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Volumn 152, Issue 5, 2012, Pages 453-462

Inhibition of acetyltransferase alters different histone modifications: Probed by small molecule inhibitor plumbagin

Author keywords

histones; inhibitors; KAT; plumbagin; post translational modifications

Indexed keywords

ACYLTRANSFERASE; E1A ASSOCIATED P300 PROTEIN; HISTONE; HISTONE H3; LYSINE; PLUMBAGIN; SERINE;

EID: 84868547961     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvs093     Document Type: Article
Times cited : (7)

References (29)
  • 2
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. (2007) Chromatin modifications and their function. Cell 128, 693-705
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 3
    • 34249299791 scopus 로고    scopus 로고
    • The complex language of chromatin regulation during transcription
    • Berger, S.L. (2007) The complex language of chromatin regulation during transcription. Nature 447, 407-412
    • (2007) Nature , vol.447 , pp. 407-412
    • Berger, S.L.1
  • 4
    • 49349107518 scopus 로고    scopus 로고
    • Lysine acetylation: Codified crosstalk with other posttranslational modifications
    • Yang, X.J. and Seto, E. (2008) Lysine acetylation: codified crosstalk with other posttranslational modifications. Mol. Cell 31, 449-461
    • (2008) Mol. Cell , vol.31 , pp. 449-461
    • Yang, X.J.1    Seto, E.2
  • 5
    • 0032030770 scopus 로고    scopus 로고
    • Histone acetylation and transcriptional regulatory mechanisms
    • Struhl, K. (1998) Histone acetylation and transcriptional regulatory mechanisms. Genes Dev. 12, 599-606
    • (1998) Genes Dev. , vol.12 , pp. 599-606
    • Struhl, K.1
  • 6
    • 2942518343 scopus 로고    scopus 로고
    • Mapping global histone acetylation patterns to gene expression
    • Kurdistani, S.K., Tavazoie, S., and Grunstein, M. (2004) Mapping global histone acetylation patterns to gene expression. Cell 117, 721-733
    • (2004) Cell , vol.117 , pp. 721-733
    • Kurdistani, S.K.1    Tavazoie, S.2    Grunstein, M.3
  • 7
    • 35848936709 scopus 로고    scopus 로고
    • Cross-regulation of histone modifications
    • Latham, J.A. and Dent, S.Y. (2007) Cross-regulation of histone modifications. Nat. Struct. Mol. Biol. 14, 1017-1024
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 1017-1024
    • Latham, J.A.1    Dent, S.Y.2
  • 8
    • 51949111451 scopus 로고    scopus 로고
    • Chemical probes for histone-modifying enzymes
    • Cole, P.A. (2008) Chemical probes for histone-modifying enzymes. Nat. Chem. Biol. 4, 590-597
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 590-597
    • Cole, P.A.1
  • 9
    • 78649855810 scopus 로고    scopus 로고
    • Small molecule modulators of histone acetylation and methylation: A disease perspective
    • Selvi, B.R., Mohankrishna, D.V., Ostwal, Y.B., and Kundu, T.K. (2010) Small molecule modulators of histone acetylation and methylation: a disease perspective. Biochim. Biophys. Acta 1799, 810-828
    • (2010) Biochim. Biophys. Acta , vol.1799 , pp. 810-828
    • Selvi, B.R.1    Mohankrishna, D.V.2    Ostwal, Y.B.3    Kundu, T.K.4
  • 10
    • 33947492804 scopus 로고    scopus 로고
    • Cross-talk between histone modifications in response to histone deacetylase inhibitors: MLL4 links histone H3 acetylation and histone H3K4 methylation
