메뉴 건너뛰기




Volumn 72, Issue 12, 1998, Pages 9934-9939

Mechanism of interferon action: Identification of essential positions within the novel 15-base-pair KCS element required for transcriptional activation of the RNA-dependent protein kinase pkr gene

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA INTERFERON; CHLORAMPHENICOL ACETYLTRANSFERASE; CYTOKINE; PROTEIN KINASE; RNA;

EID: 0031797452     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.72.12.9934-9939.1998     Document Type: Article
Times cited : (39)

References (41)
  • 1
    • 0027231434 scopus 로고
    • Translational regulation by the interferon-induced double-stranded RNA-activated 68-kDa protein kinase
    • Barber, G. N., M. Wambach, M. L. Wong, T. E. Dever, A. G. Hinnebusch, and M. G. Katze. 1993. Translational regulation by the interferon-induced double-stranded RNA-activated 68-kDa protein kinase. Proc. Natl. Acad. Sci. USA 90:4621-4625.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4621-4625
    • Barber, G.N.1    Wambach, M.2    Wong, M.L.3    Dever, T.E.4    Hinnebusch, A.G.5    Katze, M.G.6
  • 2
    • 0031014063 scopus 로고    scopus 로고
    • Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR
    • Benkirane, M., C. Neurveut, R. F. Chun, S. M. Smith, C. E. Samuel, A. Gatignol, and K.-T. Jeang. 1997. Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR. EMBO J. 16:611-624.
    • (1997) EMBO J. , vol.16 , pp. 611-624
    • Benkirane, M.1    Neurveut, C.2    Chun, R.F.3    Smith, S.M.4    Samuel, C.E.5    Gatignol, A.6    Jeang, K.-T.7
  • 3
    • 0032485912 scopus 로고    scopus 로고
    • Binding of the protein kinase PKR to RNAs with secondary structure defects: Role of the tandem A-G mismatch and noncontiguous helixes
    • Bevilacqua, P. C., C. X. George, C. E. Samuel, and T. R. Cech. 1998. Binding of the protein kinase PKR to RNAs with secondary structure defects: role of the tandem A-G mismatch and noncontiguous helixes. Biochemistry 37: 6303-6316.
    • (1998) Biochemistry , vol.37 , pp. 6303-6316
    • Bevilacqua, P.C.1    George, C.X.2    Samuel, C.E.3    Cech, T.R.4
  • 4
    • 0030989529 scopus 로고    scopus 로고
    • Characterization of the solution complex between the interferon-induced, double-stranded RNA-activated protein kinase and HIV-1 trans-activating region RNA
    • Carpick, B. W., V. Graziano, D. Schneider, R. K. Maitra, X. Lee, and B. R. G. Williams. 1997. Characterization of the solution complex between the interferon-induced, double-stranded RNA-activated protein kinase and HIV-1 trans-activating region RNA. J. Biol. Chem. 272:9510-9516.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9510-9516
    • Carpick, B.W.1    Graziano, V.2    Schneider, D.3    Maitra, R.K.4    Lee, X.5    Williams, B.R.G.6
  • 5
    • 0030725442 scopus 로고    scopus 로고
    • The double-stranded RNA-dependent protein kinase PKR: Structure and function
    • Clemens, M. J., and A. Elia. 1997. The double-stranded RNA-dependent protein kinase PKR: structure and function. J. Interferon Cytokine Res. 17:503-524.
    • (1997) J. Interferon Cytokine Res. , vol.17 , pp. 503-524
    • Clemens, M.J.1    Elia, A.2
  • 7
    • 0030840464 scopus 로고    scopus 로고
    • STATs and gene regulation
    • Darnell, J. E. 1997. STATs and gene regulation. Science 277:1630-1635.
    • (1997) Science , vol.277 , pp. 1630-1635
    • Darnell, J.E.1
  • 8
    • 0028234529 scopus 로고
    • Jak-STAT pathways and trancriptional activation in response to IFNs and other extracellular signaling proteins
    • Darnell, J. E., I. M. Kerr, and G. R. Stark. 1994. Jak-STAT pathways and trancriptional activation in response to IFNs and other extracellular signaling proteins. Science 264:1415-1421.
