메뉴 건너뛰기




Volumn 12, Issue 24, 2002, Pages 2090-2097

Crosstalk between CARM1 methylation and CBP acetylation on histone H3

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; ARGININE; COACTIVATOR ASSOCIATED ARGININE METHYLTRANSFERASE 1; COACTIVATOR-ASSOCIATED ARGININE METHYLTRANSFERASE 1; CREBBP PROTEIN, HUMAN; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; ESTROGEN; HISTONE; LYSINE; NUCLEAR PROTEIN; PROTEIN ARGININE METHYLTRANSFERASE; RECOMBINANT PROTEIN; TRANSACTIVATOR PROTEIN;

EID: 0037164736     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(02)01387-8     Document Type: Article
Times cited : (263)

References (37)
  • 1
    • 0036532026 scopus 로고    scopus 로고
    • Histone modifications in transcriptional regulation
    • Berger, S.L. (2002). Histone modifications in transcriptional regulation. Curr. Opin. Genet. Dev. 12, 142-148.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 142-148
    • Berger, S.L.1
  • 2
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun, Z.W., and Allis, C.D. (2002). Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature 418, 104-108.
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 3
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B.D., and Allis, C.D. (2000). The language of covalent histone modifications. Nature 403, 41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 4
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T., and Allis, C.D. (2001). Translating the histone code. Science 293, 1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 5
    • 0035377556 scopus 로고    scopus 로고
    • Protein modules that manipulate histone tails for chromatin regulation
    • Marmorstein, R. (2001). Protein modules that manipulate histone tails for chromatin regulation. Nat. Rev. Mol. Cell. Biol. 2, 422-432.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 422-432
    • Marmorstein, R.1
  • 6
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner, D.E., and Berger, S.L. (2000). Acetylation of histones and transcription-related factors. Microbiol. Mol. Biol. Rev. 64, 435-459.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 7
    • 33947482638 scopus 로고
    • The occurrence of ε-N-methyl lysine in histones
    • Murray, K. (1964). The occurrence of ε-N-methyl lysine in histones. Biochemistry 3, 10-15.
    • (1964) Biochemistry , vol.3 , pp. 10-15
    • Murray, K.1
  • 8
    • 0035883954 scopus 로고    scopus 로고
    • Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails
    • Zhang, Y., and Reinberg, D. (2001). Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails. Genes Dev. 15, 2343-2360.
    • (2001) Genes Dev. , vol.15 , pp. 2343-2360
    • Zhang, Y.1    Reinberg, D.2
  • 9
    • 0036532202 scopus 로고    scopus 로고
    • Histone methylation in transcriptional control
    • Kouzarides, T. (2002). Histone methylation in transcriptional control. Curr. Opin. Genet. Dev. 12, 198-209.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 198-209
    • Kouzarides, T.1
  • 10
    • 0032032823 scopus 로고    scopus 로고
    • Protein methylation: A signal event in post-translational modification
    • Aletta, J.M., Cimato, T.R., and Ettinger, M.J. (1998). Protein methylation: A signal event in post-translational modification. Trends Biochem. Sci. 23, 89-91.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 89-91
    • Aletta, J.M.1    Cimato, T.R.2    Ettinger, M.J.3
  • 15
    • 0035846953 scopus 로고    scopus 로고
    • Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities
    • Koh, S.S., Chen, D., Lee, Y.H., and Stallcup, M.R. (2001). Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities. J. Biol. Chem. 276, 1089-1098.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1089-1098
    • Koh, S.S.1    Chen, D.2    Lee, Y.H.3    Stallcup, M.R.4
  • 16
  • 17
    • 0036093624 scopus 로고    scopus 로고
    • Synergy among nuclear receptor coactivators: Selective requirement for protein methyltransferase and acetyltransferase activities
    • Lee, Y.H., Koh, S.S., Zhang, X., Cheng, X., and Stallcup, M.R. (2002). Synergy among nuclear receptor coactivators: Selective requirement for protein methyltransferase and acetyltransferase activities. Mol. Cell. Biol. 22, 3621-3632.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3621-3632
    • Lee, Y.H.1    Koh, S.S.2    Zhang, X.3    Cheng, X.4    Stallcup, M.R.5
  • 18
    • 0036311564 scopus 로고    scopus 로고
    • Involvement of histone methylation and phosphorylation in regulation of transcription by thyroid hormone receptor
    • Li, J., Lin, Q., Yoon, H.G., Huang, Z.Q., Strahl, B.D., Allis, C.D., and Wong, J. (2002). Involvement of histone methylation and phosphorylation in regulation of transcription by thyroid hormone receptor. Mol. Cell. Biol. 22, 5688-5697.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5688-5697
    • Li, J.1    Lin, Q.2    Yoon, H.G.3    Huang, Z.Q.4    Strahl, B.D.5    Allis, C.D.6    Wong, J.7
