메뉴 건너뛰기




Volumn 145, Issue 7, 2000, Pages 1305-1320

Expression of stable hepatitis B viral polymerase associated with GRP94 in E. coli

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; GLUCOSE REGULATED PROTEINS; GLUCOSE-REGULATED PROTEINS; HEAT SHOCK PROTEIN 70; MEMBRANE PROTEIN; P PROTEIN, HEPATITIS B VIRUS; POL PROTEIN; RNA DIRECTED DNA POLYMERASE;

EID: 0033656213     PISSN: 03048608     EISSN: None     Source Type: Journal    
DOI: 10.1007/s007050070092     Document Type: Article
Times cited : (15)

References (45)
  • 1
    • 0023857793 scopus 로고
    • Two proteins with reverse transcriptase activities associated with hepatitis B virus-like particles
    • Bavand MR, Laub O (1988) Two proteins with reverse transcriptase activities associated with hepatitis B virus-like particles. J Virol 62: 626-628
    • (1988) J Virol , vol.62 , pp. 626-628
    • Bavand, M.R.1    Laub, O.2
  • 2
    • 0024546607 scopus 로고
    • The hepatitis B virus-associated reverse transcriptase is encoded by the viral pol gene
    • Bavand M, Feitelson M, Laub O (1989) The hepatitis B virus-associated reverse transcriptase is encoded by the viral pol gene. J Virol 63: 1 019-1 021
    • (1989) J Virol , vol.63 , pp. 1019-1021
    • Bavand, M.1    Feitelson, M.2    Laub, O.3
  • 3
    • 0002830140 scopus 로고
    • Modulation of steroid receptor signal transduction by signal transduction by heat shock proteins
    • Morimoto RI, Tissieres A, Georgopoulos C (eds). Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Bohen SP, Yamamoto KR (1994) Modulation of steroid receptor signal transduction by signal transduction by heat shock proteins. In: Morimoto RI, Tissieres A, Georgopoulos C (eds) The biology of heat shock proteins and molecular chaperones. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, pp 313-334
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 313-334
    • Bohen, S.P.1    Yamamoto, K.R.2
  • 5
    • 0025076858 scopus 로고
    • Effects of insertional and point mutations on the functions of the duck hepatitis B virus polymerase
    • Chang LJ, Hirsch RC, Ganem D, Varmus HE (1990) Effects of insertional and point mutations on the functions of the duck hepatitis B virus polymerase. J Virol 64: 5 553-5 558
    • (1990) J Virol , vol.64 , pp. 5553-5558
    • Chang, L.J.1    Hirsch, R.C.2    Ganem, D.3    Varmus, H.E.4
  • 6
    • 0030013134 scopus 로고    scopus 로고
    • A positive regulatory sequence of hepatitis B viral small X promoter
    • Choi CY, Park GT, Rho HM (1996) A positive regulatory sequence of hepatitis B viral small X promoter. Eur J Biochem 239: 579-587
    • (1996) Eur J Biochem , vol.239 , pp. 579-587
    • Choi, C.Y.1    Park, G.T.2    Rho, H.M.3
  • 7
    • 0025991321 scopus 로고
    • Purification and partial characterization of equine infectious anemia virus transcriptase
    • DeVico A, Montelaro RC, Gallo RC, Sarngadharan MG (1991) Purification and partial characterization of equine infectious anemia virus transcriptase. Virology 185: 387-394
    • (1991) Virology , vol.185 , pp. 387-394
    • DeVico, A.1    Montelaro, R.C.2    Gallo, R.C.3    Sarngadharan, M.G.4
  • 8
    • 0032100480 scopus 로고    scopus 로고
    • Molecular chaperone GRP94 binds to the Fanconi anemia group C protein and regulates its intracellular expression
    • Hoshino T, Wang J, Devetten MP, Iwata N, Kajigaya S, Wise RJ, Liu JM, Youssoufian H (1998) Molecular chaperone GRP94 binds to the Fanconi anemia group C protein and regulates its intracellular expression. Blood 91: 4 379-4 386
    • (1998) Blood , vol.91 , pp. 4379-4386