    • (1994) Science , vol.264 , pp. 1415-1421
    • Darnell, J.E.1    Kerr, I.M.2    Stark, G.R.3
  • 10
    • 0024797894 scopus 로고
    • Protein phosphorylation controls translation rates
    • Hershey, J. W. B. 1989. Protein phosphorylation controls translation rates. J. Biol. Chem. 264:20823-20826.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20823-20826
    • Hershey, J.W.B.1
  • 11
    • 0030586859 scopus 로고    scopus 로고
    • Mechanism of interferon action. Structural organization of the human Pkr gene encoding an interferon-inducible RNA-dependent protein kinase (PKR) and differences from its mouse homolog
    • Kuhen, K. L., X. Shen, E. R. Carlisle, A. L. Richardson, H.-U. G. Weier, H. Tanaka, and C. E. Samuel. 1996. Mechanism of interferon action. Structural organization of the human Pkr gene encoding an interferon-inducible RNA-dependent protein kinase (PKR) and differences from its mouse homolog. Genomics 36:197-201.
    • (1996) Genomics , vol.36 , pp. 197-201
    • Kuhen, K.L.1    Shen, X.2    Carlisle, E.R.3    Richardson, A.L.4    Weier, H.-U.G.5    Tanaka, H.6    Samuel, C.E.7
  • 12
    • 0031555628 scopus 로고    scopus 로고
    • Isolation of the interferon-inducible RNA-dependent protein kinase Pkr promoter and identification of a novel DNA element within the 5′-flanking region of the human and mouse Pkr genes
    • Kuhen, K. L., and C. E. Samuel. 1997. Isolation of the interferon-inducible RNA-dependent protein kinase Pkr promoter and identification of a novel DNA element within the 5′-flanking region of the human and mouse Pkr genes. Virology 227:119-130.
    • (1997) Virology , vol.227 , pp. 119-130
    • Kuhen, K.L.1    Samuel, C.E.2
  • 13
    • 17444449609 scopus 로고    scopus 로고
    • Deficient cytokine signaling in mouse embryo fibroblasts with a targeted deletion in the PKR gene: Role of IRF-1 and NF-κB
    • Kumar, A., Y.-L. Yang, V. Flati, S. Der, S. Kadereit, A. Deb, J. Haque, L. Reis, C. Weissman and B. R. G. Williams. 1997. Deficient cytokine signaling in mouse embryo fibroblasts with a targeted deletion in the PKR gene: role of IRF-1 and NF-κB. EMBO J. 16:406-416.
    • (1997) EMBO J. , vol.16 , pp. 406-416
    • Kumar, A.1    Yang, Y.-L.2    Flati, V.3    Der, S.4    Kadereit, S.5    Deb, A.6    Haque, J.7    Reis, L.8    Weissman, C.9    Williams, B.R.G.10
  • 14
    • 0027496739 scopus 로고
    • Genomic structure and regulation of the promoter of the rat insulin-like growth factor binding protein-2 gene
    • Kutoh, E., J. B. Margot, and J. Schwander. 1993. Genomic structure and regulation of the promoter of the rat insulin-like growth factor binding protein-2 gene. Mol. Endocrinol. 7:1205-1216.
