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Volumn 13, Issue 9, 2014, Pages 2399-2410

Quantitative proteomic discovery of dynamic epigenome changes that control human cytomegalovirus (HCMV) infection

Author keywords

[No Author keywords available]

Indexed keywords

DOT1L PROTEIN; HISTONE H3; HISTONE H4; MESSENGER RNA; METHYLTRANSFERASE; UNCLASSIFIED DRUG; VIRUS DNA; VIRUS PROTEIN; DOT1L PROTEIN, HUMAN; HISTONE;

EID: 84907203429     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M114.039792     Document Type: Article
Times cited : (28)

References (55)
  • 1
    • 0001593941 scopus 로고    scopus 로고
    • Cytomegaloviruses and their replication
    • Knipe DM, Howley, P.M., Griffin, D.E., Lamb, R.A., Martin, M.A., Roizman, B., and Straus, S.E. (Eds.), 4 ed. Philadelphia: Lippincott-Raven
    • Mocarski ESaC, C.T. (2001) Cytomegaloviruses and their replication. In Fields Virology. Knipe DM, Howley, P.M., Griffin, D.E., Lamb, R.A., Martin, M.A., Roizman, B., and Straus, S.E. (Eds.), vol. 2, 4 ed. Philadelphia: Lippincott-Raven pp. 2629-2673
    • (2001) Fields Virology , vol.2 , pp. 2629-2673
    • Mocarski Esac, C.T.1
  • 2
    • 55549147516 scopus 로고    scopus 로고
    • Temporal dynamics of cytomegalovirus chromatin assembly in productively infected human cells
    • Nitzsche, A., Paulus, C., and Nevels, M. (2008) Temporal dynamics of cytomegalovirus chromatin assembly in productively infected human cells. J. Virol. 82, 11167-11180
    • (2008) J. Virol. , vol.82 , pp. 11167-11180
    • Nitzsche, A.1    Paulus, C.2    Nevels, M.3
  • 4
    • 52649089194 scopus 로고    scopus 로고
    • Dynamic histone H3 acetylation and methylation at human cytomegalovirus promoters during replication in fibroblasts
    • Cuevas-Bennett, C., and Shenk, T. (2008) Dynamic histone H3 acetylation and methylation at human cytomegalovirus promoters during replication in fibroblasts. J. Virol. 82, 9525-9536
    • (2008) J. Virol. , vol.82 , pp. 9525-9536
    • Cuevas-Bennett, C.1    Shenk, T.2
  • 5
    • 84866156496 scopus 로고    scopus 로고
    • Histone H3 lysine 4 methylation marks postreplicative human cytomegalovirus chromatin
    • Nitzsche, A., Steinhausser, C., Mucke, K., Paulus, C., and Nevels, M. (2012) Histone H3 lysine 4 methylation marks postreplicative human cytomegalovirus chromatin. J. Virol. 86, 9817-9827
    • (2012) J. Virol. , vol.86 , pp. 9817-9827
    • Nitzsche, A.1    Steinhausser, C.2    Mucke, K.3    Paulus, C.4    Nevels, M.5
  • 6
    • 10344222687 scopus 로고    scopus 로고
    • Human cytomegalovirus immediate-early 1 protein facilitates viral replication by antagonizing histone deacetylation
    • Nevels, M., Paulus, C., and Shenk, T. (2004) Human cytomegalovirus immediate-early 1 protein facilitates viral replication by antagonizing histone deacetylation. Proc. Natl. Acad. Sci. U.S.A. 101, 17234-17239
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 17234-17239
    • Nevels, M.1    Paulus, C.2    Shenk, T.3
  • 8
    • 0033868416 scopus 로고    scopus 로고
    • The human cytomegalovirus 86-kilodalton major immediate-early protein interacts physically and functionally with histone acetyltransferase P/CAF
    • Bryant, L. A., Mixon, P., Davidson, M., Bannister, A. J., Kouzarides, T., and Sinclair, J. H. (2000) The human cytomegalovirus 86-kilodalton major immediate-early protein interacts physically and functionally with histone acetyltransferase P/CAF. J. Virol. 74, 7230-7237
    • (2000) J. Virol. , vol.74 , pp. 7230-7237
    • Bryant, L.A.1    Mixon, P.2    Davidson, M.3    Bannister, A.J.4    Kouzarides, T.5    Sinclair, J.H.6
  • 9
    • 33749496663 scopus 로고    scopus 로고
    • Autorepression of the human cytomegalovirus major immediateearly promoter/enhancer at late times of infection is mediated by the recruitment of chromatin remodeling enzymes by IE86
