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Volumn 88, Issue 3, 2014, Pages 1473-1483

Differential role for host translation factors in host and viral protein synthesis during human cytomegalovirus infection

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR 4F; VIRUS MESSENGER RNA;

EID: 84892454259     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02321-13     Document Type: Article
Times cited : (24)

References (46)
  • 1
    • 0020494571 scopus 로고
    • Protein synthesis initiation factors from human HeLa cells and rabbit reticulocytes are similar: comparison of protein structure, activities, and immunochemical properties
    • Brown-Luedi ML, Meyer LJ, Milburn SC, Yau PM, Corbett S, Hershey JW. 1982. Protein synthesis initiation factors from human HeLa cells and rabbit reticulocytes are similar: comparison of protein structure, activities, and immunochemical properties. Biochemistry 21:4202-4206. http://dx .doi.org/10.1021/bi00261a002.
    • (1982) Biochemistry , vol.21 , pp. 4202-4206
    • Brown-Luedi, M.L.1    Meyer, L.J.2    Milburn, S.C.3    Yau, P.M.4    Corbett, S.5    Hershey, J.W.6
  • 2
    • 0032834055 scopus 로고    scopus 로고
    • eIF4 initiation factors: effec-tors of mRNA recruitment to ribosomes and regulators of translation
    • Gingras AC, Raught B, Sonenberg N. 1999. eIF4 initiation factors: effec-tors of mRNA recruitment to ribosomes and regulators of translation. Annu. Rev. Biochem. 68:913-963. http://dx.doi.org/10.1146/annurev .biochem.68.1.913.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 913-963
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 4
    • 0016680603 scopus 로고
    • 5'-Terminal 7-methylguanosine in eukaryotic mRNA is required for translation
    • Muthukrishnan S, Both GW, Furuichi Y, Shatkin AJ. 1975. 5'-Terminal 7-methylguanosine in eukaryotic mRNA is required for translation. Nature 255:33-37. http://dx.doi.org/10.1038/255033a0.
    • (1975) Nature , vol.255 , pp. 33-37
    • Muthukrishnan, S.1    Both, G.W.2    Furuichi, Y.3    Shatkin, A.J.4
  • 5
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson RJ, Hellen CU, Pestova TV. 2010. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat. Rev. Mol. Cell. Biol. 11:113-127. http://dx.doi.org/10.1038/nrm2838.
    • (2010) Nat. Rev. Mol. Cell. Biol. , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 6
    • 0018516382 scopus 로고
    • Eukaryotic mRNA cap binding protein: purification by affinity chromatography on Sepharose-coupled m7GDP
    • Sonenberg N, Rupprecht KM, Hecht SM, Shatkin AJ. 1979. Eukaryotic mRNA cap binding protein: purification by affinity chromatography on Sepharose-coupled m7GDP. Proc. Natl. Acad. Sci. U.S.A. 76:4345-4349. http://dx.doi.org/10.1073/pnas.76.9.4345.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4345-4349
    • Sonenberg, N.1    Rupprecht, K.M.2    Hecht, S.M.3    Shatkin, A.J.4
  • 7
    • 0020479045 scopus 로고
    • Characterization of eukaryotic initiation factor 4A, a protein involved in ATP-dependent binding of globin mRNA
    • Grifo JA, Tahara SM, Leis JP, Morgan MA, Shatkin AJ, Merrick WC. 1982. Characterization of eukaryotic initiation factor 4A, a protein involved in ATP-dependent binding of globin mRNA. J. Biol. Chem. 257: 5246-5252.
    • (1982) J. Biol. Chem. , vol.257 , pp. 5246-5252
    • Grifo, J.A.1    Tahara, S.M.2    Leis, J.P.3    Morgan, M.A.4    Shatkin, A.J.5    Merrick, W.C.6
  • 9
    • 0035134520 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus vCyclin open reading frame contains an internal ribosome entry site
    • Bieleski L, Talbot SJ. 2001. Kaposi's sarcoma-associated herpesvirus vCyclin open reading frame contains an internal ribosome entry site. J. Virol. 75:1864-1869. http://dx.doi.org/10.1128/JVI.75.4.1864-1869.2001.