    • (1993) Mol. Endocrinol. , vol.7 , pp. 1205-1216
    • Kutoh, E.1    Margot, J.B.2    Schwander, J.3
  • 15
    • 0027949937 scopus 로고
    • The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins
    • Lee, T. G., N. Tang, S. Thompson, J. Miller, and M. G. Katze. 1994. The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins. Mol. Cell. Biol. 14:2331-2342.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2331-2342
    • Lee, T.G.1    Tang, N.2    Thompson, S.3    Miller, J.4    Katze, M.G.5
  • 16
    • 0027178076 scopus 로고
    • Tumor-suppressor genes: News about the interferon connection
    • Lengyel, P. 1993. Tumor-suppressor genes: news about the interferon connection. Proc. Natl. Acad. Sci. USA 90:5893-5895.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5893-5895
    • Lengyel, P.1
  • 17
    • 0021100710 scopus 로고
    • High efficiency polyoma DNA transfection of chloroquine treated cells
    • Luthman, H., and G. Magnusson. 1983. High efficiency polyoma DNA transfection of chloroquine treated cells. Nucleic Acids Res. 11:1295-1308.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1295-1308
    • Luthman, H.1    Magnusson, G.2
  • 18
    • 0026716255 scopus 로고
    • Mechanism of interferon action. Identification of an RNA binding domain within the N-terminal region of the human RNA-dependent P1/eIF-2α protein kinase
    • McCormack, S. J., D. C. Thomis, and C. E. Samuel 1992. Mechanism of interferon action. Identification of an RNA binding domain within the N-terminal region of the human RNA-dependent P1/eIF-2α protein kinase. Virology 188:47-56.
    • (1992) Virology , vol.188 , pp. 47-56
    • McCormack, S.J.1    Thomis, D.C.2    Samuel, C.E.3
  • 19
    • 0025298202 scopus 로고
    • Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon
    • Meurs, E., K. Chong, J. Galabru, N. S. Thomas, I. M. Kerr, B. R. G. Williams, and A. G. Hovanessian. 1990. Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon. Cell 62:379-390.
    • (1990) Cell , vol.62 , pp. 379-390
    • Meurs, E.1    Chong, K.2    Galabru, J.3    Thomas, N.S.4    Kerr, I.M.5    Williams, B.R.G.6    Hovanessian, A.G.7
  • 20
    • 0030030724 scopus 로고    scopus 로고
    • Mechanism of interferon action. Biochemical and genetic evidence for the intermolecular association of the RNA-dependent protein kinase PKR from human cells
    • Ortega, L. G., M. D. McCotter, G. L. Henry, S. J. MacCormack, D. C. Thomis, and C. E. Samuel. 1996. Mechanism of interferon action. Biochemical and genetic evidence for the intermolecular association of the RNA-dependent protein kinase PKR from human cells. Virology 215:31-39.
    • (1996) Virology , vol.215 , pp. 31-39
    • Ortega, L.G.1    McCotter, M.D.2    Henry, G.L.3    MacCormack, S.J.4    Thomis, D.C.5    Samuel, C.E.6
  • 21
    • 0029841348 scopus 로고    scopus 로고
    • Specific mutations near the amino terminus of double-stranded RNA-dependent protein kinase (PKR) differentially affect its double-stranded RNA binding and dimerization properties
    • Patel, R. C., P. K. Stanton, and G. C. Sen. 1996. Specific mutations near the amino terminus of double-stranded RNA-dependent protein kinase (PKR) differentially affect its double-stranded RNA binding and dimerization properties. J. Biol. Chem. 271:25657-25663.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25657-25663
    • Patel, R.C.1    Stanton, P.K.2    Sen, G.C.3
  • 22
    • 0028971143 scopus 로고
    • Matind and Matinspector - New fast and versatile tools for detection of consensus matches in nucleotide sequence data
    • Quandt, K., C. Frech, H. Karas, E. Wingender, and T. Weiner. 1995. Matind and Matinspector - new fast and versatile tools for detection of consensus matches in nucleotide sequence data. Nucleic Acids Res. 23:4878-4884.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4878-4884
    • Quandt, K.1    Frech, C.2    Karas, H.3    Wingender, E.4    Weiner, T.5
  • 23
    • 0029061508 scopus 로고
    • Tyrosine-phosphorylated Stat1 and Stat2 plus a 48-kDa protein all contact DNA in forming the interferon-stimulated-gene factor 3