    • Nightingale, K.P., Gendreizig, S., White, D.A., Bradbury, C, Hollfelder, F., and Turner, B.M. (2007) Cross-talk between histone modifications in response to histone deacetylase inhibitors: MLL4 links histone H3 acetylation and histone H3K4 methylation. J. Biol. Chem. 282, 4408-4416
    • (2007) J. Biol. Chem. , vol.282 , pp. 4408-4416
    • Nightingale, K.P.1    Gendreizig, S.2    White, D.A.3    Bradbury, C.4    Hollfelder, F.5    Turner, B.M.6
  • 11
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coac-tivators p300 and CBP are histone acetyltransferases
    • Ogryzko, V.V., Schiltz, R.L., Russanova, V., Howard, B.H., and Nakatani, Y. (1996) The transcriptional coac-tivators p300 and CBP are histone acetyltransferases. Cell 87, 953-959
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 12
    • 0034916613 scopus 로고    scopus 로고
    • P300/CBP proteins: HATs for transcriptional bridges and scaffolds
    • Chan, H.M. and La Thangue, N.B. (2001) p300/CBP proteins: HATs for transcriptional bridges and scaffolds. J. Cell Sci. 114, 2363-2373
    • (2001) J. Cell Sci. , vol.114 , pp. 2363-2373
    • Chan, H.M.1    La Thangue, N.B.2
  • 13
    • 0034234237 scopus 로고    scopus 로고
    • CBP/p300 in cell growth, transformation, and development
    • Goodman, R.H. and Smolik, S. (2000) CBP/p300 in cell growth, transformation, and development. Genes Dev. 14, 1553-1577
    • (2000) Genes Dev. , vol.14 , pp. 1553-1577
    • Goodman, R.H.1    Smolik, S.2
  • 16
    • 10944243759 scopus 로고    scopus 로고
    • Curcumin, a novel p300/CREB-binding protein-specific inhibitor of acetyltrans-ferase, represses the acetylation of histone/nonhistone proteins and histone acetyltransferase-dependent chromatin transcription
    • Balasubramanyam, K, Varier, R.A., Altaf, M., Swaminathan, V., Siddappa, N.B., Ranga, U., and Kundu, T.K. (2004) Curcumin, a novel p300/CREB-binding protein-specific inhibitor of acetyltrans-ferase, represses the acetylation of histone/nonhistone proteins and histone acetyltransferase-dependent chromatin transcription. J. Biol. Chem. 279, 51163-51171
    • (2004) J. Biol. Chem. , vol.279 , pp. 51163-51171
    • Balasubramanyam, K.1    Varier, R.A.2    Altaf, M.3    Swaminathan, V.4    Siddappa, N.B.5    Ranga, U.6    Kundu, T.K.7
  • 17
    • 0027989808 scopus 로고
    • Annexin v for flow cytometric detection of phosphati-dylserine expression on B cells undergoing apoptosis
    • Koopman, G, Reutelingsperger, C.P., Kuijten, G A., Keehnen, R.M., Pals, ST, and van Oers, M.H. (1994) Annexin V for flow cytometric detection of phosphati-dylserine expression on B cells undergoing apoptosis. Blood 84, 1415-1420
    • (1994) Blood , vol.84 , pp. 1415-1420
    • Koopman, G.1    Reutelingsperger, C.P.2    Kuijten, G.A.3    Keehnen, R.M.4    Pals, S.T.5    Van Oers, M.H.6
  • 18
    • 1642498276 scopus 로고    scopus 로고
    • Cytotoxic action of juglone and plumbagin: A mechanistic study using HaCaT keratinocytes
    • Inbaraj, J.J. and Chignell, C.F. (2004) Cytotoxic action of juglone and plumbagin: a mechanistic study using HaCaT keratinocytes. Chem. Res. Toxicol. 17, 55-62
    • (2004) Chem. Res. Toxicol. , vol.17 , pp. 55-62
    • Inbaraj, J.J.1    Chignell, C.F.2
  • 19
    • 58049202263 scopus 로고    scopus 로고
    • Cytotoxicity mechanism of two naphthoquinones (menadione and plumbagin) in Saccharomyces cerevisiae
    • Castro, F.A., Mariani, D., Panek, A.D., Eleutherio, E.C., and Pereira, N.D. (2008) Cytotoxicity mechanism of two naphthoquinones (menadione and plumbagin) in Saccharomyces cerevisiae. Plos One 3, e3999