    • (2001) J. Virol. , vol.75 , pp. 1864-1869
    • Bieleski, L.1    Talbot, S.J.2
  • 10
    • 77956044600 scopus 로고    scopus 로고
    • Stress-inducible alternative translation initiation of human cytomegalovirus latency protein pUL138
    • Grainger L, Cicchini L, Rak M, Petrucelli A, Fitzgerald KD, Semler BL, Goodrum F. 2010. Stress-inducible alternative translation initiation of human cytomegalovirus latency protein pUL138. J. Virol. 84:9472-9486. http://dx.doi.org/10.1128/JVI.00855-10.
    • (2010) J. Virol. , vol.84 , pp. 9472-9486
    • Grainger, L.1    Cicchini, L.2    Rak, M.3    Petrucelli, A.4    Fitzgerald, K.D.5    Semler, B.L.6    Goodrum, F.7
  • 11
    • 0035136288 scopus 로고    scopus 로고
    • Mechanisms governing expression of the v-FLIP gene of Kaposi's sarcoma-associated herpesvirus
    • Grundhoff A, Ganem D. 2001. Mechanisms governing expression of the v-FLIP gene of Kaposi's sarcoma-associated herpesvirus. J. Virol. 75: 1857-1863. http://dx.doi.org/10.1128/JVI.75.4.1857-1863.2001.
    • (2001) J. Virol. , vol.75 , pp. 1857-1863
    • Grundhoff, A.1    Ganem, D.2
  • 12
    • 3142688963 scopus 로고    scopus 로고
    • A posttranscriptional regulator of Kaposi's sarcoma-associated herpesvirus interacts with RNA-binding protein PCBP1 and controls gene expression through the IRES
    • Nishimura K, Ueda K, Guwanan E, Sakakibara S, Do E, Osaki E, Yada K, Okuno T, Yamanishi K. 2004. A posttranscriptional regulator of Kaposi's sarcoma-associated herpesvirus interacts with RNA-binding protein PCBP1 and controls gene expression through the IRES. Virology 325:364-378. http://dx.doi.org/10.1016/j.virol.2004.04.041.
    • (2004) Virology , vol.325 , pp. 364-378
    • Nishimura, K.1    Ueda, K.2    Guwanan, E.3    Sakakibara, S.4    Do, E.5    Osaki, E.6    Yada, K.7    Okuno, T.8    Yamanishi, K.9
  • 13
    • 20744448501 scopus 로고    scopus 로고
    • Regulation of the translation initiation factor eIF4F by multiple mechanisms in human cytomegalovirus-infected cells
    • Walsh D, Perez C, Notary J, Mohr I. 2005. Regulation of the translation initiation factor eIF4F by multiple mechanisms in human cytomegalovirus-infected cells. J. Virol. 79:8057-8064. http://dx.doi.org/10.1128/JVI .79.13.8057-8064.2005.
    • (2005) J. Virol. , vol.79 , pp. 8057-8064
    • Walsh, D.1    Perez, C.2    Notary, J.3    Mohr, I.4
  • 14
    • 4644252994 scopus 로고    scopus 로고
    • Human cytomegalovirus infection induces rapamycin-insensitive phosphorylation of downstream effectors of mTOR kinase
    • Kudchodkar SB, Yu Y, Maguire TG, Alwine JC. 2004. Human cytomegalovirus infection induces rapamycin-insensitive phosphorylation of downstream effectors of mTOR kinase. J. Virol. 78:11030-11039. http://dx.doi.org/10.1128/JVI.78.20.11030-11039.2004.