    • Reeves, M., Murphy, J., Greaves, R., Fairley, J., Brehm, A., and Sinclair, J. (2006) Autorepression of the human cytomegalovirus major immediateearly promoter/enhancer at late times of infection is mediated by the recruitment of chromatin remodeling enzymes by IE86. J. Virol. 80, 9998-10009
    • (2006) J. Virol. , vol.80 , pp. 9998-10009
    • Reeves, M.1    Murphy, J.2    Greaves, R.3    Fairley, J.4    Brehm, A.5    Sinclair, J.6
  • 10
    • 0036500165 scopus 로고    scopus 로고
    • Control of cytomegalovirus lytic gene expression by histone acetylation
    • Murphy, J. C., Fischle, W., Verdin, E., Sinclair, J. H. (2002) Control of cytomegalovirus lytic gene expression by histone acetylation. EMBO J. 21, 1112-1120
    • (2002) EMBO J. , vol.21 , pp. 1112-1120
    • Murphy, J.C.1    Fischle, W.2    Verdin, E.3    Sinclair, J.H.4
  • 11
    • 77954671476 scopus 로고    scopus 로고
    • Human cytomegalovirus UL29/28 protein interacts with components of the NuRD complex which promote accumulation of immediate-early RNA
    • Terhune, S. S., Moorman, N. J., Cristea, I. M., Savaryn, J. P., Cuevas-Bennett, C., Rout, M. P., Chait, B. T., and Shenk, T. (2010) Human cytomegalovirus UL29/28 protein interacts with components of the NuRD complex which promote accumulation of immediate-early RNA. PLoS Pathog. 6, e1000965
    • (2010) PLoS Pathog. , vol.6 , pp. e1000965
    • Terhune, S.S.1    Moorman, N.J.2    Cristea, I.M.3    Savaryn, J.P.4    Cuevas-Bennett, C.5    Rout, M.P.6    Chait, B.T.7    Shenk, T.8
  • 13
    • 79952830376 scopus 로고    scopus 로고
    • Human cytomegalovirus pUS27 G protein-coupled receptor homologue is required for efficient spread by the extracellular route but not for direct cell-to-cell spread
    • O'Connor, C. M., and Shenk, T. (2011) Human cytomegalovirus pUS27 G protein-coupled receptor homologue is required for efficient spread by the extracellular route but not for direct cell-to-cell spread. J. Virol. 85, 3700-3707
    • (2011) J. Virol. , vol.85 , pp. 3700-3707
    • O'connor, C.M.1    Shenk, T.2
  • 14
    • 84866161851 scopus 로고    scopus 로고
    • Genome sequence of herpes simplex virus 1 strain KOS
    • Macdonald, S. J., Mostafa, H. H., Morrison, L. A., and Davido, D. J. (2012) Genome sequence of herpes simplex virus 1 strain KOS. J. Virol. 86, 6371-6372
    • (2012) J. Virol. , vol.86 , pp. 6371-6372
    • Macdonald, S.J.1    Mostafa, H.H.2    Morrison, L.A.3    Davido, D.J.4
  • 15
    • 0017870263 scopus 로고
    • Isolation of deletion and substitution mutants of adenovirus type 1
    • Jones, N., and Shenk, T. (1978) Isolation of deletion and substitution mutants of adenovirus type 1. Cell 13, 181-188
    • (1978) Cell , vol.13 , pp. 181-188
    • Jones, N.1    Shenk, T.2
  • 16
    • 0030819379 scopus 로고    scopus 로고
    • Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo
    • Zufferey, R., Nagy, D., Mandel, R. J., Naldini, L., and Trono, D. (1997) Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo. Nat Biotechnol 15, 871-875
    • (1997) Nat Biotechnol , vol.15 , pp. 871-875
    • Zufferey, R.1    Nagy, D.2    Mandel, R.J.3    Naldini, L.4    Trono, D.5
  • 17
    • 84864923697 scopus 로고    scopus 로고
    • Proteogenomic characterization and mapping of nucleosomes decoded by Brd and HP1 proteins
    • R68
    • Leroy, G., Chepelev, I., Dimaggio, P. A., Blanco, M. A., Zee, B. M., Zhao, K., and Garcia, B. A. (2012) Proteogenomic characterization and mapping of nucleosomes decoded by Brd and HP1 proteins. Genome Biol. 2012, 13, R68
    • (2012) Genome Biol. , vol.2012 , pp. 13
    • Leroy, G.1    Chepelev, I.2    Dimaggio, P.A.3    Blanco, M.A.4    Zee, B.M.5    Zhao, K.6    Garcia, B.A.7
  • 18
    • 71049141077 scopus 로고    scopus 로고
    • A mixed integer linear optimization framework for the identification and quantification of targeted post-translational modifications of highly modified proteins using multiplexed electron transfer dissociation tandem mass spectrometry
