메뉴 건너뛰기




Volumn 15, Issue 11, 1996, Pages 2651-2658

Co-translational trimerization of the reovirus cell attachment protein

Author keywords

Protein oligomerization; Rabbit reticulocyte lysate; Reovirus protein 1

Indexed keywords

APYRASE; CELL ADHESION MOLECULE; MESSENGER RNA; VIRUS PROTEIN;

EID: 0029885416     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00625.x     Document Type: Article
Times cited : (44)

References (32)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of polypeptide chains
    • Anfinsen,C.B. (1973) Principles that govern the folding of polypeptide chains. Science, 181, 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0024205704 scopus 로고
    • High-level synthesis of biologically active reovirus protein σ1 in a mammalian expression vector system
    • Banerjea,A.C., Brechling,K.A., Ray,C.A., Erickson,H., Pickup,D.T. and Joklik,W.K. (1988) High-level synthesis of biologically active reovirus protein σ1 in a mammalian expression vector system. Virology, 167, 601-612.
    • (1988) Virology , vol.167 , pp. 601-612
    • Banerjea, A.C.1    Brechling, K.A.2    Ray, C.A.3    Erickson, H.4    Pickup, D.T.5    Joklik, W.K.6
  • 4
    • 0025303147 scopus 로고
    • Interaction of Hsp70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckmann,R.P., Mizzen,L.A. and Welch,W.J. (1990) Interaction of Hsp70 with newly synthesized proteins: implications for protein folding and assembly. Science, 248, 850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.A.2    Welch, W.J.3
  • 5
    • 0027157736 scopus 로고
    • Folding and assembly of viral membrane proteins
    • Doms,R.W., Lamb,R.A., Rose,J.K. and Helenius,A. (1993) Folding and assembly of viral membrane proteins. Virology, 193, 545-562.
    • (1993) Virology , vol.193 , pp. 545-562
    • Doms, R.W.1    Lamb, R.A.2    Rose, J.K.3    Helenius, A.4
  • 6
    • 0026524405 scopus 로고
    • Biosynthesis of reovirus-specified polypeptides: Ribosome pausing during the translation of reovirus S1 mRNA
    • Doohan,J.P. and Samuel,C.E. (1992) Biosynthesis of reovirus-specified polypeptides: ribosome pausing during the translation of reovirus S1 mRNA. Virology, 186, 409-425.
    • (1992) Virology , vol.186 , pp. 409-425
    • Doohan, J.P.1    Samuel, C.E.2
  • 7
    • 0027214192 scopus 로고
    • Biosynthesis of reovirus-specified polypeptides: Analysis of ribosome pausing during translation of reovirus S1 and S4 mRNAs in virus-infected and vector-transfected cells
    • Doohan,J.P. and Samuel,C.E. (1993) Biosynthesis of reovirus-specified polypeptides: analysis of ribosome pausing during translation of reovirus S1 and S4 mRNAs in virus-infected and vector-transfected cells. J. Biol. Chem., 268, 18313-18320.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18313-18320
    • Doohan, J.P.1    Samuel, C.E.2
  • 8
    • 0028088356 scopus 로고
    • Localization of two protease-sensitive regions separating distinct domains in the reovirus cell-attachment protein σ1
    • Duncan,R. and Lee,P.W.K. (1994) Localization of two protease-sensitive regions separating distinct domains in the reovirus cell-attachment protein σ1. Virology, 203, 149-152.
    • (1994) Virology , vol.203 , pp. 149-152
    • Duncan, R.1    Lee, P.W.K.2
  • 9
    • 0025727528 scopus 로고
    • Conformational and functional analysis of the C-terminal globular head of the reovirus cell attachment protein
    • Duncan,R., Horne,D., Strong,J.E., Leone,G., Pon,R.T., Yeung,M.C. and Lee,P.W.K. (1991) Conformational and functional analysis of the C-terminal globular head of the reovirus cell attachment protein. Virology, 182, 810-819.
    • (1991) Virology , vol.182 , pp. 810-819
    • Duncan, R.1    Horne, D.2    Strong, J.E.3    Leone, G.4    Pon, R.T.5    Yeung, M.C.6    Lee, P.W.K.7
  • 10
    • 0028127827 scopus 로고
    • Role of molecular chaperones in protein folding
    • Ellis,R.J. (1994) Role of molecular chaperones in protein folding. Curr. Opin. Struct. Biol., 4, 117-122.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 117-122
    • Ellis, R.J.1
  • 11
    • 0028889120 scopus 로고
    • Contribution of cotranslational folding to the rate of formation of native protein structure
    • Fedorov,N. and Baldwin,T.O. (1995) Contribution of cotranslational folding to the rate of formation of native protein structure. Proc. Natl Acad. Sci. USA, 92, 1227-1231.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1227-1231