    • (2004) J. Virol. , vol.78 , pp. 11030-11039
    • Kudchodkar, S.B.1    Yu, Y.2    Maguire, T.G.3    Alwine, J.C.4
  • 15
    • 41849101685 scopus 로고    scopus 로고
    • Human cytomegalovirus protein UL38 inhibits host cell stress responses by antagonizing the tuberous sclerosis protein complex
    • Moorman NJ, Cristea IM, Terhune SS, Rout MP, Chait BT, Shenk T. 2008. Human cytomegalovirus protein UL38 inhibits host cell stress responses by antagonizing the tuberous sclerosis protein complex. Cell Host Microbe 3:253-262. http://dx.doi.org/10.1016/j.chom.2008.03.002.
    • (2008) Cell Host Microbe , vol.3 , pp. 253-262
    • Moorman, N.J.1    Cristea, I.M.2    Terhune, S.S.3    Rout, M.P.4    Chait, B.T.5    Shenk, T.6
  • 16
    • 77951480815 scopus 로고    scopus 로고
    • Rapamycin-resistant mTORC1 kinase activity is required for herpesvirus replication
    • Moorman NJ, Shenk T. 2010. Rapamycin-resistant mTORC1 kinase activity is required for herpesvirus replication. J. Virol. 84:5260-5269. http://dx.doi.org/10.1128/JVI.02733-09.
    • (2010) J. Virol. , vol.84 , pp. 5260-5269
    • Moorman, N.J.1    Shenk, T.2
  • 18
    • 0035312747 scopus 로고    scopus 로고
    • Regulation of translation initiation by FRAP/mTOR
    • Gingras AC, Raught B, Sonenberg N. 2001. Regulation of translation initiation by FRAP/mTOR. Genes Dev. 15:807-826. http://dx.doi.org/10 .1101/gad.887201.
    • (2001) Genes Dev. , vol.15 , pp. 807-826
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 19
    • 79952844950 scopus 로고    scopus 로고
    • The changing role of mTOR kinase in the maintenance of protein synthesis during human cytomegalovirus infection
    • Clippinger AJ, Maguire TG, Alwine JC. 2011. The changing role of mTOR kinase in the maintenance of protein synthesis during human cytomegalovirus infection. J. Virol. 85:3930-3939. http://dx.doi.org/10 .1128/JVI.01913-10.
    • (2011) J. Virol. , vol.85 , pp. 3930-3939
    • Clippinger, A.J.1    Maguire, T.G.2    Alwine, J.C.3
  • 20
    • 79958108811 scopus 로고    scopus 로고
    • Human cytomegalovirus induces the activity and expression of acetyl-coenzyme A carboxylase, a fatty acid biosynthetic enzyme whose inhibition attenuates viral replication
    • Spencer CM, Schafer XL, Moorman NJ, Munger J. 2011. Human cytomegalovirus induces the activity and expression of acetyl-coenzyme A carboxylase, a fatty acid biosynthetic enzyme whose inhibition attenuates viral replication. J. Virol. 85:5814-5824. http://dx.doi.org/10.1128/JVI .02630-10.
    • (2011) J. Virol. , vol.85 , pp. 5814-5824
    • Spencer, C.M.1    Schafer, X.L.2    Moorman, N.J.3    Munger, J.4
  • 21
    • 9344236534 scopus 로고    scopus 로고
    • Human cytomegalovirus encodes a highly specific RANTES decoy receptor
    • Wang D, Bresnahan W, Shenk T. 2004. Human cytomegalovirus encodes a highly specific RANTES decoy receptor. Proc. Natl. Acad. Sci. U.S.A. 101:16642-16647. http://dx.doi.org/10.1073/pnas.0407233101.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 16642-16647
    • Wang, D.1    Bresnahan, W.2    Shenk, T.3
  • 23
    • 70349290582 scopus 로고    scopus 로고
    • Human cytomegalovirus UL28 and UL29 open reading frames encode a spliced mRNA and stimulate accumulation of immediate-early RNAs
    • Mitchell DP, Savaryn JP, Moorman NJ, Shenk T, Terhune SS. 2009. Human cytomegalovirus UL28 and UL29 open reading frames encode a spliced mRNA and stimulate accumulation of immediate-early RNAs. J. Virol. 83:10187-10197. http://dx.doi.org/10.1128/JVI.00396-09.
