메뉴 건너뛰기




Volumn 10, Issue 8, 2008, Pages 1687-1694

The diphthamide modification on elongation factor-2 renders mammalian cells resistant to ricin

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; DIPHTHAMIDE; ELONGATION FACTOR 2; RIBOSOME INACTIVATING PROTEIN; RIBOSOME RNA; RICIN;

EID: 47549095879     PISSN: 14625814     EISSN: 14625822     Source Type: Journal    
DOI: 10.1111/j.1462-5822.2008.01159.x     Document Type: Article
Times cited : (18)

References (35)
  • 1
    • 0026741811 scopus 로고
    • Fusions of anthrax toxin lethal factor to the ADP-ribosylation domain of Pseudomonas exotoxin A are potent cytotoxins which are translocated to the cytosol of mammalian cells
    • Arora, N., Klimpel, K.R., Singh, Y., and Leppla, S.H. (1992) Fusions of anthrax toxin lethal factor to the ADP-ribosylation domain of Pseudomonas exotoxin A are potent cytotoxins which are translocated to the cytosol of mammalian cells. J Biol Chem 267: 15542-15548.
    • (1992) J Biol Chem , vol.267 , pp. 15542-15548
    • Arora, N.1    Klimpel, K.R.2    Singh, Y.3    Leppla, S.H.4
  • 3
    • 0021161567 scopus 로고
    • Diphthamide in elongation factor 2: ADP-ribosylation, purification, and properties
    • Bodley, J.W., Dunlop, P.C., and VanNess, B.G. (1984) Diphthamide in elongation factor 2: ADP-ribosylation, purification, and properties. Methods Enzymol 106: 378-387.
    • (1984) Methods Enzymol , vol.106 , pp. 378-387
    • Bodley, J.W.1    Dunlop, P.C.2    VanNess, B.G.3
  • 4
    • 0024589101 scopus 로고
    • Effect of alpha-sarcin and ribosome-inactivating proteins on the interaction of elongation factors with ribosomes
    • Brigotti, M., Rambelli, F., Zamboni, M., Montanaro, L., and Sperti, S. (1989) Effect of alpha-sarcin and ribosome-inactivating proteins on the interaction of elongation factors with ribosomes. Biochem J 257: 723-727.
    • (1989) Biochem , vol.257 , pp. 723-727
    • Brigotti, M.1    Rambelli, F.2    Zamboni, M.3    Montanaro, L.4    Sperti, S.5
  • 5
    • 1042278043 scopus 로고    scopus 로고
    • Ovca1 regulates cell proliferation, embryonic development, and tumorigenesis
    • Chen, C.M., and Behringer, R.R. (2004) Ovca1 regulates cell proliferation, embryonic development, and tumorigenesis. Genes Dev 18: 320-332.
    • (2004) Genes Dev , vol.18 , pp. 320-332
    • Chen, C.M.1    Behringer, R.R.2
  • 6
    • 0023724627 scopus 로고
    • Biosynthesis of diphthamide in Saccharomyces cerevisiae. Partial purification and characterization of a specific S-adenosylmethionine: Elongation factor 2 methyltransferase
    • Chen, J.Y., and Bodley, J.W. (1988) Biosynthesis of diphthamide in Saccharomyces cerevisiae. Partial purification and characterization of a specific S-adenosylmethionine: Elongation factor 2 methyltransferase. J Biol Chem 263: 11692-11696.
    • (1988) J Biol Chem , vol.263 , pp. 11692-11696
    • Chen, J.Y.1    Bodley, J.W.2
  • 7
    • 0022352148 scopus 로고
    • Diphtheria toxin-resistant mutants of Saccharomyces cerevisiae
    • Chen, J.Y., Bodley, J.W., and Livingston, D.M. (1985) Diphtheria toxin-resistant mutants of Saccharomyces cerevisiae. Mol Cell Biol 5: 3357-3360.
    • (1985) Mol Cell Biol , vol.5 , pp. 3357-3360
    • Chen, J.Y.1    Bodley, J.W.2    Livingston, D.M.3
  • 8
    • 0017187578 scopus 로고
    • Protective effect of elongation factor 2 on the inactivation of ribosomes by the toxic lectins abrin and ricin
    • Fernandez-Puentes, C., Benson, S., Olsnes, S., and Pihl, A. (1976) Protective effect of elongation factor 2 on the inactivation of ribosomes by the toxic lectins abrin and ricin. Eur J Biochem 64: 437-443.
