeck, J., and Genth, H. (2009) Distinct kinetics of (H/K/N)Ras glucosylation and Rac1 glucosylation catalyzed by Clostridium sordellii lethal toxin. FEBS Lett. 583, 3133-3139
    • (2009) FEBS Lett. , vol.583 , pp. 3133-3139
    • Huelsenbeck, S.C.1    Klose, I.2    Reichenbach, M.3    Huelsenbeck, J.4    Genth, H.5
  • 37
    • 80052681298 scopus 로고    scopus 로고
    • Functional implications of lethal toxin-catalysed glucosylation of (H/K/N)Ras and Rac1 in Clostridium sordellii-associated disease
    • Genth, H., and Just, I. (2011) Functional implications of lethal toxin-catalysed glucosylation of (H/K/N)Ras and Rac1 in Clostridium sordellii-associated disease. Eur. J. Cell Biol. 90, 959-965
    • (2011) Eur. J. Cell Biol. , vol.90 , pp. 959-965
    • Genth, H.1    Just, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.