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Volumn 63, Issue , 1998, Pages 469-481

Signaling to chromatin through histone modifications: How clear is the signal?

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE; MITOGENIC AGENT; E1A PROTEIN; EPIDERMAL GROWTH FACTOR; HISTONE ACETYLTRANSFERASE GCN5; HISTONE ACETYLTRANSFERASE PCAF; HISTONE DEACETYLASE 1; HISTONE H1; HISTONE H2A; HISTONE H3; HISTONE H4; MITOGEN ACTIVATED PROTEIN KINASE; NUCLEAR RECEPTOR COACTIVATOR; POST-TRANSLATIONALLY MODIFIED PROTEIN; PROTEIN KINASE; TRANSCRIPTION FACTOR IID;

EID: 0032467010     PISSN: 00917451     EISSN: None     Source Type: Book Series    
DOI: 10.1101/sqb.1998.63.469     Document Type: Conference Paper
Times cited : (31)

References (33)
  • 1
    • 0032549013 scopus 로고    scopus 로고
    • Activation of SRF-regulated chromosomal templates by Rho-family GT-Pases requires a signal that also induces H4 hyperacetylation
    • Alberts A.S., Geneste O., and Treisman R. 1998. Activation of SRF-regulated chromosomal templates by Rho-family GT-Pases requires a signal that also induces H4 hyperacetylation. Cell 92: 475.
    • (1998) Cell , vol.92 , pp. 475
    • Alberts, A.S.1    Geneste, O.2    Treisman, R.3
  • 2
    • 0031966532 scopus 로고    scopus 로고
    • New excitement over an old word: "Chromatin."
    • Allis C.D. and Gasser S.M. 1998. New excitement over an old word: "Chromatin." Curr. Opin. Genet. Dev. 8: 137.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 137
    • Allis, C.D.1    Gasser, S.M.2
  • 3
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister A.J. and Kouzarides T. 1996. The CBP co-activator is a histone acetyltransferase. Nature 384: 641.
    • (1996) Nature , vol.384 , pp. 641
    • Bannister, A.J.1    Kouzarides, T.2
  • 4
    • 0031913215 scopus 로고    scopus 로고
    • Repression of GCN5 histone acetyltransferase activity via bromodomain- Mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase complex
    • Barlev N.A., Poltoratsky V., Owen-Hughes T., Ying C., Liu L., Workman J.L., and Berger S.L. 1998. Repression of GCN5 histone acetyltransferase activity via bromodomain- mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase complex. Mol. Cell. Biol. 18: 1349.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1349
    • Barlev, N.A.1    Poltoratsky, V.2    Owen-Hughes, T.3    Ying, C.4    Liu, L.5    Workman, J.L.6    Berger, S.L.7
  • 5
    • 0028291992 scopus 로고
    • Mitogen-stimulated phosphorylation of histone H3 is targeted to a small hyperacetylation-sensitive fraction
    • Barratt M.J., Hazzalin C.A., Cano E., and Mahadevan L.C. 1994. Mitogen-stimulated phosphorylation of histone H3 is targeted to a small hyperacetylation-sensitive fraction. Proc. Natl. Acad. Sci. 91: 4781.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 4781
    • Barratt, M.J.1    Hazzalin, C.A.2    Cano, E.3    Mahadevan, L.C.4
  • 7
    • 0026441880 scopus 로고
    • Reversible histone modifications and the chromosome cell cycle
    • Bradbury E.M. 1992. Reversible histone modifications and the chromosome cell cycle. BioEssays 14: 9.
    • (1992) BioEssays , vol.14 , pp. 9
    • Bradbury, E.M.1
  • 9
    • 0029049102 scopus 로고
    • An activity gel assay detects a single, catalytically active histone acetyltransferase subunit in Tetrahymena macronuclei
    • Brownell J.E. and Allis C.D. 1995. An activity gel assay detects a single, catalytically active histone acetyltransferase subunit in Tetrahymena macronuclei. Proc. Natl. Acad. Sci. 92: 6364.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 6364
    • Brownell, J.E.1    Allis, C.D.2
  • 10
    • 0029984469 scopus 로고    scopus 로고
    • Tetraliymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • Brownell J.E., Zhou J., Ranalli T., Kobayashi R., Edmondson D.G., Roth S.Y., and Allis C.D. 1996. Tetraliymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 84: 843.
    • (1996) Cell , vol.84 , pp. 843
    • Brownell, J.E.1    Zhou, J.2    Ranalli, T.3    Kobayashi, R.4    Edmondson, D.G.5    Roth, S.Y.6    Allis, C.D.7
  • 12
    • 0029991514 scopus 로고    scopus 로고
    • HDA1 and HDA3 are components of a yeast histone deacetylase (HDA) complex