    • (1976) Eur J Biochem , vol.64 , pp. 437-443
    • Fernandez-Puentes, C.1    Benson, S.2    Olsnes, S.3    Pihl, A.4
  • 9
    • 0029016976 scopus 로고
    • Pseudomonas exotoxin-mediated selection yields cells with altered expression of low-density lipoprotein receptor-related protein
    • [published erratum appears in J Cell Biol 1995; 130: 1015]
    • FitzGerald, D.J., Fryling, C.M., Zdanovsky, A., Saelinger, C.B., Kounnas, M., Winkles, J.A., et al. (1995) Pseudomonas exotoxin-mediated selection yields cells with altered expression of low-density lipoprotein receptor-related protein. J Cell Biol 129: 1533-1541 [published erratum appears in J Cell Biol 1995; 130: 1015].
    • (1995) J Cell Biol , vol.129 , pp. 1533-1541
    • FitzGerald, D.J.1    Fryling, C.M.2    Zdanovsky, A.3    Saelinger, C.B.4    Kounnas, M.5    Winkles, J.A.6
  • 10
    • 0028609495 scopus 로고
    • Interaction sites of ribosome-bound eukaryotic elongation factor 2 in 18S and 28S rRNA
    • Holmberg, L., and Nygard, O. (1994) Interaction sites of ribosome-bound eukaryotic elongation factor 2 in 18S and 28S rRNA. Biochemistry 33: 15159-15167.
    • (1994) Biochemistry , vol.33 , pp. 15159-15167
    • Holmberg, L.1    Nygard, O.2
  • 11
    • 15444371415 scopus 로고    scopus 로고
    • An early step in wobble uridine tRNA modification requires the Elongator complex
    • Huang, B., Johansson, M.J., and Bystrom, A.S. (2005) An early step in wobble uridine tRNA modification requires the Elongator complex. RNA 11: 424-436.
    • (2005) RNA , vol.11 , pp. 424-436
    • Huang, B.1    Johansson, M.J.2    Bystrom, A.S.3
  • 12
    • 33748142394 scopus 로고    scopus 로고
    • Site-specific mutagenesis of the histidine precursor of diphthamide in the human elongation factor-2 gene confers resistance to diphtheria toxin
    • Ivankovic, M., Rubelj, I., Matulic, M., Reich, E., and Brdar, B. (2006) Site-specific mutagenesis of the histidine precursor of diphthamide in the human elongation factor-2 gene confers resistance to diphtheria toxin. Mutat Res 609: 34-42.
    • (2006) Mutat Res , vol.609 , pp. 34-42
    • Ivankovic, M.1    Rubelj, I.2    Matulic, M.3    Reich, E.4    Brdar, B.5
  • 13
    • 0028241366 scopus 로고
    • Elongation factor 2 mutants deficient in diphthamide formation show temperature-sensitive cell growth
    • Kimata, Y., and Kohno, K. (1994) Elongation factor 2 mutants deficient in diphthamide formation show temperature-sensitive cell growth. J Biol Chem 269: 13497-13501.
    • (1994) J Biol Chem , vol.269 , pp. 13497-13501
    • Kimata, Y.1    Kohno, K.2
  • 14
    • 84882897593 scopus 로고    scopus 로고
    • Bacillus anthracis toxins
    • In Alouf, J.E., and Popoff, M.R. (eds). Burlington, MA: Academic Press
    • Leppla, S.H. (2006) Bacillus anthracis toxins. In The Comprehensive Sourcebook of Bacterial Protein Toxins. Alouf, J.E., and Popoff, M.R. (eds). Burlington, MA: Academic Press, pp. 323-347.
    • (2006) The Comprehensive Sourcebook of Bacterial Protein Toxins , pp. 323-347
    • Leppla, S.H.1
  • 15
    • 0141527346 scopus 로고    scopus 로고
    • Retroviral insertional mutagenesis identifies a small protein required for synthesis of diphthamide, the target of bacterial ADP-ribosylating toxins
    • Liu, S., and Leppla, S.H. (2003) Retroviral insertional mutagenesis identifies a small protein required for synthesis of diphthamide, the target of bacterial ADP-ribosylating toxins. Mol Cell 12: 603-613.