    • Fedorov, N.1    Baldwin, T.O.2
  • 12
    • 0028298885 scopus 로고
    • Binding of reovirus to receptor leads to conformational changes in viral capsid proteins that are reversible upon virus detachment
    • Fernandes,J., Tang,D., Leone,G. and Lee,P.W.K. (1994) Binding of reovirus to receptor leads to conformational changes in viral capsid proteins that are reversible upon virus detachment. J. Biol. Chem., 269, 17043-17047.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17043-17047
    • Fernandes, J.1    Tang, D.2    Leone, G.3    Lee, P.W.K.4
  • 13
    • 0025372616 scopus 로고
    • Molecular structure of the cell attachment protein of reovirus: Correlation of computer-processed electron micrographs with sequence-based predictions
    • Fraser,R.D.B., Furlong,D.B., Trus,B.L., Nibert,M.L., Fields,B.N. and Steven,A.C. (1990) Molecular structure of the cell attachment protein of reovirus: correlation of computer-processed electron micrographs with sequence-based predictions. J. Virol., 64, 2990-3000
    • (1990) J. Virol. , vol.64 , pp. 2990-3000
    • Fraser, R.D.B.1    Furlong, D.B.2    Trus, B.L.3    Nibert, M.L.4    Fields, B.N.5    Steven, A.C.6
  • 14
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman,J., Nimmesgern,E., Ohtsuka,K. and Hartl,F.U. (1994) Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature, 370, 111-117.
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hartl, F.U.4
  • 15
    • 0023945392 scopus 로고
    • σ1 protein of mammalian reoviruses extends from the surfaces of viral particles
    • Furlong,D.B., Nibert,M.L. and Fields,B.N. (1988) σ1 protein of mammalian reoviruses extends from the surfaces of viral particles. J. Virol., 62, 246-256.
    • (1988) J. Virol. , vol.62 , pp. 246-256
    • Furlong, D.B.1    Nibert, M.L.2    Fields, B.N.3
  • 16
    • 0027333423 scopus 로고
    • Role of the major heat shock proteins as molecular chaperones
    • Georgopoulos,C. and Welch,W.J. (1993) Role of the major heat shock proteins as molecular chaperones. Annu. Rev. Cell Biol., 9, 601-634.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 601-634
    • Georgopoulos, C.1    Welch, W.J.2
  • 17
    • 0028117314 scopus 로고
    • Molecular chaperones in protein folding: The art of avoiding sticky situations
    • Hartl,F.U., Hlodan,R. and Langer,T. (1994) Molecular chaperones in protein folding: the art of avoiding sticky situations. Trends Biochem. Sci., 19, 20-25.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 20-25
    • Hartl, F.U.1    Hlodan, R.2    Langer, T.3
  • 18
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendrick,J.P. and Hartl,F.U. (1993) Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem., 62, 349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.U.2
  • 19
    • 0028094779 scopus 로고
    • Folding of firefly luciferase during translation in a cell-free system
    • Kolb,V.A., Makeyev,E.V. and Spirin,A.S. (1994) Folding of firefly luciferase during translation in a cell-free system. EMBO J., 13, 3631-3637.
    • (1994) EMBO J. , vol.13 , pp. 3631-3637
    • Kolb, V.A.1    Makeyev, E.V.2    Spirin, A.S.3
  • 21
    • 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
  • 22
    • 0019522275 scopus 로고
    • Protein σ1 is the reovirus cell attachment protein
    • Lee,P.W.K., Hayes,E.C. and Joklik,W.K. (1981) Protein σ1 is the reovirus cell attachment protein. Virology, 108, 156-163.
    • (1981) Virology , vol.108 , pp. 156-163
    • Lee, P.W.K.1    Hayes, E.C.2    Joklik, W.K.3
  • 23
    • 0025810915 scopus 로고
    • The N-terminal heptad repeat region of reovirus cell attachment protein σ1 is responsible for σ1 oligomer stability and possesses intrinsic oligomerization function
    • Leone,G., Duncan,R., Mah,D.C.W., Price,A., Cashdollar,L.W. and Lee,P.W.K. (1991 a) The N-terminal heptad repeat region of reovirus cell attachment protein σ1 is responsible for σ1 oligomer stability and possesses intrinsic oligomerization function. Virology, 182, 336-345.
    • (1991) Virology , vol.182 , pp. 336-345
    • Leone, G.1    Duncan, R.2    Mah, D.C.W.3    Price, A.4    Cashdollar, L.W.5    Lee, P.W.K.6
  • 24
    • 0025955495 scopus 로고
    • Trimerization of the reovirus cell attachment protein (σ1) induces conformational changes in σ1 necessary for its cell binding function
