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Volumn 6, Issue 3, 1997, Pages 166-174

Interaction of eukaryotic initiation factor 5A with the human immunodeficiency virus type 1 rev response element RNA and U6 snRNA requires deoxyhypusine or hypusine modification

Author keywords

Deoxyhypusine; Eukaryotic initiation factor 5A; Hypusine; Rev; RNA

Indexed keywords

DEOXYHYPUSINE; HYPUSINE; INITIATION FACTOR; INITIATION FACTOR 5A; REV PROTEIN; REX PROTEIN; RNA BINDING PROTEIN; SMALL NUCLEAR RNA; SYNTHETASE; UNCLASSIFIED DRUG; VIRUS RNA;

EID: 0030863875     PISSN: 1424862X     EISSN: 14248638     Source Type: Journal    
DOI: 10.1159/000109123     Document Type: Article
Times cited : (33)

References (34)
  • 1
    • 0027197906 scopus 로고
    • Hypu-sine: Its post-translational formation in eukaryotic initiation factor 5A and its potential role in cellular regulation
    • Park MH. Wolf TEC, Folk JE: Hypu-sine: Its post-translational formation in eukaryotic initiation factor 5A and its potential role in cellular regulation. Biofactors 1993;4:95-104.
    • (1993) Biofactors , vol.4 , pp. 95-104
    • Park Wolf, M.H.T.1    Folk, J.E.2
  • 2
    • 0020162215 scopus 로고
    • Posttranslational formation of hy-pusine in a single major protein occurs generally in growing cells and is associated with activation of lymphocyte growth
    • Cooper HL, Park MH, Folk JE: Posttranslational formation of hy-pusine in a single major protein occurs generally in growing cells and is associated with activation of lymphocyte growth. Cell 1982:29:791 -797.
    • (1982) Cell , vol.29
    • Cooper, H.L.1    Park, M.H.2    Folk, J.E.3
  • 3
    • 0021108441 scopus 로고
    • An 18,000-dalton protein metabolically labeled by polyamines in various mammalian cell lines
    • Chen KY: An 18,000-dalton protein metabolically labeled by polyamines in various mammalian cell lines. Biochim Biophys Acta 1983;756: 395-402.
    • (1983) Biochim Biophys Acta , vol.756 , pp. 395-402
    • Chen, K.Y.1
  • 6
    • 0023881236 scopus 로고
    • Polyamine metabolism and its importance in neoplastic growth and as a target for chemotherapy
    • Pegg AE: Polyamine metabolism and its importance in neoplastic growth and as a target for chemotherapy. Cancer Res 1988;48:759-774.
    • (1988) Cancer Res , vol.48 , pp. 759-774
    • Pegg, A.E.1
  • 7
    • 0025810272 scopus 로고
    • Translation initiation factor 5A and its hypusine modification arc essential for cell viability in the yeast Saccharomyces cerevisiae
    • Schnier J, Schwelberger HG, Smit-McBride Z, Kang HA, Hershey JWB: Translation initiation factor 5A and its hypusine modification arc essential for cell viability in the yeast Saccharomyces cerevisiae. Mol Cell Biol 1991;11:3105-3114.
    • (1991) Mol Cell Biol , vol.11 , pp. 3105-3114
    • Schnier, J.1    Schwelberger, H.G.2    Smit-McBride, Z.3    Kang, H.A.4    Hershey, J.5
  • 8
    • 0030000577 scopus 로고    scopus 로고
    • Dcoxyhypusine synthase gene is essential for cell viability in the yeast Saccharomyces cerevisiae
    • Sasaki K, Abid MR, Miyazaki M: Dcoxyhypusine synthase gene is essential for cell viability in the yeast Saccharomyces cerevisiae. FEBS Lett 1996;384:151-154.
    • (1996) FEBS Lett , vol.384 , pp. 151-154
    • Sasaki, K.1    Abid, M.R.2    Miyazaki, M.3
  • 9
    • 0018096765 scopus 로고