    • (2003) Mol Cell , vol.12 , pp. 603-613
    • Liu, S.1    Leppla, S.H.2
  • 17
    • 6344252525 scopus 로고    scopus 로고
    • Identification of the proteins required forbiosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2
    • Liu, S., Milne, G.T., Kuremsky, J.G., Fink, G.R., and Leppla, S.H. (2004) Identification of the proteins required forbiosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24: 9487-9497.
    • (2004) Mol Cell Biol , vol.24 , pp. 9487-9497
    • Liu, S.1    Milne, G.T.2    Kuremsky, J.G.3    Fink, G.R.4    Leppla, S.H.5
  • 18
    • 33646551181 scopus 로고    scopus 로고
    • Dph3, a small protein required for diphthamide biosynthesis, is essential in mouse development
    • Liu, S., Wiggins, J.F., Sreenath, T., Kulkarni, A.B., Ward, J.M., and Leppla, S.H. (2006) Dph3, a small protein required for diphthamide biosynthesis, is essential in mouse development. Mol Cell Biol 26: 3835-3841.
    • (2006) Mol Cell Biol , vol.26 , pp. 3835-3841
    • Liu, S.1    Wiggins, J.F.2    Sreenath, T.3    Kulkarni, A.B.4    Ward, J.M.5    Leppla, S.H.6
  • 19
    • 33947139688 scopus 로고    scopus 로고
    • Characterization of the interaction between anthrax toxin and its cellular receptors
    • Liu, S., Leung, H.J., and Leppla, S.H. (2007) Characterization of the interaction between anthrax toxin and its cellular receptors. Cell Microbiol 9: 977-987.
    • (2007) Cell Microbiol , vol.9 , pp. 977-987
    • Liu, S.1    Leung, H.J.2    Leppla, S.H.3
  • 20
    • 0026746489 scopus 로고
    • DPH5, a methyltransferase gene required for diphthamide biosynthesis in Saccharomyces cerevisiae
    • Mattheakis, L.C., Shen, W.H., and Collier, R.J. (1992) DPH5, a methyltransferase gene required for diphthamide biosynthesis in Saccharomyces cerevisiae. Mol Cell Biol 12: 4026-4037.
    • (1992) Mol Cell Biol , vol.12 , pp. 4026-4037
    • Mattheakis, L.C.1    Shen, W.H.2    Collier, R.J.3
  • 21
    • 0027442619 scopus 로고
    • Diphthamide synthesis in Saccharomyces cerevisiae: Structure of the DPH2 gene
    • Mattheakis, L.C., Sor, F., and Collier, R.J. (1993) Diphthamide synthesis in Saccharomyces cerevisiae: Structure of the DPH2 gene. Gene 132: 149-154.
    • (1993) Gene , vol.132 , pp. 149-154
    • Mattheakis, L.C.1    Sor, F.2    Collier, R.J.3
  • 22
    • 0018385392 scopus 로고
    • Characterization of the diphtheria toxin-resistance system in Chinese hamster ovary cells
    • Moehring, J.M., and Moehring, T.J. (1979) Characterization of the diphtheria toxin-resistance system in Chinese hamster ovary cells. Somatic Cell Genet 5: 453-468.
    • (1979) Somatic Cell Genet , vol.5 , pp. 453-468
    • Moehring, J.M.1    Moehring, T.J.2
  • 23
    • 0018862384 scopus 로고
    • Posttranslational modification of elongation factor 2 in diphtheria-toxin-resistant mutants of CHO-K1 cells
    • Moehring, J.M., Moehring, T.J., and Danley, D.E. (1980) Posttranslational modification of elongation factor 2 in diphtheria-toxin-resistant mutants of CHO-K1 cells. Proc Natl Acad Sci USA 77: 1010-1014.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1010-1014
    • Moehring, J.M.1    Moehring, T.J.2    Danley, D.E.3
  • 24
    • 0021251336 scopus 로고
    • In vitro biosynthesis of diphthamide, studied with mutant Chinese hamster ovary cells resistant to diphtheria toxin
    • Moehring, T.J., Danley, D.E., and Moehring, J.M. (1984) In vitro biosynthesis of diphthamide, studied with mutant Chinese hamster ovary cells resistant to diphtheria toxin. Mol Cell Biol 4: 642-650.