    • Hoshino, T.1    Wang, J.2    Devetten, M.P.3    Iwata, N.4    Kajigaya, S.5    Wise, R.J.6    Liu, J.M.7    Youssoufian, H.8
  • 9
    • 0027082582 scopus 로고
    • Duck hepatitis B virus polymerase produced by in vitro transcription and translation possesses DNA polymerase and reverse transcriptase activities
    • Howe AY, Elliott JF, Tyrrell DL (1992) Duck hepatitis B virus polymerase produced by in vitro transcription and translation possesses DNA polymerase and reverse transcriptase activities. Biochem Biophys Res Commun 189: 1 170-1 176
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 1170-1176
    • Howe, A.Y.1    Elliott, J.F.2    Tyrrell, D.L.3
  • 10
    • 0030035038 scopus 로고    scopus 로고
    • Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase
    • Hu J, Seeger C (1996) Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase. Proc Natl Acad Sci USA 93: 1 060-1 064
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1060-1064
    • Hu, J.1    Seeger, C.2
  • 11
    • 0031018112 scopus 로고    scopus 로고
    • Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids
    • HuJ, Toft DO, Seeger C (1997) Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids. EMBO J 16:59-68
    • (1997) EMBO J , vol.16 , pp. 59-68
    • Hu, J.1    Toft, D.O.2    Seeger, C.3
  • 12
    • 0027480734 scopus 로고
    • Sequences downstream of the RNA initiation site regulate human T-cell lymphotropic virus type I basal gene expression
    • Kashanchi F, Duvall JF, Lindholm PF, Radonovich MF, Brady JN (1993) Sequences downstream of the RNA initiation site regulate human T-cell lymphotropic virus type I basal gene expression. J Virol 67: 2 894-2 902
    • (1993) J Virol , vol.67 , pp. 2894-2902
    • Kashanchi, F.1    Duvall, J.F.2    Lindholm, P.F.3    Radonovich, M.F.4    Brady, J.N.5
  • 13
    • 0026569212 scopus 로고
    • Interaction of BiP with newly synthesized immunoglobulin light chain molecules: Cycles of sequential binding and release
    • Knittler MR, Haas IG (1992) Interaction of BiP with newly synthesized immunoglobulin light chain molecules: cycles of sequential binding and release. EMBO J 11: 1 573-1 581
    • (1992) EMBO J , vol.11 , pp. 1573-1581
    • Knittler, M.R.1    Haas, I.G.2
  • 14
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi Y, Segal M, Normington K, Gething MJ, Sambrook J (1988) The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332: 462-464
    • (1988) Nature , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.J.4    Sambrook, J.5
  • 15
    • 0025810945 scopus 로고
    • Characterization of DNA metabolizing enzymes in situ following polyacrylamide gel electrophoresis
    • Longley MJ, Mosbaugh DW (1991) Characterization of DNA metabolizing enzymes in situ following polyacrylamide gel electrophoresis. Biochemistry 30: 2 655-2 664
    • (1991) Biochemistry , vol.30 , pp. 2655-2664
    • Longley, M.J.1    Mosbaugh, D.W.2
  • 17
    • 0025354155 scopus 로고
    • Human homologue of murine tumor rejection antigen gp96: 5′-regulatory and coding regions and relationship to stress-induced proteins
    • Maki RG, Old LJ, Srivastava PK (1990) Human homologue of murine tumor rejection antigen gp96: 5′-regulatory and coding regions and relationship to stress-induced proteins. Proc Natl Acad Sci USA 87: 5 658-5 662
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5658-5662
    • Maki, R.G.1    Old, L.J.2    Srivastava, P.K.3
  • 18
    • 0023664518 scopus 로고
    • ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94)
    • Mazzarella RA, Green M (1987) ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94). J Biol Chem 262: 8 875-8 883