    • Purification and characterization of protein synthesis initiation factors eIF-1, eIF-4C, eIF-4D, and eIF-5 from rabbit reticulocytes
    • Benne R, Brown-Luedc M, Hershey JWB: Purification and characterization of protein synthesis initiation factors eIF-1, eIF-4C, eIF-4D, and eIF-5 from rabbit reticulocytes. J Biol Chem 1978;253:3070-3077.
    • (1978) J Biol Chem , vol.253 , pp. 3070-3077
    • Benne, R.1    Brown-Luedc, M.2    Hershey, J.3
  • 10
    • 0024418120 scopus 로고
    • The essential role of hypusine in eukaryotic translation initiation factor 4D (ElF-4D). Purification of elF-4D and its precursors and comparison of their activities
    • Park MH: The essential role of hypusine in eukaryotic translation initiation factor 4D (elF-4D). Purification of elF-4D and its precursors and comparison of their activities. J Biol Chem 1989;264:18531-18535.
    • (1989) J Biol Chem , vol.264 , pp. 18531-18535
    • Park, M.H.1
  • 11
    • 0024428107 scopus 로고
    • Protein synthesis initiation factor elF-4D. Functional comparison of native and un-hypusinated forms of the protein
    • Smit-McBride Z, Schnier J, Kaufman RJ, Hershey B: Protein synthesis initiation factor elF-4D. Functional comparison of native and un-hypusinated forms of the protein. J Biol Chem 1989;264:18527-18530.
    • (1989) J Biol Chem , vol.264 , pp. 18527-18530
    • Smit-McBride, Z.1    Schnier, J.2    Kaufman, R.J.3    Hershey, B.4
  • 12
    • 0028145708 scopus 로고
    • Effect of initiation factor elF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae
    • Kang HA, Hershey JWB: Effect of initiation factor elF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae. J Biol Chem 1994;269:3934-3940.
    • (1994) J Biol Chem , vol.269 , pp. 3934-3940
    • Kang, H.A.1    Hershey, J.2
  • 13
    • 0022998702 scopus 로고
    • Changes in eIF-4D hypusine modification or abundance are not correlated with translational repression in HeLa cells
    • Duncan RF, Hershey JW: Changes in eIF-4D hypusine modification or abundance are not correlated with translational repression in HeLa cells. J Biol Chem 1986;261:12903-12906.
    • (1986) J Biol Chem , vol.261 , pp. 12903-12906
    • Duncan, R.F.1    Hershey, J.W.2
  • 14
    • 0023645993 scopus 로고
    • Hypusine formation in eukaryotic initiation factor 4D is not reversed when rates or specificity of protein synthesis is altered
    • Gordon ED, Mora R, Meredith SC, Lindquist SL: Hypusine formation in eukaryotic initiation factor 4D is not reversed when rates or specificity of protein synthesis is altered. J Biol Chem 1987;262:16590-16595.
    • (1987) J Biol Chem , vol.262 , pp. 16590-16595
    • Gordon, E.D.1    Mora, R.2    Meredith, S.C.3    Lindquist, S.L.4
  • 16
    • 85025541875 scopus 로고
    • Regulation of human immunodeficiency virus replication
    • Cullen BR: Regulation of human immunodeficiency virus replication. Annu Rev Microbiol 1991; 380:209-214.
    • (1991) Annu Rev Microbiol , vol.380 , pp. 209-214
    • Cullen, B.R.1
  • 17
    • 0028290825 scopus 로고
    • Control of RNA initiation and elongation at the HIV-1 promoter
    • Jones KA, Peterlin BM: Control of RNA initiation and elongation at the HIV-1 promoter. Annu Rev Bio-chem 1994;63:717-743.
    • (1994) Annu Rev Bio-Chem , vol.63 , pp. 717-743
    • Jones, K.A.1    Peterlin, B.M.2
  • 18
    • 0028922123 scopus 로고
