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Volumn 15, Issue 17, 1996, Pages 4469-4476

The cytoplasmic tail of NSP4, the endoplasmic reticulum-localized non-structural glycoprotein of rotavirus, contains distinct virus binding and coiled coil domains

Author keywords

CD spectroscopy; Cytoplasmic tail; Glycoprotein receptor; Rotavirus assembly; helical coiled coil

Indexed keywords

VIRUS GLYCOPROTEIN;

EID: 0029791663     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00824.x     Document Type: Article
Times cited : (78)

References (34)
  • 1
    • 0024446502 scopus 로고
    • Receptor activity of rotavirus nonstructural glycoprotein NS28
    • Au, K.-S., Chan, W.-K., Burns, J.W. and Estes, M.K. (1989) Receptor activity of rotavirus nonstructural glycoprotein NS28. J. Virol., 63, 4553-4562.
    • (1989) J. Virol. , vol.63 , pp. 4553-4562
    • Au, K.-S.1    Chan, W.-K.2    Burns, J.W.3    Estes, M.K.4
  • 2
    • 0027217615 scopus 로고
    • A subviral particle binding domain on the rotavirus nonstructural glycoprotein NS28
    • Au, K.-S., Mattion, N.M. and Estes, M.K. (1993) A subviral particle binding domain on the rotavirus nonstructural glycoprotein NS28. Virology, 194, 665-673.
    • (1993) Virology , vol.194 , pp. 665-673
    • Au, K.-S.1    Mattion, N.M.2    Estes, M.K.3
  • 3
    • 0025177660 scopus 로고
    • Molecular biology of rotaviruses
    • Bellamy, A.R. and Both, G.W. (1990) Molecular biology of rotaviruses. Adv. Virus Res., 38, 1-43.
    • (1990) Adv. Virus Res. , vol.38 , pp. 1-43
    • Bellamy, A.R.1    Both, G.W.2
  • 4
    • 0024426841 scopus 로고
    • Topology of the non-structural rotavirus receptor glycoprotein NS28 in the rough endoplasmic reticulum
    • Bergmann, C.C., Maass, D., Poruchynsky, M.S., Atkinson, P.H. and Bellamy, A.R. (1989) Topology of the non-structural rotavirus receptor glycoprotein NS28 in the rough endoplasmic reticulum. EMBO J., 8, 1695-1703.
    • (1989) EMBO J. , vol.8 , pp. 1695-1703
    • Bergmann, C.C.1    Maass, D.2    Poruchynsky, M.S.3    Atkinson, P.H.4    Bellamy, A.R.5
  • 5
    • 0025062207 scopus 로고
    • The secondary structure of gap junctions. Influence of isolation methods and proteolysis
    • Cascio, M., Gogol, E. and Wallace, B.A. (1990) The secondary structure of gap junctions. Influence of isolation methods and proteolysis. J. Biol. Chem., 265, 2358-2364.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2358-2364
    • Cascio, M.1    Gogol, E.2    Wallace, B.A.3
  • 6
  • 7
    • 0018118041 scopus 로고
    • Circular dichroic analysis of protein conformation: Inclusion of the β-turns
    • Chang, C.T., Wu, C.-S.C. and Yang, J.T. (1978) Circular dichroic analysis of protein conformation: inclusion of the β-turns. Anal. Biochem., 91, 13-31.
    • (1978) Anal. Biochem. , vol.91 , pp. 13-31
    • Chang, C.T.1    Wu, C.-S.C.2    Yang, J.T.3
  • 8
    • 0001248650 scopus 로고
    • α-helical coiled coils - a widespread motif in proteins
    • Cohen, C. and Parry, D.A.D. (1986) α-helical coiled coils - a widespread motif in proteins. Trends Biochem. Sci., 11, 245-248.
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 245-248
    • Cohen, C.1    Parry, D.A.D.2
  • 9
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. (1967) Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry, 6, 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 10
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury, P.B., Zhang, T., Kim, P.S. and Alber, T. (1993) A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science, 262, 1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 11
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson, R., Baldwin, J.M., Ceska, T.A., Zemlin, F., Beckmann, E. and Downing, K.H. (1990) Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol., 213, 899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 12
    • 0022555883 scopus 로고
    • Refolding and association of oligomeric proteins
    • Jaenicke, R. and Rudolph, R. (1986) Refolding and association of oligomeric proteins. Methods Enzymol., 131, 218-250.
    • (1986) Methods Enzymol. , vol.131 , pp. 218-250
    • Jaenicke, R.1    Rudolph, R.2
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0021719074 scopus 로고
    • Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded α-helical coiled-coils
    • Lau, S.Y.M., Taneja, A.K. and Hodges, R.S. (1984) Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded α-helical coiled-coils. J. Biol. Chem., 259, 13253-13261.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13253-13261
    • Lau, S.Y.M.1    Taneja, A.K.2    Hodges, R.S.3
  • 15
    • 0025370971 scopus 로고
    • Rotavirus proteins VP7, NS28, and VP4 form oligomeric structures
    • Maass, D.R. and Atkinson, P.H. (1990) Rotavirus proteins VP7, NS28, and VP4 form oligomeric structures. J. Virol., 64, 2632-2641.
    • (1990) J. Virol. , vol.64 , pp. 2632-2641
    • Maass, D.R.1    Atkinson, P.H.2
  • 16
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsiudara, P. (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem., 262, 10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsiudara, P.1
  • 18
    • 0025129428 scopus 로고
