메뉴 건너뛰기




Volumn 52, Issue 39, 2013, Pages 6866-6878

Enzyme-dependent lysine deprotonation in EZH2 catalysis

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTATIONAL MODEL; DIFFERENT SUBSTRATES; EPIGENETIC REGULATION; METHYLTRANSFERASES; PRODUCT SPECIFICITY; S ADENOSYL L METHIONINES; SOLVENT KINETIC ISOTOPE EFFECTS; STEADY STATE RATES;

EID: 84885016465     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400805w     Document Type: Article
Times cited : (17)

References (48)
  • 1
    • 78049402859 scopus 로고    scopus 로고
    • Molecular signals of epigenetic states
    • Bonasio, R., Tu, S., and Reinberg, D. (2010) Molecular signals of epigenetic states Science 330 (6004) 612-616
    • (2010) Science , vol.330 , Issue.6004 , pp. 612-616
    • Bonasio, R.1    Tu, S.2    Reinberg, D.3
  • 2
    • 2642531973 scopus 로고    scopus 로고
    • Epigenetics in human disease and prospects for epigenetic therapy
    • Egger, G., Liang, G., Aparicio, A., and Jones, P. A. (2004) Epigenetics in human disease and prospects for epigenetic therapy Nature 429 (6990) 457-463
    • (2004) Nature , vol.429 , Issue.6990 , pp. 457-463
    • Egger, G.1    Liang, G.2    Aparicio, A.3    Jones, P.A.4
  • 3
    • 84870693696 scopus 로고    scopus 로고
    • Modulation of epigenetic targets for anticancer therapy: Clinicopathological relevance, structural data and drug discovery perspectives
    • Andreoli, F., Barbosa, A. J., Parenti, M. D., and Del, R. A. (2013) Modulation of epigenetic targets for anticancer therapy: Clinicopathological relevance, structural data and drug discovery perspectives Curr. Pharm. Des. 19 (4) 578-613
    • (2013) Curr. Pharm. Des. , vol.19 , Issue.4 , pp. 578-613
    • Andreoli, F.1    Barbosa, A.J.2    Parenti, M.D.3    Del, R.A.4
  • 4
    • 78651268931 scopus 로고    scopus 로고
    • Histone methyltransferases: Regulation of transcription and contribution to human disease
    • Nimura, K., Ura, K., and Kaneda, Y. (2010) Histone methyltransferases: Regulation of transcription and contribution to human disease J. Mol. Med. (Heidelberg, Ger.) 88 (12) 1213-1220
    • (2010) J. Mol. Med. (Heidelberg, Ger.) , vol.88 , Issue.12 , pp. 1213-1220
    • Nimura, K.1    Ura, K.2    Kaneda, Y.3
  • 5
    • 69949148388 scopus 로고    scopus 로고
    • Protein methyltransferases as a target class for drug discovery
    • Copeland, R. A., Solomon, M. E., and Richon, V. M. (2009) Protein methyltransferases as a target class for drug discovery Nat. Rev. Drug Discovery 8 (9) 724-732
    • (2009) Nat. Rev. Drug Discovery , vol.8 , Issue.9 , pp. 724-732
    • Copeland, R.A.1    Solomon, M.E.2    Richon, V.M.3
  • 6
    • 84856466661 scopus 로고    scopus 로고
    • The role of EZH2 in tumour progression
    • Chang, C. J. and Hung, M. C. (2012) The role of EZH2 in tumour progression Br. J. Cancer 106 (2) 243-247
    • (2012) Br. J. Cancer , vol.106 , Issue.2 , pp. 243-247
    • Chang, C.J.1    Hung, M.C.2
  • 8
    • 78650454078 scopus 로고    scopus 로고
    • Coordinated activities of wild-type plus mutant EZH2 drive tumor-associated hypertrimethylation of lysine 27 on histone H3 (H3K27) in human B-cell lymphomas
    • Sneeringer, C. J., Scott, M. P., Kuntz, K. W., Knutson, S. K., Pollock, R. M., Richon, V. M., and Copeland, R. A. (2010) Coordinated activities of wild-type plus mutant EZH2 drive tumor-associated hypertrimethylation of lysine 27 on histone H3 (H3K27) in human B-cell lymphomas Proc. Natl. Acad. Sci. U.S.A. 107 (49) 20980-20985
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , Issue.49 , pp. 20980-20985
