메뉴 건너뛰기




Volumn 264, Issue 1, 1999, Pages 106-114

Alternative splice variants of the human PKR protein kinase possessing different 5'-untranslated regions: Expression in untreated and interferon- treated cells and translational activity

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED RNA; INTERFERON; PROTEIN KINASE;

EID: 0033544339     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1999.9995     Document Type: Article
Times cited : (13)

References (43)
  • 1
    • 0023395844 scopus 로고
    • Biosynthesis of reovirus-specified polypeptides: Efficiency of expression of cDNAs of the reovirus S1 and S4 genes in transfected animal cells differs at the level of translation
    • Atwater J. A., Munemitsu S. M., Samuel C. E. Biosynthesis of reovirus-specified polypeptides: Efficiency of expression of cDNAs of the reovirus S1 and S4 genes in transfected animal cells differs at the level of translation. Virology. 159:1987;350-357.
    • (1987) Virology , vol.159 , pp. 350-357
    • Atwater, J.A.1    Munemitsu, S.M.2    Samuel, C.E.3
  • 2
    • 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., George C. X., Samuel C. E., Cech T. R. Binding of the protein kinase PKR to RNAs with secondary structure defects: Role of the tandem A-G mismatch and noncontiguous helixes. Biochemistry. 37:1998;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
  • 3
    • 0022259863 scopus 로고
    • Mechanism of interferon action: The interferon-induced phosphoprotein P1 possesses a double-stranded RNA-dependent ATP-binding site
    • Bischoff J. R., Samuel C. E. Mechanism of interferon action: The interferon-induced phosphoprotein P1 possesses a double-stranded RNA-dependent ATP-binding site. J. Biol. Chem. 260:1985;8237-8239.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8237-8239
    • Bischoff, J.R.1    Samuel, C.E.2
  • 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., Graziano V., Schneider D., Maitra R. K., Lee X., Williams B. R. G. 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. 272:1997;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
    • 0002758687 scopus 로고
    • Marathon cDNA amplification: A new method for cloning full-length cDNAs
    • Chenchik A., Moqadam F., Siebert P. Marathon cDNA amplification: A new method for cloning full-length cDNAs. Clontech. X:1995;5-8.
    • (1995) Clontech , vol.10 , pp. 5-8
    • Chenchik, A.1    Moqadam, F.2    Siebert, P.3
  • 6
    • 0030725442 scopus 로고    scopus 로고
    • The double-stranded RNA-dependent protein kinase PKR: Structure and function
    • Clemens M. J., Elia A. The double-stranded RNA-dependent protein kinase PKR: Structure and function. J. Interfer. Cytokine Res. 17:1997;503-524.
    • (1997) J. Interfer. Cytokine Res. , vol.17 , pp. 503-524
    • Clemens, M.J.1    Elia, A.2
  • 7
    • 0023277545 scopus 로고
    • Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., Sacchi N. Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:1987;156-169.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-169
    • Chomczynski, P.1    Sacchi, N.2
  • 8
    • 0024212067 scopus 로고
    • Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene specific oligonucletide primer
    • Frohman M. A., Dush M. K., Martin G. R. Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene specific oligonucletide primer. Proc. Natl. Acad. Sci. USA. 85:1988;8998-9002.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 9
    • 0033551050 scopus 로고    scopus 로고
    • Human RNA specific adenosine deaminase ADAR1 transcripts possess alternative exon 1 structures that initiate from different promoters, one constitutively active and the other interferon-inducible
    • George C. X., Samuel C. E. Human RNA specific adenosine deaminase ADAR1 transcripts possess alternative exon 1 structures that initiate from different promoters, one constitutively active and the other interferon-inducible. Proc. Natl. Acad. Sci. USA. 96:1999;4621-4626.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4621-4626
    • George, C.X.1    Samuel, C.E.2
  • 10
    • 0024797894 scopus 로고
    • Protein phosphorylation controls translation rates
    • Hershey J. W. B. Protein phosphorylation controls translation rates. J. Biol. Chem. 264:1989;20823-20826.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20823-20826
    • Hershey, J.W.B.1
  • 11
    • 0028815704 scopus 로고
    • Regulation of the interferon-induced PKR: Can viruses cope?
    • Katze M. G. Regulation of the interferon-induced PKR: Can viruses cope? Trends Microbiol. 3:1995;75-78.
    • (1995) Trends Microbiol. , vol.3 , pp. 75-78
    • Katze, M.G.1
  • 13
    • 0029058994 scopus 로고
    • Structure of the dsRNA binding domain of E. coli RNase III
    • Kharrat A., Macias M. J., Gibson T. J., Nilges M., Pastore A. Structure of the dsRNA binding domain of E. coli RNase III. EMBO J. 14:1995;3572-3584.