    • (1984) Mol Cell Biol , vol.4 , pp. 642-650
    • Moehring, T.J.1    Danley, D.E.2    Moehring, J.M.3
  • 25
    • 0026747170 scopus 로고
    • Expression cloning of a diphtheria toxin receptor: Identity with a heparin-binding EGF-like growth factor precursor
    • Naglich, J.G., Metherall, J.E., Russell, D.W., and Eidels, L. (1992) Expression cloning of a diphtheria toxin receptor: Identity with a heparin-binding EGF-like growth factor precursor. Cell 69: 1051-1061.
    • (1992) Cell , vol.69 , pp. 1051-1061
    • Naglich, J.G.1    Metherall, J.E.2    Russell, D.W.3    Eidels, L.4
  • 27
    • 0019819635 scopus 로고
    • Diphtheria toxin. Site and configuration of ADP-ribosylation of diphthamide in elongation factor 2
    • Oppenheimer, N.J., and Bodley, J.W. (1981) Diphtheria toxin. Site and configuration of ADP-ribosylation of diphthamide in elongation factor 2. J Biol Chem 256: 8579-8581.
    • (1981) J Biol Chem , vol.256 , pp. 8579-8581
    • Oppenheimer, N.J.1    Bodley, J.W.2
  • 28
    • 33845951105 scopus 로고    scopus 로고
    • Translation elongation factor 2 anticodon mimicry domain mutants affect fidelity and diphtheria toxin resistance
    • Ortiz, P.A., Ulloque, R., Kihara, G.K., Zheng, H., and Kinzy, T.G. (2006) Translation elongation factor 2 anticodon mimicry domain mutants affect fidelity and diphtheria toxin resistance. J Biol Chem 281: 32639-32648.
    • (2006) J Biol Chem , vol.281 , pp. 32639-32648
    • Ortiz, P.A.1    Ulloque, R.2    Kihara, G.K.3    Zheng, H.4    Kinzy, T.G.5
  • 30
    • 3042522611 scopus 로고    scopus 로고
    • Antiviral activity of ribosome inactivating proteins in medicine
    • Parikh, B.A., and Tumer, N.E. (2004) Antiviral activity of ribosome inactivating proteins in medicine. Mini Rev Med Chem 4: 523-543.
    • (2004) Mini Rev Med Chem , vol.4 , pp. 523-543
    • Parikh, B.A.1    Tumer, N.E.2
  • 32
    • 0026531732 scopus 로고
    • Protein toxin inhibitors of protein synthesis
    • Perentesis, J.P., Miller, S.P., and Bodley, J.W. (1992) Protein toxin inhibitors of protein synthesis. Biofactors 3: 173-184.
    • (1992) Biofactors , vol.3 , pp. 173-184
    • Perentesis, J.P.1    Miller, S.P.2    Bodley, J.W.3
  • 33
    • 0034924485 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins from plants: More than RNA N-glycosidases?
    • Peumans, W.J., Hao, Q., and Van Damme, E.J. (2001) Ribosome-inactivating proteins from plants: More than RNA N-glycosidases? FASEB J 15: 1493-1506.
    • (2001) FASEB J , vol.15 , pp. 1493-1506
    • Peumans, W.J.1    Hao, Q.2    Van Damme, E.J.3
  • 34
    • 0027529133 scopus 로고
    • Saccharomyces cerevisiae elongation factor 2. Mutagenesis of the histidine precursor of diphthamide yields a functional protein that is resistant to diphtheria toxin
    • Phan, L.D., Perentesis, J.P., and Bodley, J.W. (1993) Saccharomyces cerevisiae elongation factor 2. Mutagenesis of the histidine precursor of diphthamide yields a functional protein that is resistant to diphtheria toxin. J Biol Chem 268: 8665-8668.
    • (1993) J Biol Chem , vol.268 , pp. 8665-8668
    • Phan, L.D.1    Perentesis, J.P.2    Bodley, J.W.3
  • 35
    • 0019333247 scopus 로고
    • ADP-ribosylation of elongation factor 2 by diphtheria toxin. Isolation and properties of the novel ribosyl-amino acid and its hydrolysis products
    • Van Ness, B.G., Howard, J.B., and Bodley, J.W. (1980) ADP-ribosylation of elongation factor 2 by diphtheria toxin. Isolation and properties of the novel ribosyl-amino acid and its hydrolysis products. J Biol Chem 255: 10717-10720.
    • (1980) J Biol Chem , vol.255 , pp. 10717-10720
    • Van Ness, B.G.1    Howard, J.B.2    Bodley, J.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.