Journal of Microbiology

  • 제40권4호
  • /
  • Pages.295-300
  • /
  • 2002
  • /
  • 1225-8873(pISSN)
  • /
  • 1976-3794(eISSN)
한국미생물학회 (The Microbiological Society of Korea)
권호 표지

Overexpression of Fish DRG2 Induces Cell Rounding

  • Park, Jeong-Jae (Department of Biological Sciences, ImmunoModulation Research Center, University of Ulsan) ;
  • Cha, Seung-Ju (Department of Biological Sciences, ImmunoModulation Research Center, University of Ulsan) ;
  • Ko, Myung-Seok (Department of Biological Sciences, ImmunoModulation Research Center, University of Ulsan) ;
  • Cho, Wha-Ja (Department of Biological Sciences, ImmunoModulation Research Center, University of Ulsan) ;
  • Yoon, Won-Joon (Department of Biological Sciences, ImmunoModulation Research Center, University of Ulsan) ;
  • Moon, Chang-Hoon (Department of Biological Sciences, ImmunoModulation Research Center, University of Ulsan) ;
  • Do, Jeong-Wan (Department of Biological Sciences, ImmunoModulation Research Center, University of Ulsan) ;
  • Kim, Sung-Bum (Department of Biological Sciences, ImmunoModulation Research Center, University of Ulsan) ;
  • Hebok Song (Department of Biological Sciences, ImmunoModulation Research Center, University of Ulsan)
  • 발행 : 2002.12.01
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

Previously, we reported induced expression of developmentally regulated CTP-binding protein 2 (DRG2) in fish cells at the late stage of rhabdovirus infection. To investigate the biological role of fish DRG2 (fDRG2), we transfected CHSE-214 cells with an expression vector containing complete fDRG2 fused to the N-terminal end of an enhanced green fluorescent protein (EGFP). Low level expression of fDRG2-EGFP did not induce morphological change or cell death. However, a high level expression of fDRG2-EGFP induced cell rounding and caused depletion of the cell population in FACS analysis. Several truncated fragments were fused to EGFP. FACS analysis was conducted to determine the presence of cells expressing high levels of the resulting chimera. While cells expressing a high level of N-terminus were detected, those expressing high levels of the C-terminal fragment 243-290 containing the G4 motif were absent in FACS analysis. Based on these observations, we propose that overexpression of fDRG2 may induce cell rounding, a representative cytopathic effect of virus-infected cells in the late stage of infection and the C-terminus of the fDRG2 is essential for this function.

키워드

참고문헌

  1. J. Virol. v.71 Rhabdovirus-induced apoptosis in a fish cell line is inhibited by a human endogenous acid cysteine proteinase inhibitor. Bjorklund,H.V.;T.R.Johansson;A.Rinne.
  2. Science v.273 Complete genome sequence of the methanogenic archaeon Bult,C.J.(et al)
  3. J.Virol. v.74 Infectious ehmatopoirtic necrosis virus matrix protein inhibits hostdirected gene expression and induces morphological changes of apoptosis in cell cultures. Chiou,P.P.;C.H.Kim;P.Ormonde'J.C.Leong.
  4. Plant Mol.Biol. v.39 Characterization of DRGs, develop[mentally regulated GTP-binding proteins, from pea and Arabidopsis. Devitt,M.L.;K.J.Maas;J.P.Stafstrom.
  5. Curr.Opin.Cell Biol. v.9 Integrins and anoikis. Frisch,S.M.;E.Ruoslahti.
  6. J. Cell Biol. v.124 Disruption of epithelial cell-matrix interactions induces apoptosis. Frisch,S.M.;H.Francis.
  7. Gene v.125 Sequence of the Schizosac-charomyces pombe gtp1 gene and identification of a novel family of putative GTP-binding proteins. Hudson,J.D.;P.G.Young.
  8. Int.J.Dev.Biol. v.37 Expression of GTP-binding proteins drg during Xenopus laevis development. Kumar,S.;M.Iwao;T.Yamagishi;M.Noda;M.Asaashima.
  9. Biochem. Biophys Res. Commun v.185 Identification of a set of genes with with developmentally down-regulated expression in the mouse brain. Kumar,S.;Y.Tomooka;M.Noda.
  10. FEBS Letters v.429 Molecular cloning of a nivel GTP-binding proteins induced in fish cells by rhabdovirus infection. Lee,E.H.'H.J.Kim;J.J.Park;J.Y.Choi;W.J.Cho;S.J.Cha;C.H.Moon;J.M.Park;W.J.Yoon;B.J.Lee;D.H.Lee;H.S.Kang;M.A.Yoo;H.D.Kim;J.W.Park.
  11. Biochim.Biophys.Acta v.1491 DRG represents a family of two closely related GTP-binding proteins. Li,B.;B.Trucb.
  12. Oncogene v.12 Association of a novel GTP binding protein, DRG,with TAL oncogenic proteins. Mahaian,M.A.;S.T.Park;X.H.Sun.
  13. Mol.Biol.Cell v.4 The extracellular matrix as a cell survival fator. Merecith,J.E.;B.Fazrli;M.A.Schwartz.
  14. Cell v.86 The Tcell leukemia oncoprotein SCL/tal-1 is essential for development fo all hematopoietic lineages. Porcher,C.;W.Swat;K.Rockwell;Y.Fujiwara;F.W.Alt;S.H.Orkin.
  15. J. Cell Biol. v.149 Activated Ras prevents doenregulation of Bcl-X(L) trig-gered by detachment from the extracellular matrix.A mechanism of Ras-induced resistance to anoikis in intestnal epithelial cells. Rosen K.;J.Rak;T.Leung;N.M.Dean;R.S.Kerbel;J.Filmus.
  16. Biovhem.Biophys.Res.Commun. v.189 DRG: a novel developmentally regulated GTP-binding protein. Sazuka,T.;Y.Tomooka;Y.Ikawa;M.Noda;S.Kumar.
  17. J.Biol.Chem. v.269 A novel GTP-binding protein which is selectively repressed in SV40 transformed fibroblasts. Schenker,T.;C.Lach;B.Kessler;S.Calderara;B.Trueb.
  18. EMBO J. v.8 Characterization of the L11,L1,L10 and L12 equivalent ribosomal protein gene cluster of the halophilic archaebacterium Halobacterium cutirubrum. Shimmin,L.C.;P.P.Dennis.
  19. J.Virol. v.76 Ebola virus glycoproteins induce global surface protein down-modulation and loss of cell adherence. Simmons,G.;R.J.Wool-Lewis;F.Baribaud;R.C.Netter;P.Bates.
  20. Mol.Gen.Genet. v.242 The gene upstream of DmRP128 cides for a novel GTP-binding protein of Drosophila melanogaster. Sommer,K.A.;G.Petersen;E.K.F.Bautz.
  21. Science v.274 Tricorn protease- the core of a modular proteolytic systerm. Tamura,T.;N.Tamura;Z.Cejka;R.Hegerl;F.Lottspeich;W.Baumeister.
  22. J. Virol. v.71 Regulation of apoptosis by viral gene products. Teodoro,J.G.;P.E.Branton.
  23. Nature v.368 2.2 Mb of contiguous nucleotide sequence from chromosome Ⅲ of C. elegans. Wilson,R.
  24. Biochem.Biophys. Acta. v.1448 SCL binds the human homologue of DRG in vivo. Zhao,X.F.;P.D.Aplan.