메뉴 건너뛰기




Volumn 7, Issue 3, 2012, Pages

Function of the active site lysine autoacetylation in Tip60 catalysis

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CYSTEINE; GLUTAMIC ACID; HISTONE ACETYLTRANSFERASE; HIV TAT INTERACTIVE PROTEIN 60; LYSINE; TRANSACTIVATOR PROTEIN; UNCLASSIFIED DRUG; ACETYL COENZYME A; KAT5 PROTEIN, HUMAN; RECOMBINANT PROTEIN;

EID: 84859045769     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0032886     Document Type: Article
Times cited : (36)

References (63)
  • 1
    • 59449087016 scopus 로고    scopus 로고
    • Histone modifying enzymes: structures, mechanisms, and specificities
    • Marmorstein R, Trievel RC, (2009) Histone modifying enzymes: structures, mechanisms, and specificities. Biochim Biophys Acta 1789: 58-68.
    • (2009) Biochim Biophys Acta , vol.1789 , pp. 58-68
    • Marmorstein, R.1    Trievel, R.C.2
  • 2
    • 2342599619 scopus 로고    scopus 로고
    • The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases
    • Yang XJ, (2004) The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases. Nucleic Acids Res 32: 959-976.
    • (2004) Nucleic Acids Res , vol.32 , pp. 959-976
    • Yang, X.J.1
  • 3
    • 0037242383 scopus 로고    scopus 로고
    • The MYST family of histone acetyltransferases
    • Utley RT, Cote J, (2003) The MYST family of histone acetyltransferases. Curr Top Microbiol Immunol 274: 203-236.
    • (2003) Curr Top Microbiol Immunol , vol.274 , pp. 203-236
    • Utley, R.T.1    Cote, J.2
  • 4
    • 9744255506 scopus 로고    scopus 로고
    • Structure and functions of the GNAT superfamily of acetyltransferases
    • Vetting MW, LP SdC, Yu M, Hegde SS, Magnet S, et al. (2005) Structure and functions of the GNAT superfamily of acetyltransferases. Arch Biochem Biophys 433: 212-226.
    • (2005) Arch Biochem Biophys , vol.433 , pp. 212-226
    • Vetting, M.W.1    Lp, S.D.C.2    Yu, M.3    Hegde, S.S.4    Magnet, S.5
  • 5
    • 33947532026 scopus 로고    scopus 로고
    • Histone acetyltransferase complexes: one size doesn't fit all
    • Lee KK, Workman JL, (2007) Histone acetyltransferase complexes: one size doesn't fit all. Nat Rev Mol Cell Biol 8: 284-295.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 284-295
    • Lee, K.K.1    Workman, J.L.2
  • 7
    • 6044256118 scopus 로고    scopus 로고
    • Histones and histone modifications
    • Peterson CL, Laniel MA, (2004) Histones and histone modifications. Curr Biol 14: R546-551.
    • (2004) Curr Biol , vol.14
    • Peterson, C.L.1    Laniel, M.A.2
  • 9
    • 25444476733 scopus 로고    scopus 로고
    • DNA repair in the context of chromatin
    • Morrison AJ, Shen X, (2005) DNA repair in the context of chromatin. Cell Cycle 4: 568-571.
    • (2005) Cell Cycle , vol.4 , pp. 568-571
    • Morrison, A.J.1    Shen, X.2
  • 10
    • 34249793251 scopus 로고    scopus 로고
    • Histone acetylation and methylation: combinatorial players for transcriptional regulation
    • An W, (2007) Histone acetylation and methylation: combinatorial players for transcriptional regulation. Subcell Biochem 41: 351-369.
    • (2007) Subcell Biochem , vol.41 , pp. 351-369
    • An, W.1
  • 11
    • 0034968667 scopus 로고    scopus 로고
    • Structure and function of histone acetyltransferases
    • Marmorstein R, (2001) Structure and function of histone acetyltransferases. Cellular & Molecular Life Sciences 58: 693-703.
    • (2001) Cellular & Molecular Life Sciences , vol.58 , pp. 693-703
    • Marmorstein, R.1
  • 12
    • 57049120143 scopus 로고    scopus 로고
    • Structure and chemistry of the p300/CBP and Rtt109 histone acetyltransferases: implications for histone acetyltransferase evolution and function
    • Wang L, Tang Y, Cole PA, Marmorstein R, (2008) Structure and chemistry of the p300/CBP and Rtt109 histone acetyltransferases: implications for histone acetyltransferase evolution and function. Curr Opin Struct Biol 18: 741-747.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 741-747
    • Wang, L.1    Tang, Y.2    Cole, P.A.3    Marmorstein, R.4
  • 13
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner DE, Berger SL, (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
  • 15
    • 32444434989 scopus 로고    scopus 로고
    • Histone H4-K16 acetylation controls chromatin structure and protein interactions
    • Shogren-Knaak M, Ishii H, Sun JM, Pazin MJ, Davie JR, et al. (2006) Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 311: 844-847.
    • (2006) Science , vol.311 , pp. 844-847
    • Shogren-Knaak, M.1    Ishii, H.2    Sun, J.M.3    Pazin, M.J.4    Davie, J.R.5
  • 16
    • 77149148756 scopus 로고    scopus 로고
    • Regulation of cellular metabolism by protein lysine acetylation