    • Sneeringer, C.J.1    Scott, M.P.2    Kuntz, K.W.3    Knutson, S.K.4    Pollock, R.M.5    Richon, V.M.6    Copeland, R.A.7
  • 10
    • 79955513100 scopus 로고    scopus 로고
    • Aberrations of EZH2 in cancer
    • Chase, A. and Cross, N. C. (2011) Aberrations of EZH2 in cancer Clin. Cancer Res. 17 (9) 2613-2618
    • (2011) Clin. Cancer Res. , vol.17 , Issue.9 , pp. 2613-2618
    • Chase, A.1    Cross, N.C.2
  • 11
    • 70349515386 scopus 로고    scopus 로고
    • Polycomb group protein enhancer of zeste 2 is an oncogene that promotes the neoplastic transformation of a benign prostatic epithelial cell line
    • Karanikolas, B. D., Figueiredo, M. L., and Wu, L. (2009) Polycomb group protein enhancer of zeste 2 is an oncogene that promotes the neoplastic transformation of a benign prostatic epithelial cell line Mol. Cancer Res. 7 (9) 1456-1465
    • (2009) Mol. Cancer Res. , vol.7 , Issue.9 , pp. 1456-1465
    • Karanikolas, B.D.1    Figueiredo, M.L.2    Wu, L.3
  • 12
    • 79955119487 scopus 로고    scopus 로고
    • Pharmacologic disruption of Polycomb Repressive Complex 2 inhibits tumorigenicity and tumor progression in prostate cancer
    • Crea, F., Hurt, E. M., Mathews, L. A., Cabarcas, S. M., Sun, L., Marquez, V. E., Danesi, R., and Farrar, W. L. (2011) Pharmacologic disruption of Polycomb Repressive Complex 2 inhibits tumorigenicity and tumor progression in prostate cancer Mol. Cancer 10, 40
    • (2011) Mol. Cancer , vol.10 , pp. 40
    • Crea, F.1    Hurt, E.M.2    Mathews, L.A.3    Cabarcas, S.M.4    Sun, L.5    Marquez, V.E.6    Danesi, R.7    Farrar, W.L.8
  • 13
    • 60149096212 scopus 로고    scopus 로고
    • Downregulation of EZH2 decreases growth of estrogen receptor-negative invasive breast carcinoma and requires BRCA1
    • Gonzalez, M. E., Li, X., Toy, K., DuPrie, M., Ventura, A. C., Banerjee, M., Ljungman, M., Merajver, S. D., and Kleer, C. G. (2009) Downregulation of EZH2 decreases growth of estrogen receptor-negative invasive breast carcinoma and requires BRCA1 Oncogene 28 (6) 843-853
    • (2009) Oncogene , vol.28 , Issue.6 , pp. 843-853
    • Gonzalez, M.E.1    Li, X.2    Toy, K.3    Duprie, M.4    Ventura, A.C.5    Banerjee, M.6    Ljungman, M.7    Merajver, S.D.8    Kleer, C.G.9
  • 16
    • 80455125845 scopus 로고    scopus 로고
    • Structural Chemistry of Human SET Domain Protein Methyltransferases
    • Schapira, M. (2011) Structural Chemistry of Human SET Domain Protein Methyltransferases Curr. Chem. Genomics 5 (Suppl. 1) 85-94
    • (2011) Curr. Chem. Genomics , vol.5 , Issue.SUPPL. 1 , pp. 85-94
    • Schapira, M.1
  • 17
    • 80052591715 scopus 로고    scopus 로고
    • Substrate and product specificities of SET domain methyltransferases
    • Del Rizzo, P. A. and Trievel, R. C. (2011) Substrate and product specificities of SET domain methyltransferases Epigenetics 6 (9) 1059-1067
    • (2011) Epigenetics , vol.6 , Issue.9 , pp. 1059-1067
    • Del Rizzo, P.A.1    Trievel, R.C.2
  • 18
    • 23944509075 scopus 로고    scopus 로고
    • The SET-domain protein superfamily: Protein lysine methyltransferases
    • Dillon, S. C., Zhang, X., Trievel, R. C., and Cheng, X. (2005) The SET-domain protein superfamily: Protein lysine methyltransferases Genome Biol. 6 (8) 227
    • (2005) Genome Biol. , vol.6 , Issue.8 , pp. 227
    • Dillon, S.C.1    Zhang, X.2    Trievel, R.C.3    Cheng, X.4
  • 19
    • 20544461679 scopus 로고    scopus 로고
    • Structural and sequence motifs of protein (histone) methylation enzymes