    • (1987) J Biol Chem , vol.262 , pp. 8875-8883
    • Mazzarella, R.A.1    Green, M.2
  • 19
    • 0026808864 scopus 로고
    • The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains
    • Melnick J, Aviel S, Argon Y (1992) The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains. J Biol Chem 267: 21 303-21 306
    • (1992) J Biol Chem , vol.267 , pp. 21303-21306
    • Melnick, J.1    Aviel, S.2    Argon, Y.3
  • 20
    • 0028170231 scopus 로고
    • Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
    • Melnick J, Dul JL, Argon Y (1994) Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature 370: 373-375
    • (1994) Nature , vol.370 , pp. 373-375
    • Melnick, J.1    Dul, J.L.2    Argon, Y.3
  • 21
    • 0025784485 scopus 로고
    • A mutation in the ectodomain of herpes simplex virus 1 glycoprotein B causes defective processing and retention in the endoplasmic reticulum
    • Navarro D, Qadri I, Pereira L (1991) A mutation in the ectodomain of herpes simplex virus 1 glycoprotein B causes defective processing and retention in the endoplasmic reticulum. Virology 184: 253-264
    • (1991) Virology , vol.184 , pp. 253-264
    • Navarro, D.1    Qadri, I.2    Pereira, L.3
  • 22
    • 0023916795 scopus 로고
    • Duck hepatitis B virus: DNA polymerase and reverse transcriptase activities of replicative complexes isolated from liver and their inhibition in vitro
    • Offensperger WB, Walter E, Offensperger S, Zeschnigk C, Blum HE, Gerok W (1988) Duck hepatitis B virus: DNA polymerase and reverse transcriptase activities of replicative complexes isolated from liver and their inhibition in vitro. Virology 164: 48-54
    • (1988) Virology , vol.164 , pp. 48-54
    • Offensperger, W.B.1    Walter, E.2    Offensperger, S.3    Zeschnigk, C.4    Blum, H.E.5    Gerok, W.6
  • 23
    • 0028095240 scopus 로고
    • Site-specific RNA binding by a hepatitis B virus reverse transcriptase initiates two distinct reactions: RNA packaging and DNA synthesis
    • Pollack JR, Ganem D (1994) Site-specific RNA binding by a hepatitis B virus reverse transcriptase initiates two distinct reactions: RNA packaging and DNA synthesis. J Virol 68: 5 579-5 587
    • (1994) J Virol , vol.68 , pp. 5579-5587
    • Pollack, J.R.1    Ganem, D.2
  • 24
    • 0027451956 scopus 로고
    • The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor
    • Pratt WB (1993) The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. J Biol Chem 268: 21 455-21 458
    • (1993) J Biol Chem , vol.268 , pp. 21455-21458
    • Pratt, W.B.1
  • 25
    • 0025061039 scopus 로고
    • Mutational analysis of the hepatitis B virus P gene product: Domain structure and RNase H activity
    • Radziwill G, Tucker W, Schaller H (1990) Mutational analysis of the hepatitis B virus P gene product: domain structure and RNase H activity. J Virol 64: 613-620
    • (1990) J Virol , vol.64 , pp. 613-620
    • Radziwill, G.1    Tucker, W.2    Schaller, H.3
  • 26
    • 0019171101 scopus 로고
    • Biochemical and immunological properties of the DNA polymerase and RNAase H activities of purified feline leukemia virus reverse transcriptase
    • Rho HM, Gallo RC (1980) Biochemical and immunological properties of the DNA polymerase and RNAase H activities of purified feline leukemia virus reverse transcriptase. Cancer Lett 10: 207-221
    • (1980) Cancer Lett , vol.10 , pp. 207-221
    • Rho, H.M.1    Gallo, R.C.2
  • 27
    • 0024517420 scopus 로고
    • The nucleotide sequence and reading frames of a mutant hepatitis B virus subtype adr