    • (1995) EMBO J. , vol.14 , pp. 3572-3584
    • Kharrat, A.1    Macias, M.J.2    Gibson, T.J.3    Nilges, M.4    Pastore, A.5
  • 14
    • 0026729831 scopus 로고
    • Regulation of translation in eukaryotic systems
    • Kozak M. Regulation of translation in eukaryotic systems. Annu. Rev. Cell Biol. 8:1992;197-225.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 197-225
    • Kozak, M.1
  • 16
    • 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., Samuel C. E. 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. 227:1997;119-130.
    • (1997) Virology , vol.227 , pp. 119-130
    • Kuhen, K.L.1    Samuel, C.E.2
  • 17
    • 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., Shen X., Carlisle E. R., Richardson A. L., Weier H.-U. G., Tanaka H., Samuel C. E. 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. 36:1996;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
  • 18
    • 0031797452 scopus 로고    scopus 로고
    • 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
    • Kuhen K. L., Vessey J. W., Samuel C. E. 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. J. Virol. 72:1998;9934-9939.
    • (1998) J. Virol. , vol.72 , pp. 9934-9939
    • Kuhen, K.L.1    Vessey, J.W.2    Samuel, C.E.3
  • 19
    • 0033603359 scopus 로고    scopus 로고
    • Serotonin-2C receptor pre-mRNA editing in rat brain and in vitro by splice site variants of the interferon-inducible double-stranded RNA-specific adenosine deaminase ADAR1
    • Liu Y., Emeson R. B., Samuel C. E. Serotonin-2C receptor pre-mRNA editing in rat brain and in vitro by splice site variants of the interferon-inducible double-stranded RNA-specific adenosine deaminase ADAR1. J. Biol. Chem. 274:1999;18351-18358.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18351-18358
    • Liu, Y.1    Emeson, R.B.2    Samuel, C.E.3
  • 20
    • 0033582534 scopus 로고    scopus 로고
    • Editing of glutamate receptor subunit B pre-mRNA by splice-site variants of interferon-inducible dsRNA-specific adenosine deaminase ADAR1
    • Liu Y., Samuel C. E. Editing of glutamate receptor subunit B pre-mRNA by splice-site variants of interferon-inducible dsRNA-specific adenosine deaminase ADAR1. J. Biol. Chem. 274:1999;5070-5077.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5070-5077
    • Liu, Y.1    Samuel, C.E.2
  • 21
    • 0021100710 scopus 로고
    • High efficiency polyoma DNA transfection of chloroquine treated cells
    • Luthman H., Magnusson G. High efficiency polyoma DNA transfection of chloroquine treated cells. Nucleic Acids Res. 11:1983;1295-1308.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1295-1308
    • Luthman, H.1    Magnusson, G.2
  • 23
    • 0026716255 scopus 로고
    • Mechanism of interferon action: Identification of a RNA binding domain within the N-terminal region of the human RNA-dependent P1/eIF-2α protein kinase
    • McCormack S. J., Thomis D. C., Samuel C. E. Mechanism of interferon action: Identification of a RNA binding domain within the N-terminal region of the human RNA-dependent P1/eIF-2α protein kinase. Virology. 188:1992;47-56.
    • (1992) Virology , vol.188 , pp. 47-56
    • McCormack, S.J.1    Thomis, D.C.2    Samuel, C.E.3
  • 24
    • 0025298202 scopus 로고
    • Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon
    • Meurs E., Chong K., Galabru J., Thomas N. S., Kerr I. M., Williams B. R. G., Hovanessian A. G. Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon. Cell. 62:1990;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
  • 25
    • 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., Stanton P. K., Sen G. C. 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. 271:1996;25657-25663.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25657-25663
    • Patel, R.C.1    Stanton, P.K.2    Sen, G.C.3
  • 26
    • 0029164692 scopus 로고
    • Expression and regulation by interferon of a double-stranded-RNA specific adenosine deaminase from human cells: Evidence for two forms of the deaminase
    • Patterson J. B., Samuel C. E. Expression and regulation by interferon of a double-stranded-RNA specific adenosine deaminase from human cells: Evidence for two forms of the deaminase. Mol. Cell. Biol. 15:1995;5376-5388.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5376-5388
    • Patterson, J.B.1    Samuel, C.E.2
  • 27
    • 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., Garcia-Barrio M. T., Zhang X., Wang Q., Taylor D. R., Zhang F., Herring C., Mathews M. B., Qin J., Hinnenbush A. G. 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. 18:1998;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
  • 28
    • 0033529064 scopus 로고    scopus 로고
    • Regulation of alternative splicing by RNA editing
    • Rueter S., Dawson T. R., Emeson R. B. Regulation of alternative splicing by RNA editing. Nature. 399:1999;75-80.