    • (2009) J. Virol. , vol.83 , pp. 10187-10197
    • Mitchell, D.P.1    Savaryn, J.P.2    Moorman, N.J.3    Shenk, T.4    Terhune, S.S.5
  • 24
    • 77954485440 scopus 로고    scopus 로고
    • Human cytomegalovirus pUL83 stimulates activity of the viral immediate-early promoter through its interaction with the cellular IFI16 protein
    • Cristea IM, Moorman NJ, Terhune SS, Cuevas CD, O'Keefe ES, Rout MP, Chait BT, Shenk T. 2010. Human cytomegalovirus pUL83 stimulates activity of the viral immediate-early promoter through its interaction with the cellular IFI16 protein. J. Virol. 84:7803-7814. http://dx.doi.org/10.1128/JVI.00139-10.
    • (2010) J. Virol. , vol.84 , pp. 7803-7814
    • Cristea, I.M.1    Moorman, N.J.2    Terhune, S.S.3    Cuevas, C.D.4    O'Keefe, E.S.5    Rout, M.P.6    Chait, B.T.7    Shenk, T.8
  • 28
    • 84860527756 scopus 로고    scopus 로고
    • A unifying model for mTORC1-mediated regulation ofmRNA translation
    • Thoreen CC, Chantranupong L, Keys HR, Wang T, Gray NS, Sabatini DM. 2012. A unifying model for mTORC1-mediated regulation ofmRNA translation. Nature 485:109-113. http://dx.doi.org/10.1038/nature11083.
    • (2012) Nature , vol.485 , pp. 109-113
    • Thoreen, C.C.1    Chantranupong, L.2    Keys, H.R.3    Wang, T.4    Gray, N.S.5    Sabatini, D.M.6
  • 29
    • 0013794928 scopus 로고
    • A comparison of methods for the isolation and fractionation of reticulocyte ribosomes
    • Arnstein HR, Cox RA, Gould H, Potter H. 1965. A comparison of methods for the isolation and fractionation of reticulocyte ribosomes. Biochem. J. 96:500-506.
    • (1965) Biochem. J. , vol.96 , pp. 500-506
    • Arnstein, H.R.1    Cox, R.A.2    Gould, H.3    Potter, H.4
  • 30
    • 0035032444 scopus 로고    scopus 로고
    • The requirement for eukaryotic initiation factor 4A (elF4A) in translation is in direct proportion to the degree of mRNA 5' secondary structure
    • Svitkin YV, Pause A, Haghighat A, Pyronnet S, Witherell G, Belsham GJ, Sonenberg N. 2001. The requirement for eukaryotic initiation factor 4A (elF4A) in translation is in direct proportion to the degree of mRNA 5' secondary structure. RNA 7:382-394. http://dx.doi.org/10.1017/S135583820100108X.
    • (2001) RNA , vol.7 , pp. 382-394
    • Svitkin, Y.V.1    Pause, A.2    Haghighat, A.3    Pyronnet, S.4    Witherell, G.5    Belsham, G.J.6    Sonenberg, N.7
  • 31
    • 78650074979 scopus 로고    scopus 로고
    • Translational control of the abundance of cytoplasmic poly(A) binding protein in human cytomegalovirus-infected cells
    • Perez C, McKinney C, Chulunbaatar U, Mohr I. 2011. Translational control of the abundance of cytoplasmic poly(A) binding protein in human cytomegalovirus-infected cells. J. Virol. 85:156-164. http://dx.doi .org/10.1128/JVI.01778-10.
    • (2011) J. Virol. , vol.85 , pp. 156-164
    • Perez, C.1    McKinney, C.2    Chulunbaatar, U.3    Mohr, I.4
  • 32
    • 48849084411 scopus 로고    scopus 로고
    • Nuts and bolts of human cytomegalovirus lytic DNA replication
    • Pari GS. 2008. Nuts and bolts of human cytomegalovirus lytic DNA replication. Curr. Top. Microbiol. Immunol. 325:153-166. http://dx.doi.org/10.1007/978-3-540-77349-8_9.