    • DiMaggio, P. A., Jr., Young, N. L., Baliban, R. C., Garcia, B. A., and Floudas, C. A. (2009) A mixed integer linear optimization framework for the identification and quantification of targeted post-translational modifications of highly modified proteins using multiplexed electron transfer dissociation tandem mass spectrometry. Mol. Cell. Proteomics 8, 2527-2543
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2527-2543
    • DiMaggio, P.A.1    Young, N.L.2    Baliban, R.C.3    Garcia, B.A.4    Floudas, C.A.5
  • 19
    • 84874055056 scopus 로고    scopus 로고
    • Novel phosphorylation sites in the S. Cerevisiae Cdc13 protein reveal new targets for telomere length regulation
    • Wu, Y., DiMaggio, P. A., Jr., Perlman, D. H., Zakian, V. A., and Garcia, B. A. (2013) Novel phosphorylation sites in the S. cerevisiae Cdc13 protein reveal new targets for telomere length regulation. J. Proteome Res. 12, 316-327
    • (2013) J. Proteome Res. , vol.12 , pp. 316-327
    • Wu, Y.1    DiMaggio, P.A.2    Perlman, D.H.3    Zakian, V.A.4    Garcia, B.A.5
  • 22
    • 0028801332 scopus 로고
    • Human cytomegalovirus IE1 and IE2 proteins block apoptosis
    • Zhu H, Shen Y, Shenk T: (1995) Human cytomegalovirus IE1 and IE2 proteins block apoptosis. J. Virol. 69, 7960-7970
    • (1995) J. Virol. , vol.69 , pp. 7960-7970
    • Zhu, H.1    Shen, Y.2    Shenk, T.3
  • 23
    • 0141856234 scopus 로고    scopus 로고
    • Human cytomegalovirus UL99-encoded pp28 is required for the cytoplasmic envelopment of tegument-associated capsids
    • Silva, M. C., Yu, Q. C., Enquist, L., and Shenk, T. (2003) Human cytomegalovirus UL99-encoded pp28 is required for the cytoplasmic envelopment of tegument-associated capsids. J. Virol. 77, 10594-10605
    • (2003) J. Virol. , vol.77 , pp. 10594-10605
    • Silva, M.C.1    Yu, Q.C.2    Enquist, L.3    Shenk, T.4
  • 24
    • 0021358727 scopus 로고
    • Physical mapping of human cytomegalovirus genes: Identification of DNA sequences coding for a virion phosphoprotein of 71 kDa and a viral 65-kDa polypeptide
    • Nowak, B., Gmeiner, A., Sarnow, P., Levine, A. J., and Fleckenstein, B. (1984) Physical mapping of human cytomegalovirus genes: identification of DNA sequences coding for a virion phosphoprotein of 71 kDa and a viral 65-kDa polypeptide. Virology 134, 91-102
    • (1984) Virology , vol.134 , pp. 91-102
    • Nowak, B.1    Gmeiner, A.2    Sarnow, P.3    Levine, A.J.4    Fleckenstein, B.5
  • 25
    • 0037373383 scopus 로고    scopus 로고
    • Human cytomegalovirus pp71 stimulates cell cycle progression by inducing the proteasome-dependent degradation of the retinoblastoma family of tumor suppressors
    • Kalejta, R. F., Bechtel, J. T., and Shenk, T. (2003) Human cytomegalovirus pp71 stimulates cell cycle progression by inducing the proteasome-dependent degradation of the retinoblastoma family of tumor suppressors. Mol. Cell. Biol. 23, 1885-1895
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1885-1895
    • Kalejta, R.F.1    Bechtel, J.T.2    Shenk, T.3
  • 26
    • 0019789105 scopus 로고
    • Monoclonal antibodies to herpes simplex virus type 1 proteins, including the immediate-early protein ICP 1
    • Showalter, S. D., Zweig, M., Hampar, B. (1981) Monoclonal antibodies to herpes simplex virus type 1 proteins, including the immediate-early protein ICP 1. Infect. Immun. 34, 684-692
    • (1981) Infect. Immun. , vol.34 , pp. 684-692
    • Showalter, S.D.1    Zweig, M.2    Hampar, B.3
  • 27
    • 0020501764 scopus 로고
    • Monoclonal antibodies which recognize native and denatured forms of the adenovirus DNA-binding protein
    • Reich, N. C., Sarnow, P., Duprey, E., and Levine, A. J. (1983) Monoclonal antibodies which recognize native and denatured forms of the adenovirus DNA-binding protein. Virology 128, 480-484
    • (1983) Virology , vol.128 , pp. 480-484
