메뉴 건너뛰기




Volumn 4, Issue 3, 2008, Pages

Methylated DNA recognition during the reversal of epigenetic silencing is regulated by cysteine and serine residues in the Epstein-Barr virus lytic switch protein

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYSTEINE; CYTOSINE; GENOMIC RNA; IMMEDIATE EARLY PROTEIN BZLF1; SERINE; BZLF1 PROTEIN, HERPESVIRUS 4, HUMAN; DNA BINDING PROTEIN; TRANSACTIVATOR PROTEIN; VIRUS PROTEIN;

EID: 42949174160     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1000005     Document Type: Article
Times cited : (37)

References (26)
  • 1
    • 32344450824 scopus 로고    scopus 로고
    • Genomic DNA methylation: The mark and its mediators
    • Klose RJ, Bird AP (2006) Genomic DNA methylation: the mark and its mediators. Trends Biochem Sci 31: 89-97.
    • (2006) Trends Biochem Sci , vol.31 , pp. 89-97
    • Klose, R.J.1    Bird, A.P.2
  • 2
    • 0024081657 scopus 로고
    • Cytosine methylation prevents binding to DNA of a HeLa cell transcription factor required for optimal expression of the adenovirus major late promoter
    • Watt F, Molloy PL (1988) Cytosine methylation prevents binding to DNA of a HeLa cell transcription factor required for optimal expression of the adenovirus major late promoter. Genes Dev 2: 1136-43.
    • (1988) Genes Dev , vol.2 , pp. 1136-1143
    • Watt, F.1    Molloy, P.L.2
  • 3
    • 6944244957 scopus 로고    scopus 로고
    • The EBV lytic switch protein, Z, preferentially binds to and activates the methylated viral genome
    • Bhende PM, Seaman WT, Delecluse HJ, Kenney SC (2004) The EBV lytic switch protein, Z, preferentially binds to and activates the methylated viral genome. Nat Genet 36: 1099-104.
    • (2004) Nat Genet , vol.36 , pp. 1099-1104
    • Bhende, P.M.1    Seaman, W.T.2    Delecluse, H.J.3    Kenney, S.C.4
  • 4
    • 19944397140 scopus 로고    scopus 로고
    • BZLF1 activation of the methylated form of the BRLF1 immediate-early promoter is regulated by BZLF1 residue 186
    • Bhende PM, Seaman WT, Delecluse HJ, Kenney SC (2005) BZLF1 activation of the methylated form of the BRLF1 immediate-early promoter is regulated by BZLF1 residue 186. J Virol 79: 7338-48.
    • (2005) J Virol , vol.79 , pp. 7338-7348
    • Bhende, P.M.1    Seaman, W.T.2    Delecluse, H.J.3    Kenney, S.C.4
  • 5
  • 7
    • 0024328960 scopus 로고
    • The switch between EBV latency and replication
    • Miller G (1989) The switch between EBV latency and replication. Yale J Biol Med 62: 205-13.
    • (1989) Yale J Biol Med , vol.62 , pp. 205-213
    • Miller, G.1
  • 8
    • 11244266124 scopus 로고    scopus 로고
    • Latent and lytic Epstein-Barr virus replication strategies
    • Tsurumi T, Fujita M, Kudoh A (2005) Latent and lytic Epstein-Barr virus replication strategies. Rev Med Virol 15: 3-15.
    • (2005) Rev Med Virol , vol.15 , pp. 3-15
    • Tsurumi, T.1    Fujita, M.2    Kudoh, A.3
  • 9
    • 0025214570 scopus 로고
    • Autoregulation of Epstein-Barr Virus putative lytic switch gene BZLF1
    • Flemington E, Speck SH (1990) Autoregulation of Epstein-Barr Virus putative lytic switch gene BZLF1. Journal of Virology 64: 1227-1232.
    • (1990) Journal of Virology , vol.64 , pp. 1227-1232
    • Flemington, E.1    Speck, S.H.2
  • 10
    • 0026163624 scopus 로고
    • Pathways of activation of the Epstein-Barr virus productive cycle
    • Sinclair AJ, Brimmell M, Shanahan F, Farrell PJ (1991) Pathways of activation of the Epstein-Barr virus productive cycle. J Virol 65: 2237-44.
    • (1991) J Virol , vol.65 , pp. 2237-2244
    • Sinclair, A.J.1    Brimmell, M.2    Shanahan, F.3    Farrell, P.J.4
  • 11
    • 0034660443 scopus 로고    scopus 로고
    • The Epstein-Barr virus lytic program is controlled by the cooperative functions of two transactivators
    • Feederle R, Kost M, Baumann M, Janz A, Drouet E, Hammerschmidt W, Delecluse HJ (2000) The Epstein-Barr virus lytic program is controlled by the cooperative functions of two transactivators. EMBO J 19: 3080-3089.
    • (2000) EMBO J , vol.19 , pp. 3080-3089
    • Feederle, R.1    Kost, M.2    Baumann, M.3    Janz, A.4    Drouet, E.5    Hammerschmidt, W.6    Delecluse, H.J.7
  • 12
    • 27144531199 scopus 로고    scopus 로고
    • A redox-sensitive cysteine in Zta is required for Epstein-Barr virus lytic cycle DNA replication
    • Wang P, Day L, Dheekollu J, Lieberman PM (2005) A redox-sensitive cysteine in Zta is required for Epstein-Barr virus lytic cycle DNA replication. J Virol 79: 13298-309.