    • Effects of translational initiation factor cIF-5A on the functioning of human T-cell leukemia virus type 1 Rex and human immunodeficiency virus Rev inhibited trans-dominant-ly by a Rex mutant deficient in RNA binding
    • Katahira J, Ishizaki T, Sakai H, Ad-achi A, Yamamoto K, Shida H: Effects of translational initiation factor cIF-5A on the functioning of human T-cell leukemia virus type 1 Rex and human immunodeficiency virus Rev inhibited trans-dominant-ly by a Rex mutant deficient in RNA binding. J Virol 1995;69:3125-3133.
    • (1995) J Virol , vol.69 , pp. 3125-3133
    • Katahira, J.1    Ishizaki, T.2    Sakai, H.3    Ad-Achi, A.4    Yamamoto, K.5    Shida, H.6
  • 19
    • 0026705268 scopus 로고
    • A fraction of the mRNA 5' cap-binding protein, eukaryotic initiation factor 4E, localizes to the nucleus
    • Lejbkowiez F, Goyer C, Darvcau A, Neron S, Lemieux R, Sonenberg N: A fraction of the mRNA 5' cap-binding protein, eukaryotic initiation factor 4E, localizes to the nucleus. Proc Natl Acad Sci USA 1992; 89:9612-9616.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9612-9616
    • Lejbkowiez, F.1    Goyer, C.2    Darvcau, A.3    Neron, S.4    Lemieux, R.5    Sonenberg, N.6
  • 21
    • 0025190644 scopus 로고
    • HIV-1 structural gene expression requires binding of the Rev trans-activator to its RNA target sequence
    • Malim MH, Tiley LS, McCam DF, Rusche JR, Hauber J, Cullen BR: HIV-1 structural gene expression requires binding of the Rev trans-activator to its RNA target sequence. Cell 1990;60:675-683.
    • (1990) Cell , vol.60 , pp. 675-683
    • Malim, M.H.1    Tiley, L.S.2    McCam, D.F.3    Rusche, J.R.4    Hauber, J.5    Cullen, B.R.6
  • 22
    • 0029295578 scopus 로고    scopus 로고
    • The influenza virus NS1 protein binds to a specific region in human U6 snRNA and inhibits U6-U2 andU6-U4 snRNA interactions during splicing
    • Qiu Y, Nemeroff M, Krug RM: The influenza virus NS1 protein binds to a specific region in human U6 snRNA and inhibits U6-U2 andU6-U4 snRNA interactions during splicing. RNA 1996;1:304-316.
    • (1996) RNA , vol.1 , pp. 304-316
    • Qiu, Y.1    Nemeroff, M.2    Krug, R.M.3
  • 23
    • 0025166385 scopus 로고
    • HIV-1 regulator of viron expression (Rev) protein binds to an RNA stem loop structure located within the Rev response element region
    • Hcaphy S, Dingwall C, Emberg I, Gait M, Green SM, Kam J, Lowe AD, Singh M, Skinner MA: HIV-1 regulator of viron expression (Rev) protein binds to an RNA stem loop structure located within the Rev response element region. Cell 1990; 60:685-693.
    • (1990) Cell , vol.60 , pp. 685-693
    • Hcaphy, S.1    Dingwall, C.2    Emberg, I.3    Gait, M.4    Green, S.M.5    Kam, J.6    Lowe, A.D.7    Singh, M.8    Skinner, M.A.9
  • 24
    • 0028102463 scopus 로고
    • PCR-bascd cloning of the full-length Neurospora eukaryotic initiation factor 5A cDNA: Polvhistidine-tagging and overexpression for protein affinity binding
    • Tao Y, Chen KY: PCR-bascd cloning of the full-length Neurospora eukaryotic initiation factor 5A cDNA: Polvhistidine-tagging and overexpression for protein affinity binding. Biochem J 1994:302:517-525.
    • (1994) Biochem J , vol.302 , pp. 517-525
    • Tao, Y.1    Chen, K.Y.2
  • 25
    • 0028852113 scopus 로고