    • Reich, N.C.1    Sarnow, P.2    Duprey, E.3    Levine, A.J.4
  • 28
    • 18744375196 scopus 로고    scopus 로고
    • Identifying and quantifying in vivo methylation sites by heavy methyl SILAC
    • Ong, S. E., Mittler, G., and Mann, M. (2004) Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. Nat. Methods 1, 119-126
    • (2004) Nat. Methods , vol.1 , pp. 119-126
    • Ong, S.E.1    Mittler, G.2    Mann, M.3
  • 30
    • 0033989064 scopus 로고    scopus 로고
    • Accumulation of virion tegument and envelope proteins in a stable cytoplasmic compartment during human cytomegalovirus replication: Characterization of a potential site of virus assembly
    • Sanchez, V., Greis, K. D., Sztul, E., and Britt, W. J. (2000) Accumulation of virion tegument and envelope proteins in a stable cytoplasmic compartment during human cytomegalovirus replication: characterization of a potential site of virus assembly. J. Virol. 74, 975-986
    • (2000) J. Virol. , vol.74 , pp. 975-986
    • Sanchez, V.1    Greis, K.D.2    Sztul, E.3    Britt, W.J.4
  • 33
    • 79959960773 scopus 로고    scopus 로고
    • The diverse functions of Dot1 and H3K79 methylation
    • Nguyen, A. T., and Zhang, Y. (2011) The diverse functions of Dot1 and H3K79 methylation. Genes Dev. 25, 1345-1358
    • (2011) Genes Dev. , vol.25 , pp. 1345-1358
    • Nguyen, A.T.1    Zhang, Y.2
  • 35
    • 0029011873 scopus 로고
    • Purification of P-TEFb, a transcription factor required for the transition into productive elongation
    • Marshall, N. F., and Price, D. H. (1995) Purification of P-TEFb, a transcription factor required for the transition into productive elongation. J. Biol. Chem. 270, 12335-12338
    • (1995) J. Biol. Chem. , vol.270 , pp. 12335-12338
    • Marshall, N.F.1    Price, D.H.2
  • 37
    • 84879610545 scopus 로고    scopus 로고
    • Methylation of histone H3 on lysine 79 associates with a group of replication origins and helps limit DNA replication once per cell cycle
    • Fu, H., Maunakea, A. K., Martin, M. M., Huang, L., Zhang, Y., Ryan, M., Kim, R., Lin, C. M., Zhao, K., and Aladje, M. I. (2013) Methylation of histone H3 on lysine 79 associates with a group of replication origins and helps limit DNA replication once per cell cycle. PLoS Genet. 9, e1003542
    • (2013) PLoS Genet. , vol.9 , pp. e1003542
    • Fu, H.1    Maunakea, A.K.2    Martin, M.M.3    Huang, L.4    Zhang, Y.5    Ryan, M.6    Kim, R.7    Lin, C.M.8    Zhao, K.9    Aladje, M.I.10
  • 38
    • 79953131815 scopus 로고    scopus 로고
    • SUV420H2-mediated H4K20 trimethylation enforces RNA polymerase II promoterproximal pausing by blocking hMOF-dependent H4K16 acetylation
    • Kapoor-Vazirani, P., Kagey, J. D., and Vertino, P. M. (2011) SUV420H2-mediated H4K20 trimethylation enforces RNA polymerase II promoterproximal pausing by blocking hMOF-dependent H4K16 acetylation. Mol. Cell. Biol. 31, 1594-1609
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 1594-1609
    • Kapoor-Vazirani, P.1    Kagey, J.D.2    Vertino, P.M.3
  • 39
    • 27144546434 scopus 로고    scopus 로고
    • A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 1
    • Smith, E. R., Cayrou, C., Huang, R., Lane, W. S., Cote, J., and Lucchesi, J. C. (2005) A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 1. Mol. Cell. Biol. 25, 9175-9188
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 9175-9188
    • Smith, E.R.1    Cayrou, C.2    Huang, R.3    Lane, W.S.4    Cote, J.5    Lucchesi, J.C.6
  • 40
    • 22544480772 scopus 로고    scopus 로고
    • HMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells
    • Taipale, M., Rea, S., Richter, K., Vilar, A., Lichter, P., Imhof, A., and Akhtar, A. (2005) hMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells. Mol. Cell. Biol. 25, 6798-6810
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6798-6810