    • Rho HM, Kim K, Hyun SW, Kim YS (1989) The nucleotide sequence and reading frames of a mutant hepatitis B virus subtype adr. Nucleic Acids Res 17: 2124
    • (1989) Nucleic Acids Res , vol.17 , pp. 2124
    • Rho, H.M.1    Kim, K.2    Hyun, S.W.3    Kim, Y.S.4
  • 28
    • 0025323818 scopus 로고
    • Sequences 5′ to the polyadenylation signal mediate differential poly(A) site use in hepatitis B viruses
    • Russnak R, Ganem D (1990) Sequences 5′ to the polyadenylation signal mediate differential poly(A) site use in hepatitis B viruses. Genes Dev 4: 764-776
    • (1990) Genes Dev , vol.4 , pp. 764-776
    • Russnak, R.1    Ganem, D.2
  • 30
    • 0026742999 scopus 로고
    • HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells
    • Schaiff WT, Hruska KA Jr, McCourt DW, Green M, Schwartz BD (1992) HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells. J Exp Med 176: 657-666
    • (1992) J Exp Med , vol.176 , pp. 657-666
    • Schaiff, W.T.1    Hruska K.A., Jr.2    McCourt, D.W.3    Green, M.4    Schwartz, B.D.5
  • 31
    • 0027164918 scopus 로고
    • Recombinant human hepatitis B virus reverse transcriptase is active in the absence of the nucleocapsid or the viral replication origin, DR1
    • Seifer M, Standring DN (1993) Recombinant human hepatitis B virus reverse transcriptase is active in the absence of the nucleocapsid or the viral replication origin, DR1. J Virol 67: 4 513-4 520
    • (1993) J Virol , vol.67 , pp. 4513-4520
    • Seifer, M.1    Standring, D.N.2
  • 32
    • 0022483344 scopus 로고
    • Foscarnet decreases serum and liver duck hepatitis B virus DNA in chronically infected ducks
    • Sherker AH, Hirota K, Omata M, Okuda K (1986) Foscarnet decreases serum and liver duck hepatitis B virus DNA in chronically infected ducks. Gastroenterology 91: 818-824
    • (1986) Gastroenterology , vol.91 , pp. 818-824
    • Sherker, A.H.1    Hirota, K.2    Omata, M.3    Okuda, K.4
  • 33
    • 0028224526 scopus 로고
    • Expression of recombinant human casein kinase II and recombinant heat shock protein 90 in Escherichia coli and characterization of their interactions
    • Shi Y, Brown ED, Walsh CT (1994) Expression of recombinant human casein kinase II and recombinant heat shock protein 90 in Escherichia coli and characterization of their interactions. Proc Natl Acad Sci USA 91: 2 767-2 771
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2767-2771
    • Shi, Y.1    Brown, E.D.2    Walsh, C.T.3
  • 34
    • 0029019476 scopus 로고
    • Release of the hepatitis B virus-associated DNA polymerase from the viral particle by the proteolytic cleavage
    • Shin HJ, Rho HM (1995) Release of the hepatitis B virus-associated DNA polymerase from the viral particle by the proteolytic cleavage. J Biol Chem 270: 11 047-11 050
    • (1995) J Biol Chem , vol.270 , pp. 11047-11050
    • Shin, H.J.1    Rho, H.M.2
  • 35
    • 0027447541 scopus 로고
    • Steroid receptors and their associated proteins
    • Smith DF, Toft DO (1993) Steroid receptors and their associated proteins. Mol Endocrinol 7: 4-11
    • (1993) Mol Endocrinol , vol.7 , pp. 4-11
    • Smith, D.F.1    Toft, D.O.2
  • 36
    • 0023660117 scopus 로고
    • The glucose-regulated protein grp94 is related to heat shock protein hsp90
    • Sorger PK, Pelham HR (1987) The glucose-regulated protein grp94 is related to heat shock protein hsp90. J Mol Biol 194: 341-344
    • (1987) J Mol Biol , vol.194 , pp. 341-344
    • Sorger, P.K.1    Pelham, H.R.2
  • 37
    • 0019949367 scopus 로고
    • Replication of the genome of a hepatitis B-like virus by reverse transcription of an RNA intermediate