    • Leone,G., Duncan,R. and Lee,P.W.K. (1991b) Trimerization of the reovirus cell attachment protein (σ1) induces conformational changes in σ1 necessary for its cell binding function. Virology, 184, 758-761.
    • (1991) Virology , vol.184 , pp. 758-761
    • Leone, G.1    Duncan, R.2    Lee, P.W.K.3
  • 25
    • 0025811406 scopus 로고
    • The incorporation of reovirus cell attachment protein σ1 into virions requires the N-terminal hydrophobic tail and the adjacent heptad repeat region
    • Leone,G., Mah,D.C.W. and Lee,P.W.K. (1991c) The incorporation of reovirus cell attachment protein σ1 into virions requires the N-terminal hydrophobic tail and the adjacent heptad repeat region. Virology, 182, 346-350.
    • (1991) Virology , vol.182 , pp. 346-350
    • Leone, G.1    Mah, D.C.W.2    Lee, P.W.K.3
  • 26
    • 0026466142 scopus 로고
    • The reovirus cell attachment protein possesses two independently active trimerization domains: Basis of dominant negative effects
    • Leone,G., Maybaum,L. and Lee,P.W.K. (1992) The reovirus cell attachment protein possesses two independently active trimerization domains: basis of dominant negative effects. Cell, 71, 479-488.
    • (1992) Cell , vol.71 , pp. 479-488
    • Leone, G.1    Maybaum, L.2    Lee, P.W.K.3
  • 27
    • 0029922120 scopus 로고    scopus 로고
    • C-terminal trimerization, but not N-terminal trimerization, of the reovirus cell attachment protein in a post-translational and Hsp70/ATP-dependent process
    • in press
    • Leone,G., Coffey,M.C., Gilmore,R., Duncan,R., Maybaum,L. and Lee,P.W.K. (1996) C-terminal trimerization, but not N-terminal trimerization, of the reovirus cell attachment protein in a post-translational and Hsp70/ATP-dependent process. J. Biol. Chem., in press.
    • (1996) J. Biol. Chem.
    • Leone, G.1    Coffey, M.C.2    Gilmore, R.3    Duncan, R.4    Maybaum, L.5    Lee, P.W.K.6
  • 28
    • 0025051279 scopus 로고
    • The N-terminal quarter of reovirus cell attachment protein σ1 possesses intrinsic virion-anchoring function
    • Mah,D.C.W., Leone,G., Jankowski,J.M. and Lee,P.W.K. (1990) The N-terminal quarter of reovirus cell attachment protein σ1 possesses intrinsic virion-anchoring function. Virology, 179, 95-103
    • (1990) Virology , vol.179 , pp. 95-103
    • Mah, D.C.W.1    Leone, G.2    Jankowski, J.M.3    Lee, P.W.K.4
  • 29
    • 0023404326 scopus 로고
    • Analysis of functional domains on reovirus cell attachment protein σ1 using cloned S1 gene deletion mutants
    • Nagata,L., Masri,S.A., Pon,R.T. and Lee,P.W.K. (1987) Analysis of functional domains on reovirus cell attachment protein σ1 using cloned S1 gene deletion mutants. Virology, 160, 162-168.
    • (1987) Virology , vol.160 , pp. 162-168
    • Nagata, L.1    Masri, S.A.2    Pon, R.T.3    Lee, P.W.K.4
  • 30
    • 0025866624 scopus 로고
    • Biochemical and biophysical characterization of the reovirus cell attachment protein σ1: Evidence that it is a homotrimer
    • Strong,J.E., Leone,G., Duncan,R., Sharma,R.K. and Lee,P.W.K. (1991) Biochemical and biophysical characterization of the reovirus cell attachment protein σ1: evidence that it is a homotrimer. Virology, 184, 23-32
    • (1991) Virology , vol.184 , pp. 23-32
    • Strong, J.E.1    Leone, G.2    Duncan, R.3    Sharma, R.K.4    Lee, P.W.K.5
  • 31
    • 0026503712 scopus 로고
    • Site-directed mutagenesis of the C-terminal portion of reovirus protein σ1: Evidence for a conformation-dependent receptor binding domain
    • Turner,D.L., Duncan,R. and Lee,P.W.K. (1992) Site-directed mutagenesis of the C-terminal portion of reovirus protein σ1: evidence for a conformation-dependent receptor binding domain. Virology, 186, 219-227
    • (1992) Virology , vol.186 , pp. 219-227
    • Turner, D.L.1    Duncan, R.2    Lee, P.W.K.3
  • 32
    • 0024524475 scopus 로고
    • The cell attachment proteins of type 1 and type 3 reovirus are differentially susceptible to trypsin and chymotrypsin
    • Yeung,M.C, Lim,D., Duncan,R., Shahrabadi,M.S., Cashdollar,L.W. and Lee,P.W.K. (1989) The cell attachment proteins of type 1 and type 3 reovirus are differentially susceptible to trypsin and chymotrypsin. Virology, 170, 62-70.
    • (1989) Virology , vol.170 , pp. 62-70
    • Yeung, M.C.1    Lim, D.2    Duncan, R.3    Shahrabadi, M.S.4    Cashdollar, L.W.5    Lee, P.W.K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.