    • Qureshi, S. A., M. Salditt-Georgieff, and J. E. Darnell. 1995. Tyrosine-phosphorylated Stat1 and Stat2 plus a 48-kDa protein all contact DNA in forming the interferon-stimulated-gene factor 3. Proc. Natl. Acad. Sci. USA 92:3829-3833.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3829-3833
    • Qureshi, S.A.1    Salditt-Georgieff, M.2    Darnell, J.E.3
  • 24
    • 0031899816 scopus 로고    scopus 로고
    • Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2α kinases PKR and GCN2
    • Romano, P. R., M. T. Garcia-Barrio, X. Zhang, Q. Wang, D. R. Taylor, F. Zhang, C. Herring, M. B. Mathews, J. Qin, and A. G. Hinnenbush. 1998. Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2α kinases PKR and GCN2. Mol. Cell Biol. 18:2282-2297.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 2282-2297
    • Romano, P.R.1    Garcia-Barrio, M.T.2    Zhang, X.3    Wang, Q.4    Taylor, D.R.5    Zhang, F.6    Herring, C.7    Mathews, M.B.8    Qin, J.9    Hinnenbush, A.G.10
  • 25
    • 0022372670 scopus 로고
    • Enzymatic amplification of β-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia
    • Saiki, R. K., S. Scharf, F. Faloona, K. B. Mullis, G. T. Horn, H. A. Erlich, and N. Arnheim. 1985. Enzymatic amplification of β-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia. Science 230:1350-1354.
    • (1985) Science , vol.230 , pp. 1350-1354
    • Saiki, R.K.1    Scharf, S.2    Faloona, F.3    Mullis, K.B.4    Horn, G.T.5    Erlich, H.A.6    Arnheim, N.7
  • 27
    • 0040350202 scopus 로고
    • Mechanism of interferon action. Phosphorylation of protein synthesis initiation factor eIF-2 in interferon-treated human cells by a ribosome-associated protein kinase possessing site-specificity similar to hemin-regulated rabbit reticulocyte kinase
    • Samuel, C. E. 1979. Mechanism of interferon action. Phosphorylation of protein synthesis initiation factor eIF-2 in interferon-treated human cells by a ribosome-associated protein kinase possessing site-specificity similar to hemin-regulated rabbit reticulocyte kinase. Proc. Natl. Acad. Sci. USA 76: 600-604.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 600-604
    • Samuel, C.E.1
  • 28
    • 0025739093 scopus 로고
    • Antiviral actions of interferon. Interferon-regulated cellular proteins and their surprisingly selective antiviral activities
    • Samuel, C. E. 1991. Antiviral actions of interferon. Interferon-regulated cellular proteins and their surprisingly selective antiviral activities. Virology 183:1-11.
    • (1991) Virology , vol.183 , pp. 1-11
    • Samuel, C.E.1
  • 29
    • 0027418321 scopus 로고
    • The eIF-2α protein kinases, regulators of translation in eukaryotes from yeasts to humans
    • Samuel, C. E. 1993. The eIF-2α protein kinases, regulators of translation in eukaryotes from yeasts to humans. J. Biol. Chem. 268:7603-7606.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7603-7606
    • Samuel, C.E.1
  • 31
    • 0029069145 scopus 로고
    • Transcriptional responses to polypeptide ligands. The Jak-STAT pathway
    • Schindler, C., and J. E. Darnell. 1995. Transcriptional responses to polypeptide ligands. The Jak-STAT pathway. Annu. Rev. Biochem. 64:621-651.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 621-651
    • Schindler, C.1    Darnell, J.E.2
  • 32
    • 0026739463 scopus 로고
    • The interferon system: A bird's eye view of its biochemistry
    • Sen, G. C., and P. Lengyel. 1992. The interferon system: a bird's eye view of its biochemistry. J. Biol. Chem. 267:5017-5020.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5017-5020
    • Sen, G.C.1    Lengyel, P.2
  • 33
    • 0027999025 scopus 로고
    • Mechanism of interferon action. Structure of the mouse PKR gene encoding the interferon-inducible RNA-dependent protein kinase
    • Tanaka, H., and C. E. Samuel. 1994. Mechanism of interferon action. Structure of the mouse PKR gene encoding the interferon-inducible RNA-dependent protein kinase. Proc. Natl. Acad. Sci. USA 91:7995-7999.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7995-7999
    • Tanaka, H.1    Samuel, C.E.2
  • 34
    • 3643145929 scopus 로고    scopus 로고
    • Tanaka, H., and C. E. Samuel. Unpublished data
    • Tanaka, H., and C. E. Samuel. Unpublished data.