    • (2008) Curr. Top. Microbiol. Immunol. , vol.325 , pp. 153-166
    • Pari, G.S.1
  • 33
    • 75449105003 scopus 로고    scopus 로고
    • Glutamine metabolism is essential for human cytomegalovirus infection
    • Chambers JW, Maguire TG, Alwine JC. 2010. Glutamine metabolism is essential for human cytomegalovirus infection. J. Virol. 84:1867-1873. http://dx.doi.org/10.1128/JVI.02123-09.
    • (2010) J. Virol. , vol.84 , pp. 1867-1873
    • Chambers, J.W.1    Maguire, T.G.2    Alwine, J.C.3
  • 34
    • 84857471383 scopus 로고    scopus 로고
    • HCMV targets the metabolic stress response through activation of AMPK whose activity is important for viral replication
    • McArdle J, Moorman NJ, Munger J. 2012. HCMV targets the metabolic stress response through activation of AMPK whose activity is important for viral replication. PLoS Pathog. 8:e1002502. http://dx.doi.org/10.1371/journal.ppat.1002502.
    • (2012) PLoS Pathog. , vol.8
    • McArdle, J.1    Moorman, N.J.2    Munger, J.3
  • 35
    • 33845970245 scopus 로고    scopus 로고
    • Dynamics of the cellular metabolome during human cytomegalovirus infection
    • Munger J, Bajad SU, Coller HA, Shenk T, Rabinowitz JD. 2006. Dynamics of the cellular metabolome during human cytomegalovirus infection. PLoS Pathog. 2:e132. http://dx.doi.org/10.1371/journal.ppat .0020132.
    • (2006) PLoS Pathog. , vol.2
    • Munger, J.1    Bajad, S.U.2    Coller, H.A.3    Shenk, T.4    Rabinowitz, J.D.5
  • 36
  • 37
    • 77953229290 scopus 로고    scopus 로고
    • Genome-wide analysis of helicase gene family from rice and Arabidopsis: a comparison with yeast and human
    • Umate P, Tuteja R, Tuteja N. 2010. Genome-wide analysis of helicase gene family from rice and Arabidopsis: a comparison with yeast and human. Plant Mol. Biol. 73:449-465. http://dx.doi.org/10.1007/s11103-010-9632-5.
    • (2010) Plant Mol. Biol. , vol.73 , pp. 449-465
    • Umate, P.1    Tuteja, R.2    Tuteja, N.3
  • 38
    • 32644444260 scopus 로고    scopus 로고
    • Assembly of an active translation initiation factor complex by a viral protein
    • Walsh D, Mohr I. 2006. Assembly of an active translation initiation factor complex by a viral protein. Genes Dev. 20:461-472. http://dx.doi.org/10 .1101/gad.1375006.
    • (2006) Genes Dev. , vol.20 , pp. 461-472
    • Walsh, D.1    Mohr, I.2
  • 39
    • 77249151465 scopus 로고    scopus 로고
    • Human cytomegalovirus UL69 protein facilitates translation by associating with the mRNA cap-binding complex and excluding 4EBP1
    • Aoyagi M, Gaspar M, Shenk TE. 2010. Human cytomegalovirus UL69 protein facilitates translation by associating with the mRNA cap-binding complex and excluding 4EBP1. Proc. Natl. Acad. Sci. U.S.A. 107:2640-2645. http://dx.doi.org/10.1073/pnas.0914856107.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 2640-2645
    • Aoyagi, M.1    Gaspar, M.2    Shenk, T.E.3
  • 40
    • 0035787721 scopus 로고    scopus 로고
    • The mRNA closed-loop model: the function of PABP and PABP-interacting proteins in mRNA transla-tion
    • Kahvejian A, Roy G, Sonenberg N. 2001. The mRNA closed-loop model: the function of PABP and PABP-interacting proteins in mRNA transla-tion. Cold Spring Harbor Symp. Quant. Biol. 66:293-300. http://dx.doi .org/10.1101/sqb.2001.66.293.