    • Carmen A.A., Rundlett S.E., and Grunstein M. 1996. HDA1 and HDA3 are components of a yeast histone deacetylase (HDA) complex. J. Biol. Chem. 271: 15837.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15837
    • Carmen, A.A.1    Rundlett, S.E.2    Grunstein, M.3
  • 13
    • 0029120154 scopus 로고
    • Increased phosphorylation of histone HI in mouse fibroblasts transformed with oncogenes of constitutively active mitogen-activated protein kinase kinase
    • Chadee D.N., Taylor W.R., Hurta R.A.R., Allis C.D., Wright J.A., and Davie J. 1995. Increased phosphorylation of histone HI in mouse fibroblasts transformed with oncogenes of constitutively active mitogen-activated protein kinase kinase. J. Biol. Chem. 270: 20098.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20098
    • Chadee, D.N.1    Taylor, W.R.2    Hurta, R.A.R.3    Allis, C.D.4    Wright, J.A.5    Davie, J.6
  • 14
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
    • Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L., Privalsky ML., Nakatani Y., and Evans R.M. 1997. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 90: 569.
    • (1997) Cell , vol.90 , pp. 569
    • Chen, H.1    Lin, R.J.2    Schiltz, R.L.3    Chakravarti, D.4    Nash, A.5    Nagy, L.6    Privalsky, M.L.7    Nakatani, Y.8    Evans, R.M.9
  • 15
    • 0026608787 scopus 로고
    • Nuclear localization and regulation of erk- And rsk-encoded protein kinases
    • Chen R.H., Sarnecki C., and Blenis J. 1992. Nuclear localization and regulation of erk- and rsk-encoded protein kinases. Mol. Cell. Biol. 12: 915.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 915
    • Chen, R.H.1    Sarnecki, C.2    Blenis, J.3
  • 16
    • 0022650761 scopus 로고
    • Nonrandom utilization of acetylation sites in histones isolated from Tetrahymena: Evidence for functionally distinct H4 acetylation sites
    • Chicoine L.G., Schulman I.G., Richman R., Cook R.G., and Allis C.D. 1986. Nonrandom utilization of acetylation sites in histones isolated from Tetrahymena: Evidence for functionally distinct H4 acetylation sites. J. Biol. Chem. 261: 1071.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1071
    • Chicoine, L.G.1    Schulman, I.G.2    Richman, R.3    Cook, R.G.4    Allis, C.D.5
  • 17
    • 0031106457 scopus 로고    scopus 로고
    • Where is the globular domain of linker histone located on the nucleosome?
    • Crane-Robinson C. 1997. Where is the globular domain of linker histone located on the nucleosome? Trends Biochem. Sci. 22: 75.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 75
    • Crane-Robinson, C.1
  • 18
    • 0031891003 scopus 로고    scopus 로고
    • NF-Y is associated with the histone acetyltransferases GCN5 and P/CAF
    • Currie R.A. 1998. NF-Y is associated with the histone acetyltransferases GCN5 and P/CAF. J. Biol. Chem. 273: 1430.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1430
    • Currie, R.A.1
  • 19
    • 0032055037 scopus 로고    scopus 로고
    • Covalent modifications of histones: Expression from chromatin templates
    • Davie J. 1998. Covalent modifications of histones: Expression from chromatin templates. Curr. Opin. Genet. Dev. 8: 173.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 173
    • Davie, J.1
  • 20
    • 0032484897 scopus 로고    scopus 로고
    • Transcriptional repression: The cancerchromatin connection
    • DePinho R.A. 1998. Transcriptional repression: The cancerchromatin connection. Nature 391: 533.
    • (1998) Nature , vol.391 , pp. 533
    • DePinho, R.A.1
  • 21
    • 0030003051 scopus 로고    scopus 로고
    • Repression domain of the yeast global repressor Tupl interacts directly with histones H3 and H4
    • Edmondson D.G., Smith M.M., and Roth S.Y. 1996. Repression domain of the yeast global repressor Tupl interacts directly with histones H3 and H4. Genes Dev. 10: 1247.
    • (1996) Genes Dev. , vol.10 , pp. 1247
    • Edmondson, D.G.1    Smith, M.M.2    Roth, S.Y.3
  • 22
    • 0031470152 scopus 로고    scopus 로고
    • Human histone acetyltransferase GCN5 exists in a stable macromolecular complex lacking the adapter ADA2