    • Isolation and structural characterization of different isoforms of the hypusine-containing protein c!F-5A from HcLa cells
    • Klier H, Csonga R, Joao HC, Eck-erskom C, Auer M, Lottspeich F, Eder J: Isolation and structural characterization of different isoforms of the hypusine-containing protein c!F-5A from HcLa cells. Biochemistry 1995;34:14693-14702.
    • (1995) Biochemistry , vol.34 , pp. 14693-14702
    • Klier, H.1    Csonga, R.2    Joao, H.C.3    Eck-Erskom, C.4    Auer, M.5    Lottspeich, F.6    Eder, J.7
  • 26
    • 0025949412 scopus 로고
    • Nuclear targeting sequence - a consensus?
    • Dingall C, Laskey RA: Nuclear targeting sequence - a consensus? TIBS 1991;16:478-481.
    • (1991) TIBS , vol.16 , pp. 478-481
    • Dingall, C.1    Laskey, R.A.2
  • 27
    • 0029130169 scopus 로고
    • The HIV-I Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
    • Fisher U, Huber J, Boelens WC, Mattaj IW, Luhrmann R: The HIV-I Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell 1995;82:475-483.
    • (1995) Cell , vol.82 , pp. 475-483
    • Fisher, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Luhrmann, R.5
  • 28
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • Wen W, Meinkoth JL, Tsien RY, Taylor SS: Identification of a signal for rapid export of proteins from the nucleus. Cell 1995;82:463-473.
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinkoth, J.L.2    Tsien, R.Y.3    Taylor, S.S.4
  • 29
    • 0028080261 scopus 로고
    • The leucine-rich repeat: A versatile binding motif
    • Kobe B, Deisenhofer J: The leucine-rich repeat: A versatile binding motif. Trends Biochem Sci 1994; 19: 415-420.
    • (1994) Trends Biochem Sci , vol.19 , pp. 415-420
    • Kobe, B.1    Deisenhofer, J.2
  • 31
    • 0015524802 scopus 로고
    • Cohen SS: 4-Thiouridinc and the conformation of E. Coli tRNA induced by spermidine
    • Pochon F, Cohen SS: 4-Thiouridinc and the conformation of E. coli tRNA induced by spermidine. Bio-chem Biophys Res Commun 1973; 47:720-726.
    • (1973) Bio-Chem Biophys Res Commun , vol.47 , pp. 720-726
    • Pochon, F.1
  • 32
    • 0025818452 scopus 로고
    • HIV-1 structural gene expression requires the binding of multiple Rev monomers to the viral RRE: Implications for HIV-1 latency
    • Malim MH, Cullen BR: HIV-1 structural gene expression requires the binding of multiple Rev monomers to the viral RRE: Implications for HIV-1 latency. Cell 1991;65: 241-248.
    • (1991) Cell , vol.65 , pp. 241-248
    • Malim, M.H.1    Cullen, B.R.2
  • 33
    • 0028274131 scopus 로고
    • The influenza virus NS1 protein is a poly(A)-binding protein that inhibits nuclear transport of mRNAs containing poly(A)
    • Qiu Y, Krug RM: The influenza virus NS1 protein is a poly(A)-binding protein that inhibits nuclear transport of mRNAs containing poly(A). J Virol 1994;68:2425-2432.
    • (1994) J Virol , vol.68 , pp. 2425-2432
    • Qiu, Y.1    Krug, R.M.2
  • 34
    • 0028209823 scopus 로고
    • Two functional domains of the influenza virus NS1 protein are required for regulation of nuclear export of mRNA
    • Qian X-Y, Alonso-Caplen F, Krug RM: Two functional domains of the influenza virus NS1 protein are required for regulation of nuclear export of mRNA. J Virol 1994:68: 2433-2441.
    • (1994) J Virol , vol.68 , pp. 2433-2441
    • Qian, X.-Y.1    Alonso-Caplen, F.2    Krug, R.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.