    • Taipale, M.1    Rea, S.2    Richter, K.3    Vilar, A.4    Lichter, P.5    Imhof, A.6    Akhtar, A.7
  • 42
    • 32444434989 scopus 로고    scopus 로고
    • Histone H4-K16 acetylation controls chromatin structure and protein interactions
    • Shogren-Knaak, M., Ishii, H., Sun, J. M., Pazin, M. J., Davie, J. R., and Peterson, C. L. (2006) Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 311, 844-847
    • (2006) Science , vol.311 , pp. 844-847
    • Shogren-Knaak, M.1    Ishii, H.2    Sun, J.M.3    Pazin, M.J.4    Davie, J.R.5    Peterson, C.L.6
  • 45
    • 84856120332 scopus 로고    scopus 로고
    • Understanding the language of Lys36 methylation at histone H3
    • Wagner, E. J., and Carpenter, P. B. (2012) Understanding the language of Lys36 methylation at histone H3. Nat. Rev. Mol. Cell Biol. 13, 115-126
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 115-126
    • Wagner, E.J.1    Carpenter, P.B.2
  • 47
    • 0037131523 scopus 로고    scopus 로고
    • Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites
    • Czermin, B., Melfi, R., McCabe, D., Seitz, V., Imhof, A., and Pirrotta, V. (2002) Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites. Cell 111, 185-196
    • (2002) Cell , vol.111 , pp. 185-196
    • Czermin, B.1    Melfi, R.2    McCabe, D.3    Seitz, V.4    Imhof, A.5    Pirrotta, V.6
  • 49
    • 0036340237 scopus 로고    scopus 로고
    • The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans
    • Levine, S. S., Weiss, A., Erdjument-Bromage, H., Shao, Z., Tempst, P., and Kingston, R. E. (2002) The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans. Mol. Cell. Biol. 22, 6070-6078
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6070-6078
    • Levine, S.S.1    Weiss, A.2    Erdjument-Bromage, H.3    Shao, Z.4    Tempst, P.5    Kingston, R.E.6
  • 50
    • 70349469565 scopus 로고    scopus 로고
    • Mechanisms of polycomb gene silencing: Knowns and unknowns
    • Simon, J. A., and Kingston, R. E. (2009) Mechanisms of polycomb gene silencing: knowns and unknowns. Nat. Rev. Mol. Cell Biol. 10, 697-708
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 697-708
    • Simon, J.A.1    Kingston, R.E.2
  • 52
    • 0035194167 scopus 로고    scopus 로고
    • Altered cellular mRNA levels in human cytomegalovirus-infected fibroblasts: Viral block to the accumulation of antiviral mRNAs
    • Browne, E. P., Wing, B., Coleman, D., and Shenk, T. (2001) Altered cellular mRNA levels in human cytomegalovirus-infected fibroblasts: viral block to the accumulation of antiviral mRNAs. J. Virol. 75, 12319-12330
    • (2001) J. Virol. , vol.75 , pp. 12319-12330
    • Browne, E.P.1    Wing, B.2    Coleman, D.3    Shenk, T.4
  • 53
    • 57949105676 scopus 로고    scopus 로고
    • Biclustering via optimal re-ordering of data matrices in systems biology: Rigorous methods and comparative studies
    • DiMaggio, P. A., Jr., McAllister, S. R., Floudas, C. A., Feng, X. J., Rabinowitz, J. D., and Rabitz, H. A. (2008) Biclustering via optimal re-ordering of data matrices in systems biology: rigorous methods and comparative studies. BMC Bioinformatics 9, 458
    • (2008) BMC Bioinformatics , vol.9 , pp. 458
    • DiMaggio, P.A.1    McAllister, S.R.2    Floudas, C.A.3    Feng, X.J.4    Rabinowitz, J.D.5    Rabitz, H.A.6
  • 55
    • 77957759247 scopus 로고    scopus 로고
    • Activator-dependent p300 acetylation of chromatin in vitro: Enhancement of transcription by disruption of repressive nucleosome-nucleosome interactions
    • Szerlong, H. J., Prenni, J. E., Nyborg, J. K., and Hansen, J. C. (2010) Activator-dependent p300 acetylation of chromatin in vitro: enhancement of transcription by disruption of repressive nucleosome-nucleosome interactions. J. Biol. Chem. 285, 31954-31964
    • (2010) J. Biol. Chem. , vol.285 , pp. 31954-31964
    • Szerlong, H.J.1    Prenni, J.E.2    Nyborg, J.K.3    Hansen, J.C.4


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