    • Oligomers of the cytoplasmic domain of the p62/E2 membrane protein of Semliki Forest virus bind to the nucleocapsid in vitro
    • Metsikkö, K. and Garoff, H. (1990) Oligomers of the cytoplasmic domain of the p62/E2 membrane protein of Semliki Forest virus bind to the nucleocapsid in vitro. J. Virol., 64, 4678-4683.
    • (1990) J. Virol. , vol.64 , pp. 4678-4683
    • Metsikkö, K.1    Garoff, H.2
  • 20
    • 0024534241 scopus 로고
    • Evidence that the leucine zipper is a coiled coil
    • O'Shea, E.K., Rutkowski, R. and Kim, P.S. (1989) Evidence that the leucine zipper is a coiled coil. Science, 243, 538-542.
    • (1989) Science , vol.243 , pp. 538-542
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 21
    • 0022538396 scopus 로고
    • Intracellular assembly and packaging of Hepatitis B surface antigen particles occur in the endoplasmic reticulum
    • Patzer, E.J., Nakamura, G.R., Simonsen, C.C, Levinson, A.D. and Brands, R. (1986) Intracellular assembly and packaging of Hepatitis B surface antigen particles occur in the endoplasmic reticulum. J. Virol., 58, 884-892.
    • (1986) J. Virol. , vol.58 , pp. 884-892
    • Patzer, E.J.1    Nakamura, G.R.2    Simonsen, C.C.3    Levinson, A.D.4    Brands, R.5
  • 22
    • 0020681930 scopus 로고
    • Effects of tunicamycin on rotavirus morphogenesis and infectivity
    • Petrie, B.L., Estes, M.K. and Graham, D.Y. (1983) Effects of tunicamycin on rotavirus morphogenesis and infectivity. J. Virol., 46, 270-274.
    • (1983) J. Virol. , vol.46 , pp. 270-274
    • Petrie, B.L.1    Estes, M.K.2    Graham, D.Y.3
  • 23
    • 0025913093 scopus 로고
    • Calcium depletion blocks the maturation of rotavirus by altering the oligomerization of virus-encoded proteins in the ER
    • Poruchynsky, M.S., Maass, D.R. and Atkinson, P.H. (1991) Calcium depletion blocks the maturation of rotavirus by altering the oligomerization of virus-encoded proteins in the ER. J. Cell Biol., 114, 651-661.
    • (1991) J. Cell Biol. , vol.114 , pp. 651-661
    • Poruchynsky, M.S.1    Maass, D.R.2    Atkinson, P.H.3
  • 24
    • 0019904644 scopus 로고
    • Effect of tunicamycin on rotavirus assembly and infectivity
    • Sabara, M., Babiuk, L.A., Gilchrist, J. and Misra, V. (1982) Effect of tunicamycin on rotavirus assembly and infectivity. J. Virol., 43, 1082-1090.
    • (1982) J. Virol. , vol.43 , pp. 1082-1090
    • Sabara, M.1    Babiuk, L.A.2    Gilchrist, J.3    Misra, V.4
  • 25
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H. and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem., 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 26
    • 0019066885 scopus 로고
    • The budding mechanisms of enveloped animal viruses
    • Simons, K. and Garoff, H. (1980) The budding mechanisms of enveloped animal viruses. J. Gen. Virol., 50, 1-21.
    • (1980) J. Gen. Virol. , vol.50 , pp. 1-21
    • Simons, K.1    Garoff, H.2
  • 27
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D.B. and Johnson, K.S. (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene, 67, 31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 28
    • 0026691322 scopus 로고
    • Spike protein-nucleocapsid interactions drive the budding of alphaviruses
    • Suomalainen, M., Liljeström, P. and Garoff, H. (1992) Spike protein-nucleocapsid interactions drive the budding of alphaviruses. J. Virol., 66, 4737-4747.
    • (1992) J. Virol. , vol.66 , pp. 4737-4747
    • Suomalainen, M.1    Liljeström, P.2    Garoff, H.3
  • 29
    • 0026773866 scopus 로고
    • Transient expression and mutational analysis of the rotavirus intracellular receptor: The C-terminal methionine residue is essential for ligand binding
    • Taylor, J.A., Meyer, J.C., Legge, M.A., O'Brien, J.A., Street, J.E., Lord, V.J., Bergmann, C.C. and Bellamy, A.R. (1992) Transient expression and mutational analysis of the rotavirus intracellular receptor: the C-terminal methionine residue is essential for ligand binding. J. Virol., 66, 3566-3572.
    • (1992) J. Virol. , vol.66 , pp. 3566-3572
    • Taylor, J.A.1    Meyer, J.C.2    Legge, M.A.3    O'Brien, J.A.4    Street, J.E.5    Lord, V.J.6    Bergmann, C.C.7    Bellamy, A.R.8
  • 30
    • 0027302456 scopus 로고
    • The RER-localized rotavirus intracellular receptor: A truncated purified soluble form is multivalent and binds virus particles
    • Taylor, J.A., O'Brien, J.A., Lord, V.J., Meyer, J.C. and Bellamy, A.R. (1993) The RER-localized rotavirus intracellular receptor: a truncated purified soluble form is multivalent and binds virus particles. Virology, 194, 807-814.
    • (1993) Virology , vol.194 , pp. 807-814
    • Taylor, J.A.1    O'Brien, J.A.2    Lord, V.J.3    Meyer, J.C.4    Bellamy, A.R.5
  • 32
    • 0003605587 scopus 로고
    • Prentice-Hall, Englewood Cliffs, NJ
    • Van Holde, K.E. (1971) Physical Biochemistry. Prentice-Hall, Englewood Cliffs, NJ, p. 81.
    • (1971) Physical Biochemistry , pp. 81
    • Van Holde, K.E.1
  • 33
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3Å resolution
    • Wilson, I.A., Skehel, J.J. and Wiley, D.C. (1981) Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3Å resolution. Nature, 289, 366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3


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