    • Cheng, X., Collins, R. E., and Zhang, X. (2005) Structural and sequence motifs of protein (histone) methylation enzymes Annu. Rev. Biophys. Biomol. Struct. 34, 267-294
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , pp. 267-294
    • Cheng, X.1    Collins, R.E.2    Zhang, X.3
  • 20
    • 84874789539 scopus 로고    scopus 로고
    • Targeting genetic alterations in protein methyltransferases for personalized cancer therapeutics
    • Copeland, R. A., Moyer, M. P., and Richon, V. M. (2013) Targeting genetic alterations in protein methyltransferases for personalized cancer therapeutics Oncogene 32 (8) 939-946
    • (2013) Oncogene , vol.32 , Issue.8 , pp. 939-946
    • Copeland, R.A.1    Moyer, M.P.2    Richon, V.M.3
  • 21
    • 77950501203 scopus 로고    scopus 로고
    • Mixed lineage leukemia: A structure-function perspective of the MLL1 protein
    • Cosgrove, M. S. and Patel, A. (2010) Mixed lineage leukemia: A structure-function perspective of the MLL1 protein FEBS J. 277 (8) 1832-1842
    • (2010) FEBS J. , vol.277 , Issue.8 , pp. 1832-1842
    • Cosgrove, M.S.1    Patel, A.2
  • 22
    • 22344454519 scopus 로고    scopus 로고
    • Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
    • Couture, J. F., Collazo, E., Brunzelle, J. S., and Trievel, R. C. (2005) Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase Genes Dev. 19 (12) 1455-1465
    • (2005) Genes Dev. , vol.19 , Issue.12 , pp. 1455-1465
    • Couture, J.F.1    Collazo, E.2    Brunzelle, J.S.3    Trievel, R.C.4
  • 25
    • 0042164227 scopus 로고    scopus 로고
    • Structural basis for the product specificity of histone lysine methyltransferases
    • Zhang, X., Yang, Z., Khan, S. I., Horton, J. R., Tamaru, H., Selker, E. U., and Cheng, X. (2003) Structural basis for the product specificity of histone lysine methyltransferases Mol. Cell 12 (1) 177-185
    • (2003) Mol. Cell , vol.12 , Issue.1 , pp. 177-185
    • Zhang, X.1    Yang, Z.2    Khan, S.I.3    Horton, J.R.4    Tamaru, H.5    Selker, E.U.6    Cheng, X.7
  • 26
    • 0037020199 scopus 로고    scopus 로고
    • Structure and catalytic mechanism of a SET domain protein methyltransferase
    • Trievel, R. C., Beach, B. M., Dirk, L. M., Houtz, R. L., and Hurley, J. H. (2002) Structure and catalytic mechanism of a SET domain protein methyltransferase Cell 111 (1) 91-103
    • (2002) Cell , vol.111 , Issue.1 , pp. 91-103
    • Trievel, R.C.1    Beach, B.M.2    Dirk, L.M.3    Houtz, R.L.4    Hurley, J.H.5
  • 27
    • 0037439085 scopus 로고    scopus 로고
    • Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet
    • Kwon, T., Chang, J. H., Kwak, E., Lee, C. W., Joachimiak, A., Kim, Y. C., Lee, J., and Cho, Y. (2003) Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet EMBO J. 22 (2) 292-303
    • (2003) EMBO J. , vol.22 , Issue.2 , pp. 292-303
    • Kwon, T.1    Chang, J.H.2    Kwak, E.3    Lee, C.W.4    Joachimiak, A.5    Kim, Y.C.6    Lee, J.7    Cho, Y.8
  • 29
    • 34547433238 scopus 로고    scopus 로고
    • Mechanism of histone methylation catalyzed by protein lysine methyltransferase SET7/9 and origin of product specificity
    • Guo, H. B. and Guo, H. (2007) Mechanism of histone methylation catalyzed by protein lysine methyltransferase SET7/9 and origin of product specificity Proc. Natl. Acad. Sci. U.S.A. 104 (21) 8797-8802
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , Issue.21 , pp. 8797-8802
    • Guo, H.B.1    Guo, H.2
  • 30
    • 0038419637 scopus 로고    scopus 로고
    • Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT
    • Trievel, R. C., Flynn, E. M., Houtz, R. L., and Hurley, J. H. (2003) Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT Nat. Struct. Biol. 10 (7) 545-552
    • (2003) Nat. Struct. Biol. , vol.10 , Issue.7 , pp. 545-552
    • Trievel, R.C.1    Flynn, E.M.2    Houtz, R.L.3    Hurley, J.H.4
  • 31
    • 45749140396 scopus 로고    scopus 로고
    • Product specificity and mechanism of protein lysine methyltransferases: Insights from the histone lysine methyltransferase SET8
    • Zhang, X. and Bruice, T. C. (2008) Product specificity and mechanism of protein lysine methyltransferases: Insights from the histone lysine methyltransferase SET8 Biochemistry 47 (25) 6671-6677
    • (2008) Biochemistry , vol.47 , Issue.25 , pp. 6671-6677
    • Zhang, X.1    Bruice, T.C.2
  • 32
    • 44449162039 scopus 로고    scopus 로고
    • Enzymatic mechanism and product specificity of SET-domain protein lysine methyltransferases
    • Zhang, X. and Bruice, T. C. (2008) Enzymatic mechanism and product specificity of SET-domain protein lysine methyltransferases Proc. Natl. Acad. Sci. U.S.A. 105 (15) 5728-5732
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , Issue.15 , pp. 5728-5732
    • Zhang, X.1    Bruice, T.C.2
  • 33
    • 40149088321 scopus 로고    scopus 로고
    • Mechanism of product specificity of AdoMet methylation catalyzed by lysine methyltransferases: Transcriptional factor p53 methylation by histone lysine methyltransferase SET7/9
    • Zhang, X. and Bruice, T. C. (2008) Mechanism of product specificity of AdoMet methylation catalyzed by lysine methyltransferases: Transcriptional factor p53 methylation by histone lysine methyltransferase SET7/9 Biochemistry 47 (9) 2743-2748
    • (2008) Biochemistry , vol.47 , Issue.9 , pp. 2743-2748
    • Zhang, X.1    Bruice, T.C.2
  • 34
    • 37349096313 scopus 로고    scopus 로고
    • Histone lysine methyltransferase SET7/9: Formation of a water channel precedes each methyl transfer
    • Zhang, X. and Bruice, T. C. (2007) Histone lysine methyltransferase SET7/9: Formation of a water channel precedes each methyl transfer Biochemistry 46 (51) 14838-14844
    • (2007) Biochemistry , vol.46 , Issue.51 , pp. 14838-14844
    • Zhang, X.1    Bruice, T.C.2
  • 35
    • 34548201646 scopus 로고    scopus 로고
    • A quantum mechanics/molecular mechanics study of the catalytic mechanism and product specificity of viral histone lysine methyltransferase
    • Zhang, X. and Bruice, T. C. (2007) A quantum mechanics/molecular mechanics study of the catalytic mechanism and product specificity of viral histone lysine methyltransferase Biochemistry 46 (34) 9743-9751
    • (2007) Biochemistry , vol.46 , Issue.34 , pp. 9743-9751
    • Zhang, X.1    Bruice, T.C.2
  • 36
    • 34248197964 scopus 로고    scopus 로고
    • Catalytic mechanism and product specificity of rubisco large subunit methyltransferase: QM/MM and MD investigations
    • Zhang, X. and Bruice, T. C. (2007) Catalytic mechanism and product specificity of rubisco large subunit methyltransferase: QM/MM and MD investigations Biochemistry 46 (18) 5505-5514
    • (2007) Biochemistry , vol.46 , Issue.18 , pp. 5505-5514
    • Zhang, X.1    Bruice, T.C.2
  • 37
    • 58549112187 scopus 로고    scopus 로고
    • Structural origins for the product specificity of SET domain protein methyltransferases
    • Couture, J. F., Dirk, L. M., Brunzelle, J. S., Houtz, R. L., and Trievel, R. C. (2008) Structural origins for the product specificity of SET domain protein methyltransferases Proc. Natl. Acad. Sci. U.S.A. 105 (52) 20659-20664