    • (2001) Cold Spring Harbor Symp. Quant. Biol. , vol.66 , pp. 293-300
    • Kahvejian, A.1    Roy, G.2    Sonenberg, N.3
  • 41
    • 84859597567 scopus 로고    scopus 로고
    • Poly(A) binding protein abundance regulates eukaryotic translation initiation factor 4F assembly in human cytomegalovirus-infected cells
    • McKinney C, Perez C, Mohr I. 2012. Poly(A) binding protein abundance regulates eukaryotic translation initiation factor 4F assembly in human cytomegalovirus-infected cells. Proc. Natl. Acad. Sci. U.S.A. 109:5627-5632. http://dx.doi.org/10.1073/pnas.1202829109.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 5627-5632
    • McKinney, C.1    Perez, C.2    Mohr, I.3
  • 42
    • 81255160914 scopus 로고    scopus 로고
    • Viral subversion of the host protein synthesis machinery
    • Walsh D, MohrI. 2011. Viral subversion of the host protein synthesis machinery. Nat. Rev. Microbiol. 9:860-875. http://dx.doi.org/10.1038/nrmicro2655.
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 860-875
    • Walsh, D.1    Mohr, I.2
  • 43
    • 71849102316 scopus 로고    scopus 로고
    • Bridging IRES elements in mRNAs to the eukaryotic translation apparatus
    • Fitzgerald KD, Semler BL. 2009. Bridging IRES elements in mRNAs to the eukaryotic translation apparatus. Biochim. Biophys. Acta 1789:518-528. http://dx.doi.org/10.1016/j.bbagrm.2009.07.004.
    • (2009) Biochim. Biophys. Acta , vol.1789 , pp. 518-528
    • Fitzgerald, K.D.1    Semler, B.L.2
  • 44
    • 80052411929 scopus 로고    scopus 로고
    • CBP80-promoted mRNP rearrangements during the pioneer round of translation, nonsensemediatedmRNAdecay, and thereafter
    • Maquat LE, Hwang J, Sato H, Tang Y. 2010. CBP80-promoted mRNP rearrangements during the pioneer round of translation, nonsensemediatedmRNAdecay, and thereafter. Cold Spring Harbor Symp. Quant. Biol. 75:127-134. http://dx.doi.org/10.1101/sqb.2010.75.028.
    • (2010) Cold Spring Harbor Symp. Quant. Biol. , vol.75 , pp. 127-134
    • Maquat, L.E.1    Hwang, J.2    Sato, H.3    Tang, Y.4
  • 45
    • 1842682946 scopus 로고    scopus 로고
    • The pioneer translation initiation complex is functionally distinct from but structurally overlaps with the steady-state translation initiation complex
    • Chiu SY, Lejeune F, Ranganathan AC, Maquat LE. 2004. The pioneer translation initiation complex is functionally distinct from but structurally overlaps with the steady-state translation initiation complex. Genes Dev. 18:745-754. http://dx.doi.org/10.1101/gad.1170204.
    • (2004) Genes Dev. , vol.18 , pp. 745-754
    • Chiu, S.Y.1    Lejeune, F.2    Ranganathan, A.C.3    Maquat, L.E.4
  • 46
    • 65949112246 scopus 로고    scopus 로고
    • Bunyavirus N: eIF4F surrogate and cap-guardian
    • Panganiban AT, Mir MA. 2009. Bunyavirus N: eIF4F surrogate and cap-guardian. Cell Cycle 8:1332-1337. http://dx.doi.org/10.4161/cc.8 .9.8315.
    • (2009) Cell Cycle , vol.8 , pp. 1332-1337
    • Panganiban, A.T.1    Mir, M.A.2


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