    • (1999) Nature , vol.399 , pp. 75-80
    • Rueter, S.1    Dawson, T.R.2    Emeson, R.B.3
  • 29
    • 0022372670 scopus 로고
    • Enzymatic amplification of β-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia
    • Saiki R. K., Scharf S., Faloona F., Mullis K. B., Horn G. T., Erlich H. A., Arnheim N. Enzymatic amplification of β-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia. Science. 230:1985;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
  • 31
    • 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. 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. 76:1979;600-604.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 600-604
    • Samuel, C.E.1
  • 32
    • 0025739093 scopus 로고
    • Antiviral actions of interferon: Interferon-regulated cellular proteins and their surprisingly selective antiviral activities
    • Samuel C. E. Antiviral actions of interferon: Interferon-regulated cellular proteins and their surprisingly selective antiviral activities. Virology. 183:1991;1-11.
    • (1991) Virology , vol.183 , pp. 1-11
    • Samuel, C.E.1
  • 33
    • 0027418321 scopus 로고
    • The eIF-2α protein kinases, regulators of translation in eukaryotes from yeasts to humans
    • Samuel C. E. The eIF-2α protein kinases, regulators of translation in eukaryotes from yeasts to humans. J. Biol. Chem. 268:1993;7603-7606.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7603-7606
    • Samuel, C.E.1
  • 35
    • 0030893062 scopus 로고    scopus 로고
    • A ribonuclease specific for inosine-containing RNA: A potential role in antiviral defence?
    • Scadden A. D., Smith C. W. A ribonuclease specific for inosine-containing RNA: A potential role in antiviral defence? EMBO J. 16:1997;2140-2149.
    • (1997) EMBO J. , vol.16 , pp. 2140-2149
    • Scadden, A.D.1    Smith, C.W.2
  • 36
    • 0026739463 scopus 로고
    • The interferon system: A bird's eye view of its biochemistry
    • Sen G. C., Lengyel P. The interferon system: A bird's eye view of its biochemistry. J. Biol. Chem. 267:1992;5017-5020.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5017-5020
    • Sen, G.C.1    Lengyel, P.2
  • 38
    • 0027999025 scopus 로고
    • Mechanism of interferon action. Structure of the mouse PKR gene encoding the interferon-inducible RNA-dependent protein kinase
    • Tanaka H., Samuel C. E. Mechanism of interferon action. Structure of the mouse PKR gene encoding the interferon-inducible RNA-dependent protein kinase. Proc. Natl. Acad. Sci. USA. 91:1994;7995-7999.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7995-7999
    • Tanaka, H.1    Samuel, C.E.2
  • 39
    • 0026716253 scopus 로고
    • Mechanism of interferon action: CDNA structure, expression and regulation of the interferon-induced, RNA-dependent Pl/eIF-2α protein kinase from human cells
    • Thomis D. C., Doohan J. P., Samuel C. E. Mechanism of interferon action: cDNA structure, expression and regulation of the interferon-induced, RNA-dependent Pl/eIF-2α protein kinase from human cells. Virology. 188:1992;33-46.
    • (1992) Virology , vol.188 , pp. 33-46
    • Thomis, D.C.1    Doohan, J.P.2    Samuel, C.E.3
  • 40
    • 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., Samuel C. E. Mechanism of interferon action: Evidence for intermolecular autophosphorylation and autoactivation of the interferon-induced, RNA-dependent protein kinase PKR. J. Virol. 67:1993;7695-7700.
    • (1993) J. Virol. , vol.67 , pp. 7695-7700
    • Thomis, D.C.1    Samuel, C.E.2
  • 41
    • 0020479426 scopus 로고
    • Cytoplasmic dot hybridization: Simple analysis of relative mRNA levels in multiple small cell or tissue samples
    • White B. A., Bancroft F. C. Cytoplasmic dot hybridization: Simple analysis of relative mRNA levels in multiple small cell or tissue samples. J. Biol. Chem. 257:1982;8569-8572.
    • (1982) J. Biol. Chem. , vol.257 , pp. 8569-8572
    • White, B.A.1    Bancroft, F.C.2
  • 42
    • 0031849783 scopus 로고    scopus 로고
    • Genomic features of human PKR: Alternative splicing and a polymorphic CGG repeat in the 5′-untranslated region
    • Xu Z., Williams B. R. G. Genomic features of human PKR: Alternative splicing and a polymorphic CGG repeat in the 5′-untranslated region. J. Interfer. Cytokine Res. 18:1998;609-616.
    • (1998) J. Interfer. Cytokine Res. , vol.18 , pp. 609-616
    • Xu, Z.1    Williams, B.R.G.2
  • 43
    • 0027510449 scopus 로고
    • Expression cloning of 2-5A-dependent RNAase: A uniquely regulated mediator of interferon action
    • Zhou A., Hassel B. A., Silverman R. H. Expression cloning of 2-5A-dependent RNAase: A uniquely regulated mediator of interferon action. Cell. 72:1993;753-765.
    • (1993) Cell , vol.72 , pp. 753-765
    • Zhou, A.1    Hassel, B.A.2    Silverman, R.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.