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , Issue.52 , pp. 20659-20664
    • Couture, J.F.1    Dirk, L.M.2    Brunzelle, J.S.3    Houtz, R.L.4    Trievel, R.C.5
  • 40
    • 84879580827 scopus 로고    scopus 로고
    • Convergent evolution of chromatin modification by structurally distinct enzymes: Comparative enzymology of histone H3 Lys27 methylation by human polycomb repressive complex 2 and vSET
    • Swalm, B. M., Hallenbeck, K. K., Majer, C. R., Jin, L., Scott, M. P., Moyer, M. P., Copeland, R. A., and Wigle, T. J. (2013) Convergent evolution of chromatin modification by structurally distinct enzymes: comparative enzymology of histone H3 Lys27 methylation by human polycomb repressive complex 2 and vSET Biochem. J. 453 (2) 241-247
    • (2013) Biochem. J. , vol.453 , Issue.2 , pp. 241-247
    • Swalm, B.M.1    Hallenbeck, K.K.2    Majer, C.R.3    Jin, L.4    Scott, M.P.5    Moyer, M.P.6    Copeland, R.A.7    Wigle, T.J.8
  • 43
    • 0026005186 scopus 로고
    • Human immunodeficiency virus-1 protease. 2. Use of pH rate studies and solvent kinetic isotope effects to elucidate details of chemical mechanism
    • Hyland, L. J., Tomaszek, T. A., Jr., and Meek, T. D. (1991) Human immunodeficiency virus-1 protease. 2. Use of pH rate studies and solvent kinetic isotope effects to elucidate details of chemical mechanism Biochemistry 30 (34) 8454-8463
    • (1991) Biochemistry , vol.30 , Issue.34 , pp. 8454-8463
    • Hyland, L.J.1    Tomaszek Jr., T.A.2    Meek, T.D.3
  • 45
    • 33947615716 scopus 로고    scopus 로고
    • Kinetic manifestation of processivity during multiple methylations catalyzed by SET domain protein methyltransferases
    • Dirk, L. M., Flynn, E. M., Dietzel, K., Couture, J. F., Trievel, R. C., and Houtz, R. L. (2007) Kinetic manifestation of processivity during multiple methylations catalyzed by SET domain protein methyltransferases Biochemistry 46 (12) 3905-3915
    • (2007) Biochemistry , vol.46 , Issue.12 , pp. 3905-3915
    • Dirk, L.M.1    Flynn, E.M.2    Dietzel, K.3    Couture, J.F.4    Trievel, R.C.5    Houtz, R.L.6
  • 46
    • 33646203168 scopus 로고    scopus 로고
    • Structural insights of the specificity and catalysis of a viral histone H3 lysine 27 methyltransferase
    • Qian, C., Wang, X., Manzur, K., Sachchidanand, Farooq, A., Zeng, L., Wang, R., and Zhou, M. M. (2006) Structural insights of the specificity and catalysis of a viral histone H3 lysine 27 methyltransferase J. Mol. Biol. 359 (1) 86-96
    • (2006) J. Mol. Biol. , vol.359 , Issue.1 , pp. 86-96
    • Qian, C.1    Wang, X.2    Manzur, K.3    Sachchidanand4    Farooq, A.5    Zeng, L.6    Wang, R.7    Zhou, M.M.8
  • 47
    • 84961978260 scopus 로고    scopus 로고
    • Direct evidence for methyl group coordination by carbon-oxygen hydrogen bonds in the lysine methyltransferase SET7/9
    • Horowitz, S., Yesselman, J. D., Al-Hashimi, H. M., and Trievel, R. C. (2011) Direct evidence for methyl group coordination by carbon-oxygen hydrogen bonds in the lysine methyltransferase SET7/9 J. Biol. Chem. 286 (21) 18658-18663
    • (2011) J. Biol. Chem. , vol.286 , Issue.21 , pp. 18658-18663
    • Horowitz, S.1    Yesselman, J.D.2    Al-Hashimi, H.M.3    Trievel, R.C.4
  • 48
    • 9744244276 scopus 로고    scopus 로고
    • The use of isotope effects to determine enzyme mechanisms
    • Cleland, W. W. (2005) The use of isotope effects to determine enzyme mechanisms Arch. Biochem. Biophys. 433 (1) 2-12
    • (2005) Arch. Biochem. Biophys. , vol.433 , Issue.1 , pp. 2-12
    • Cleland, W.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.