    • (2005) J Virol , vol.79 , pp. 13298-13309
    • Wang, P.1    Day, L.2    Dheekollu, J.3    Lieberman, P.M.4
  • 13
    • 27144458370 scopus 로고    scopus 로고
    • Mutation of a single amino acid residue in the basic region of the Epstein-Barr virus (EBV) lytic cycle switch protein Zta (BZLF1) prevents reactivation of EBV from latency
    • Schelcher C, Valencia S, Delecluse HJ, Hicks M, Sinclair AJ (2005) Mutation of a single amino acid residue in the basic region of the Epstein-Barr virus (EBV) lytic cycle switch protein Zta (BZLF1) prevents reactivation of EBV from latency. J Virol 79: 13822-8.
    • (2005) J Virol , vol.79 , pp. 13822-13828
    • Schelcher, C.1    Valencia, S.2    Delecluse, H.J.3    Hicks, M.4    Sinclair, A.J.5
  • 15
    • 32444448106 scopus 로고    scopus 로고
    • Structural Basis of Lytic Cycle Activation by the Epstein-Barr Virus ZEBRA Protein
    • Petosa C, Morand P, Baudin F, Moulin M, Artero JB, Muller CW (2006) Structural Basis of Lytic Cycle Activation by the Epstein-Barr Virus ZEBRA Protein. Mol Cell 21: 565-72.
    • (2006) Mol Cell , vol.21 , pp. 565-572
    • Petosa, C.1    Morand, P.2    Baudin, F.3    Moulin, M.4    Artero, J.B.5    Muller, C.W.6
  • 16
    • 3042560021 scopus 로고    scopus 로고
    • Structural analysis of cation-pi interactions in DNA binding proteins
    • Gromiha M, Santhosh C, Ahmad S (2004) Structural analysis of cation-pi interactions in DNA binding proteins. Int J Biol Macromol 34: 203-211.
    • (2004) Int J Biol Macromol , vol.34 , pp. 203-211
    • Gromiha, M.1    Santhosh, C.2    Ahmad, S.3
  • 17
    • 0032881445 scopus 로고    scopus 로고
    • Strong hydrophobic nature of cysteine residues in proteins
    • Nagano N, Ota M, Nishikawa K (1999) Strong hydrophobic nature of cysteine residues in proteins. FEBS Lett 458: 69-71.
    • (1999) FEBS Lett , vol.458 , pp. 69-71
    • Nagano, N.1    Ota, M.2    Nishikawa, K.3
  • 20
    • 33645017891 scopus 로고    scopus 로고
    • EBV EBNA 2 stimulates CDK9-dependent transcription and RNA polymerase II phosphorylation on serine 5
    • Bark-Jones SJ, Webb HM, West MJ (2006) EBV EBNA 2 stimulates CDK9-dependent transcription and RNA polymerase II phosphorylation on serine 5. Oncogene 25: 1775-85.
    • (2006) Oncogene , vol.25 , pp. 1775-1785
    • Bark-Jones, S.J.1    Webb, H.M.2    West, M.J.3
  • 21
    • 0035038931 scopus 로고    scopus 로고
    • Biophysical analysis of natural variants of the multimerization region of Epstein-Barr virus lytic-switch protein BZLF1
    • Hicks MR, Balesaria S, Medina-Palazon C, Pandya MJ, Woolfson DN, Sinclair AJ (2001) Biophysical analysis of natural variants of the multimerization region of Epstein-Barr virus lytic-switch protein BZLF1. Journal of Virology 75: 5381-5384.
    • (2001) Journal of Virology , vol.75 , pp. 5381-5384
    • Hicks, M.R.1    Balesaria, S.2    Medina-Palazon, C.3    Pandya, M.J.4    Woolfson, D.N.5    Sinclair, A.J.6
  • 22
    • 0038420735 scopus 로고    scopus 로고
    • The zipper region of Epstein-Barr virus bZIP transcription factor Zta is necessary but not sufficient to direct DNA binding
    • Hicks MR, Al-Mehairi SS, Sinclair AJ (2003) The zipper region of Epstein-Barr virus bZIP transcription factor Zta is necessary but not sufficient to direct DNA binding. J Virol 77: 8173-7.
    • (2003) J Virol , vol.77 , pp. 8173-8177
    • Hicks, M.R.1    Al-Mehairi, S.S.2    Sinclair, A.J.3
  • 23
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47 (Pt 2): 110-9.
    • (1991) Acta Crystallogr A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 24
    • 0026738923 scopus 로고
    • C-C-A-G-G-C-m5C-T-G-G. Helical fine structure, hydration, and comparison with C-C-A-G-G-C-C-T-G-G
    • Heinemann U, Hahn M (1992) C-C-A-G-G-C-m5C-T-G-G. Helical fine structure, hydration, and comparison with C-C-A-G-G-C-C-T-G-G. J Biol Chem 267: 7332-41.
    • (1992) J Biol Chem , vol.267 , pp. 7332-7341
    • Heinemann, U.1    Hahn, M.2
  • 25
    • 0033119938 scopus 로고    scopus 로고
    • Esnouf RM (1999) Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr D Biol Crystallogr 55: 938-40
    • Esnouf RM (1999) Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr D Biol Crystallogr 55: 938-40.
  • 26
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic Molecular Graphics
    • Merritt EA, Bacon DJ (1997) Raster3D: Photorealistic Molecular Graphics. Methods in Enzymology 277: 505-524.
    • (1997) Methods in Enzymology , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.