    • Forsberg E.C., Lam L.T., Yang X.J., Nakatani Y., and Bresnick E.H. 1997. Human histone acetyltransferase GCN5 exists in a stable macromolecular complex lacking the adapter ADA2. Biochemistry 36: 15918.
    • (1997) Biochemistry , vol.36 , pp. 15918
    • Forsberg, E.C.1    Lam, L.T.2    Yang, X.J.3    Nakatani, Y.4    Bresnick, E.H.5
  • 23
    • 0030741529 scopus 로고    scopus 로고
    • Role of histone tails in nucleosome remodeling by Drosophila NURF
    • Georgel P.T., Tsukiyama T., and Wu C. 1997. Role of histone tails in nucleosome remodeling by Drosophila NURF. EMBO J. 16:4717.
    • (1997) EMBO J. , vol.16 , pp. 4717
    • Georgel, P.T.1    Tsukiyama, T.2    Wu, C.3
  • 25
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein M. 1997. Histone acetylation in chromatin structure and transcription. Nature 389: 349.
    • (1997) Nature , vol.389 , pp. 349
    • Grunstein, M.1
  • 26
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu W. and Roeder R.G. 1997. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90: 595.
    • (1997) Cell , vol.90 , pp. 595
    • Gu, W.1    Roeder, R.G.2
  • 27
    • 0028931408 scopus 로고
    • Chromosome condensation induced by fostriecin does not require p34cdc2 kinase activity and histone HI hyperphosphorylation, but is associated with enhanced histone H2A and H3 phosphorylation
    • Guo X.W., Th'ng J.P., Swank R.A., Anderson H.J., Tudan C., Bradbury E.M., and Roberge M. 1995. Chromosome condensation induced by fostriecin does not require p34cdc2 kinase activity and histone HI hyperphosphorylation, but is associated with enhanced histone H2A and H3 phosphorylation. EMBO J. 14:976.
    • (1995) EMBO J. , vol.14 , pp. 976
    • Guo, X.W.1    Th'Ng, J.P.2    Swank, R.A.3    Anderson, H.J.4    Tudan, C.5    Bradbury, E.M.6    Roberge, M.7
  • 28
    • 28944447730 scopus 로고    scopus 로고
    • The core histone amino-termini: Combinatorial interaction domains that link chromatin structure with function
    • Hansen J.C. 1997. The core histone amino-termini: Combinatorial interaction domains that link chromatin structure with function. Chemtracts-Biochem. AM. Biol. 10: 737.
    • (1997) Chemtracts-Biochem. AM. Biol. , vol.10 , pp. 737
    • Hansen, J.C.1
  • 29
    • 0031244521 scopus 로고    scopus 로고
    • Nuclear histone acetylases and deacetylases and transcriptional regulation: HATs off to HDACs
    • Hassig C.A. and Schreiber S.L. 1997. Nuclear histone acetylases and deacetylases and transcriptional regulation: HATs off to HDACs. Curr. Opin. Chem. Biol. 1: 300.
    • (1997) Curr. Opin. Chem. Biol. , vol.1 , pp. 300
    • Hassig, C.A.1    Schreiber, S.L.2
  • 30
    • 0029787814 scopus 로고    scopus 로고
    • Site-directed cleavage of DNA by a linker histone-Fe(II) EDTA conjugate: Localization of a globular domain binding site within a nucleosome
    • Hayes J.J. 1996. Site-directed cleavage of DNA by a linker histone-Fe(II) EDTA conjugate: Localization of a globular domain binding site within a nucleosome. Biochemistry 35: 11931.
    • (1996) Biochemistry , vol.35 , pp. 11931
    • Hayes, J.J.1
  • 31
    • 0027248504 scopus 로고
    • Preferential and asymmetric interaction of linker histones with 5S DNA in the nucleosome
    • Hayes J.J. and Wolffe A.P. 1993. Preferential and asymmetric interaction of linker histones with 5S DNA in the nucleosome. Proc. Natl. Acad. Sci. 90: 6415.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 6415
    • Hayes, J.J.1    Wolffe, A.P.2
  • 32
    • 0028031310 scopus 로고
    • Contacts of the globular domain of histone H5 and core histones with DNA in a "chromatosome"
    • Hayes J.J., Pruss D., and Wolffe A.P. 1994. Contacts of the globular domain of histone H5 and core histones with DNA in a "chromatosome." Proc. Natl. Acad. Sci. 91: 7817.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 7817
    • Hayes, J.J.1    Pruss, D.2    Wolffe, A.P.3
  • 33
    • 0024003456 scopus 로고
    • A direct link between core histone acetylation and transcriptionally active chromatin
    • Hebbes T.R., Thorne A.W., and Crane-Robinson C. 1988. A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J. 7: 1395.
    • (1988) EMBO J. , vol.7 , pp. 1395
    • Hebbes, T.R.1    Thorne, A.W.2    Crane-Robinson, C.3


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