  • 20
    • 0034731452 scopus 로고    scopus 로고
    • Synergistic, p160 coactivator-dependent enhancement of estrogen receptor function by CARM1 and p300
    • Chen, D., Huang, S.M., and Stallcup, M.R, (2000). Synergistic, p160 coactivator-dependent enhancement of estrogen receptor function by CARM1 and p300, J. Biol. Chem. 275, 40810-40816.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40810-40816
    • Chen, D.1    Huang, S.M.2    Stallcup, M.R.3
  • 21
    • 0033615656 scopus 로고    scopus 로고
    • The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity
    • Pollack, B.P., Kotenko, S.V., He, W., Izotova, L.S., Barnoski, B.L., and Pestka, S. (1999). The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity. J. Biol. Chem. 274, 31531-31542.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31531-31542
    • Pollack, B.P.1    Kotenko, S.V.2    He, W.3    Izotova, L.S.4    Barnoski, B.L.5    Pestka, S.6
  • 23
    • 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, C.D., 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
  • 24
    • 0034644473 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications
    • Cheung, P., Allis, C.D., and Sassone-Corsi, P. (2000). Signaling to chromatin through histone modifications. Cell 103, 263-271.
    • (2000) Cell , vol.103 , pp. 263-271
    • Cheung, P.1    Allis, C.D.2    Sassone-Corsi, P.3
  • 25
    • 0035839135 scopus 로고    scopus 로고
    • Snf1-a histone kinase that works in concert with the histone acetyltransferase gcn5 to regulate transcription
    • Lo, W.S., Duggan, L., Tolga, N.C., Emre, Belotserkovskya, R., Lane, W.S., Shiekhattar, R., and Berger, S.L. (2001). Snf1-a histone kinase that works in concert with the histone acetyltransferase gcn5 to regulate transcription. Science 293, 1142-1146.
    • (2001) Science , vol.293 , pp. 1142-1146
    • Lo, W.S.1    Duggan, L.2    Tolga, N.C.3    Emre4    Belotserkovskya, R.5    Lane, W.S.6    Shiekhattar, R.7    Berger, S.L.8
  • 26
    • 0035146586 scopus 로고    scopus 로고
    • Binding of TATA binding protein to a naturally positioned nucleosome is facilitated by histone acetylation
    • Sewack, G.F., Ellis, T.W., and Hansen, U. (2001). Binding of TATA binding protein to a naturally positioned nucleosome is facilitated by histone acetylation. Mol. Cell. Biol. 21, 1404-1415.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1404-1415
    • Sewack, G.F.1    Ellis, T.W.2    Hansen, U.3
  • 28
    • 0034968667 scopus 로고    scopus 로고
    • Structure and function of histone acetyltransferases
    • Marmorstein, R. (2001). Structure and function of histone acetyltransferases. Cell. Mol. Life Sci. 58, 693-703.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 693-703
    • Marmorstein, R.1
  • 29
    • 0033637703 scopus 로고    scopus 로고
    • Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription
    • Shang, Y., Hu, X., DiRenzo, J., Lazar, M.A., and Brown, M. (2000). Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell 103, 843-852.
    • (2000) Cell , vol.103 , pp. 843-852
    • Shang, Y.1    Hu, X.2    DiRenzo, J.3    Lazar, M.A.4    Brown, M.5
  • 31
    • 0033397841 scopus 로고    scopus 로고
    • Preparation of site-specific antibodies to acetylated histones
    • White, D.A., Belyaev, N.D., and Turner, B.M. (1999). Preparation of site-specific antibodies to acetylated histones. Methods 19, 417-424.
    • (1999) Methods , vol.19 , pp. 417-424
    • White, D.A.1    Belyaev, N.D.2    Turner, B.M.3
  • 33
    • 0031080378 scopus 로고    scopus 로고
    • Analysis of chromatin structure by in vivo formaldehyde cross-linking
    • Orlando, V., Strutt, H., and Paro, R. (1997). Analysis of chromatin structure by in vivo formaldehyde cross-linking. Methods 11, 205-214.
    • (1997) Methods , vol.11 , pp. 205-214
    • Orlando, V.1    Strutt, H.2    Paro, R.3
  • 35
    • 0033924890 scopus 로고    scopus 로고
    • Parent-of-origin specific histone acetylation and reactivation of a key imprinted gene locus in Prader-Willi syndrome
    • Saitoh, S., and Wada, T. (2000). Parent-of-origin specific histone acetylation and reactivation of a key imprinted gene locus in Prader-Willi syndrome. Am. J. Hum. Genet. 66, 1958-1962.
    • (2000) Am. J. Hum. Genet. , vol.66 , pp. 1958-1962
    • Saitoh, S.1    Wada, T.2
  • 36
    • 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, 641-643.
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 37
    • 0030725367 scopus 로고    scopus 로고
    • Nucleosome positioning and transcription-associated chromatin alterations on the human estrogen-responsive pS2 promoter
    • Sewack, G.F., and Hansen, U. (1997). Nucleosome positioning and transcription-associated chromatin alterations on the human estrogen-responsive pS2 promoter. J. Biol. Chem. 272, 31118-31129.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31118-31129
    • Sewack, G.F.1    Hansen, U.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.