    • (2008) Plos One , vol.3
    • Castro, F.A.1    Mariani, D.2    Panek, A.D.3    Eleutherio, E.C.4    Pereira, N.D.5
  • 21
    • 79956367114 scopus 로고    scopus 로고
    • Dynamic acetylation of all lysine-4 trimethylated histone H3 is evolutionarily conserved and mediated by p300/CBP
    • Crump, N.T., Hazzalin, C.A., Bowers, E.M., Alani, R.M., Cole, P.A., and Mahadevan, L.C. (2011) Dynamic acetylation of all lysine-4 trimethylated histone H3 is evolutionarily conserved and mediated by p300/CBP. Proc. Natl Acad. Sci. USA 108, 7814-7819
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 7814-7819
    • Crump, N.T.1    Hazzalin, C.A.2    Bowers, E.M.3    Alani, R.M.4    Cole, P.A.5    Mahadevan, L.C.6
  • 22
    • 29144463657 scopus 로고    scopus 로고
    • Dynamic acetylation of all lysine 4-methylated histone H3 in the mouse nucleus: Analysis at c-fos and c-jun
    • Hazzalin, C.A. and Mahadevan, L.C. (2005) Dynamic acetylation of all lysine 4-methylated histone H3 in the mouse nucleus: analysis at c-fos and c-jun. PLoS Biol. 3, e393
    • (2005) PLoS Biol , vol.3
    • Hazzalin, C.A.1    Mahadevan, L.C.2
  • 23
    • 35349006314 scopus 로고    scopus 로고
    • Histone lysine demethylases: Emerging roles in development, physiology and disease
    • Shi, Y. (2007) Histone lysine demethylases: emerging roles in development, physiology and disease. Nat. Rev. Genet. 8, 829-833
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 829-833
    • Shi, Y.1
  • 24
    • 0035694922 scopus 로고    scopus 로고
    • Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase
    • Wang, H., Cao, R., Xia, L., Erdjument-Bromage, H, Borchers, C, Tempst, P., and Zhang, Y. (2001) Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. Mol. Cell 8, 1207-1217
    • (2001) Mol. Cell , vol.8 , pp. 1207-1217
    • Wang, H.1    Cao, R.2    Xia, L.3    Erdjument-Bromage, H.4    Borchers, C.5    Tempst, P.6    Zhang, Y.7
  • 26
    • 0033638105 scopus 로고    scopus 로고
    • Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14
    • Lo, W.S., Trievel, R.C., Rojas, J.R., Duggan, L., Hsu, J.Y., Allis, CD., Marmorstein, R., and Berger, S.L. (2000) Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14. Mol. Cell 5, 917-926
    • (2000) Mol. Cell , vol.5 , pp. 917-926
    • Lo, W.S.1    Trievel, R.C.2    Rojas, J.R.3    Duggan, L.4    Hsu, J.Y.5    Allis, C.D.6    Marmorstein, R.7    Berger, S.L.8
  • 27
    • 0033636595 scopus 로고    scopus 로고
    • Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation
    • Cheung, P., Tanner, K.G, Cheung, W.L., Sassone-Corsi, P., Denu, J.M., and Allis, CD. (2000) Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation. Mol. Cell5, 905-915
    • (2000) Mol. Cell , vol.5 , pp. 905-915
    • Cheung, P.1    Tanner, K.G.2    Cheung, W.L.3    Sassone-Corsi, P.4    Denu, J.M.5    Allis, C.D.6
  • 28
    • 0034679625 scopus 로고    scopus 로고
    • Phosphoacetylation of histone H3 on c-fos-and c-jun-associated nucleosomes upon gene activation
    • Clayton, A.L., Rose, S., Barratt, M.J., and Mahadevan, L.C. (2000) Phosphoacetylation of histone H3 on c-fos-and c-jun-associated nucleosomes upon gene activation. EMBO J. 19, 3714-3726
    • (2000) EMBO J. , vol.19 , pp. 3714-3726
    • Clayton, A.L.1    Rose, S.2    Barratt, M.J.3    Mahadevan, L.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.