  • 35
    • 10244257563 scopus 로고    scopus 로고
    • Autophosphorylation sites participate in the activation of the double-stranded RNA-activated protein kinase
    • Taylor, D. R., S. B. Lee, P. R. Romano, D. R. Marshak, A. G. Hinnenbush, M. Esteban, and M. B. Mathews. 1996. Autophosphorylation sites participate in the activation of the double-stranded RNA-activated protein kinase. Mol. Cell Biol. 16:6295-6302.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 6295-6302
    • Taylor, D.R.1    Lee, S.B.2    Romano, P.R.3    Marshak, D.R.4    Hinnenbush, A.G.5    Esteban, M.6    Mathews, M.B.7
  • 36
    • 0026716253 scopus 로고
    • Mechanism of interferon action. cDNA structure, expression and regulation of the interferon-induced, RNA-dependent P1/eIF-2α protein kinase from human cells
    • Thomis, D. C., J. P. Doohan, and C. E. Samuel. 1992. Mechanism of interferon action. cDNA structure, expression and regulation of the interferon-induced, RNA-dependent P1/eIF-2α protein kinase from human cells. Virology 188:33-46.
    • (1992) Virology , vol.188 , pp. 33-46
    • Thomis, D.C.1    Doohan, J.P.2    Samuel, C.E.3
  • 37
    • 0026442274 scopus 로고
    • Mechanism of interferon action: Autoregulation of RNA-dependent P1/eIF-2α protein kinase (PKR) expression in transfected mammalian cells
    • Thomis, D. C., and C. E. Samuel. 1992. Mechanism of interferon action: autoregulation of RNA-dependent P1/eIF-2α protein kinase (PKR) expression in transfected mammalian cells. Proc. Natl. Acad. Sci. USA 89:10837-10841.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10837-10841
    • Thomis, D.C.1    Samuel, C.E.2
  • 38
    • 0027420488 scopus 로고
    • Mechanism of interferon action: Evidence for intermolecular autophosphorylation and autoactivation of the interferon-induced, RNA-dependent protein kinase PKR
    • Thomis, D. C., and C. E. Samuel. 1993. Mechanism of interferon action: evidence for intermolecular autophosphorylation and autoactivation of the interferon-induced, RNA-dependent protein kinase PKR. J. Virol. 67:7695-7700.
    • (1993) J. Virol. , vol.67 , pp. 7695-7700
    • Thomis, D.C.1    Samuel, C.E.2
  • 39
    • 0025797722 scopus 로고
    • Transcriptional regulation of interferon-stimulated genes
    • Williams, B. R. G. 1991. Transcriptional regulation of interferon-stimulated genes. Eur. J. Biochem. 200:1-11
    • (1991) Eur. J. Biochem. , vol.200 , pp. 1-11
    • Williams, B.R.G.1
  • 40
    • 0343852938 scopus 로고    scopus 로고
    • Physical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathways
    • Wong, A. H.-T., N. W. N. Tam, Y.-L. Yang, A. R. Cuddihy, S. Li, S. Kirchoff, H. Hauser, T. Decker, and A. E. Koromilas. 1997. Physical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathways. EMBO J. 16:1291-1304.
    • (1997) EMBO J. , vol.16 , pp. 1291-1304
    • Wong, A.H.-T.1    Tam, N.W.N.2    Yang, Y.-L.3    Cuddihy, A.R.4    Li, S.5    Kirchoff, S.6    Hauser, H.7    Decker, T.8    Koromilas, A.E.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.