    • Summers J, Mason WS (1982) Replication of the genome of a hepatitis B-like virus by reverse transcription of an RNA intermediate. Cell 29: 403-415
    • (1982) Cell , vol.29 , pp. 403-415
    • Summers, J.1    Mason, W.S.2
  • 38
    • 0027210553 scopus 로고
    • Expression of functional hepatitis B virus polymerase in yeast reveals it to be the sole viral protein required for correct initiation of reverse transcription
    • Tavis JE, Ganem D (1993) Expression of functional hepatitis B virus polymerase in yeast reveals it to be the sole viral protein required for correct initiation of reverse transcription. Proc Natl Acad Sci USA 90: 4 107-4 111
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4107-4111
    • Tavis, J.E.1    Ganem, D.2
  • 39
    • 0029833252 scopus 로고    scopus 로고
    • Evidence for activation of the hepatitis B virus polymerase by binding of its RNA template
    • Tavis JE, Ganem D (1996) Evidence for activation of the hepatitis B virus polymerase by binding of its RNA template. J Virol 70: 5 741-5 750
    • (1996) J Virol , vol.70 , pp. 5741-5750
    • Tavis, J.E.1    Ganem, D.2
  • 40
    • 0031777692 scopus 로고    scopus 로고
    • The duck hepatitis B virus polymerase is activated by its RNA packaging signal, epsilon
    • Tavis JE, Massey B, Gong Y (1998) The duck hepatitis B virus polymerase is activated by its RNA packaging signal, epsilon. J Virol 72: 5 789-5 796
    • (1998) J Virol , vol.72 , pp. 5789-5796
    • Tavis, J.E.1    Massey, B.2    Gong, Y.3
  • 41
    • 0026603594 scopus 로고
    • Single-step purification of bacterially expressed polypeptides containing an oligo-histidine domain
    • Van Dyke MW, Sirito M, Sawadogo M (1992) Single-step purification of bacterially expressed polypeptides containing an oligo-histidine domain. Gene 111: 99-104
    • (1992) Gene , vol.111 , pp. 99-104
    • Van Dyke, M.W.1    Sirito, M.2    Sawadogo, M.3
  • 42
    • 0026493753 scopus 로고
    • The reverse transcriptase of hepatitis B virus acts as a protein primer for viral DNA synthesis
    • Wang G-H, Seeger C (1992) The reverse transcriptase of hepatitis B virus acts as a protein primer for viral DNA synthesis. Cell 71: 663-670
    • (1992) Cell , vol.71 , pp. 663-670
    • Wang, G.-H.1    Seeger, C.2
  • 43
    • 0031797727 scopus 로고    scopus 로고
    • BiP (GRP78) and endoplasmin (GRP94) are induced following rotavirus infection and bind transiently to an endoplasmic reticulum-localized virion component
    • Xu A, Bellamy AR, Taylor JA (1998) BiP (GRP78) and endoplasmin (GRP94) are induced following rotavirus infection and bind transiently to an endoplasmic reticulum-localized virion component. J Virol 72: 9 865-9 872
    • (1998) J Virol , vol.72 , pp. 9865-9872
    • Xu, A.1    Bellamy, A.R.2    Taylor, J.A.3
  • 44
    • 0030756523 scopus 로고    scopus 로고
    • Activation of hepatitis B virus S promoter by the viral large surface protein via induction of stress in the endoplasmic reticulum
    • Xu Z, Jensen G, Yen TS (1997) Activation of hepatitis B virus S promoter by the viral large surface protein via induction of stress in the endoplasmic reticulum. J Virol 71: 7 387-7 392
    • (1997) J Virol , vol.71 , pp. 7387-7392
    • Xu, Z.1    Jensen, G.2    Yen, T.S.3
  • 45
    • 0028091053 scopus 로고
    • Reverse transcription in hepatitis B viruses is primed by a tyrosine residue of the polymerase
    • Zoulim F, Seeger C (1994) Reverse transcription in hepatitis B viruses is primed by a tyrosine residue of the polymerase. J Virol 68: 6-13
    • (1994) J Virol , vol.68 , pp. 6-13
    • Zoulim, F.1    Seeger, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.