    • Zhao S, Xu W, Jiang W, Yu W, Lin Y, et al. (2010) Regulation of cellular metabolism by protein lysine acetylation. Science 327: 1000-1004.
    • (2010) Science , vol.327 , pp. 1000-1004
    • Zhao, S.1    Xu, W.2    Jiang, W.3    Yu, W.4    Lin, Y.5
  • 17
    • 77149120797 scopus 로고    scopus 로고
    • Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux
    • Wang Q, Zhang Y, Yang C, Xiong H, Lin Y, et al. (2010) Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux. Science 327: 1004-1007.
    • (2010) Science , vol.327 , pp. 1004-1007
    • Wang, Q.1    Zhang, Y.2    Yang, C.3    Xiong, H.4    Lin, Y.5
  • 18
    • 62149143727 scopus 로고    scopus 로고
    • Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis
    • Lin YY, Lu JY, Zhang J, Walter W, Dang W, et al. (2009) Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis. Cell 136: 1073-1084.
    • (2009) Cell , vol.136 , pp. 1073-1084
    • Lin, Y.Y.1    Lu, J.Y.2    Zhang, J.3    Walter, W.4    Dang, W.5
  • 19
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, et al. (2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325: 834-840.
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5
  • 20
    • 56049090769 scopus 로고    scopus 로고
    • Acetylation of non-histone proteins modulates cellular signalling at multiple levels
    • Spange S, Wagner T, Heinzel T, Kramer OH, (2009) Acetylation of non-histone proteins modulates cellular signalling at multiple levels. Int J Biochem Cell Biol 41: 185-198.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 185-198
    • Spange, S.1    Wagner, T.2    Heinzel, T.3    Kramer, O.H.4
  • 21
  • 22
    • 18844385730 scopus 로고    scopus 로고
    • Gene expression analysis of the function of the male-specific lethal complex in Drosophila
    • Bhadra MP, Bhadra U, Kundu J, Birchler JA, (2005) Gene expression analysis of the function of the male-specific lethal complex in Drosophila. Genetics 169: 2061-2074.
    • (2005) Genetics , vol.169 , pp. 2061-2074
    • Bhadra, M.P.1    Bhadra, U.2    Kundu, J.3    Birchler, J.A.4
  • 24
    • 12344284062 scopus 로고    scopus 로고
    • Imprinting and looping: epigenetic marks control interactions between regulatory elements
    • Kato Y, Sasaki H, (2005) Imprinting and looping: epigenetic marks control interactions between regulatory elements. Bioessays 27: 1-4.
    • (2005) Bioessays , vol.27 , pp. 1-4
    • Kato, Y.1    Sasaki, H.2
  • 25
    • 79953712902 scopus 로고    scopus 로고
    • MYST-family histone acetyltransferases: beyond chromatin
    • Sapountzi V, Cote J, (2010) MYST-family histone acetyltransferases: beyond chromatin. Cellular and Molecular Life Sciences 68: 1147-1156.
    • (2010) Cellular and Molecular Life Sciences , vol.68 , pp. 1147-1156
    • Sapountzi, V.1    Cote, J.2
  • 26
    • 0037306843 scopus 로고    scopus 로고
    • Quantification of histone acetyltransferase and histone deacetylase transcripts during early bovine embryo development
    • McGraw S, Robert C, Massicotte L, Sirard MA, (2003) Quantification of histone acetyltransferase and histone deacetylase transcripts during early bovine embryo development. Biol Reprod 68: 383-389.
    • (2003) Biol Reprod , vol.68 , pp. 383-389
    • McGraw, S.1    Robert, C.2    Massicotte, L.3    Sirard, M.A.4
  • 27
    • 34249779851 scopus 로고    scopus 로고
    • Functions of myst family histone acetyltransferases and their link to disease
    • Avvakumov N, Cote J, (2007) Functions of myst family histone acetyltransferases and their link to disease. Subcell Biochem 41: 295-317.
    • (2007) Subcell Biochem , vol.41 , pp. 295-317
    • Avvakumov, N.1    Cote, J.2
  • 28
    • 50249091120 scopus 로고    scopus 로고
    • Chemical regulation of epigenetic modifications: Opportunities for new cancer therapy
    • Zheng YG, Wu J, Chen Z, Goodman M, (2008) Chemical regulation of epigenetic modifications: Opportunities for new cancer therapy. Med Res Rev 28: 645-687.
    • (2008) Med Res Rev , vol.28 , pp. 645-687
    • Zheng, Y.G.1    Wu, J.2    Chen, Z.3    Goodman, M.4
  • 29
    • 0029961534 scopus 로고    scopus 로고
    • Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator
    • Kamine J, Elangovan B, Subramanian T, Coleman D, Chinnadurai G, (1996) Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator. Virology 216: 357-366.
    • (1996) Virology , vol.216 , pp. 357-366
    • Kamine, J.1    Elangovan, B.2    Subramanian, T.3    Coleman, D.4    Chinnadurai, G.5
  • 30
    • 0033529253 scopus 로고    scopus 로고
    • Control of the histone-acetyltransferase activity of Tip60 by the HIV-1 transactivator protein, Tat
    • Creaven M, Hans F, Mutskov V, Col E, Caron C, et al. (1999) Control of the histone-acetyltransferase activity of Tip60 by the HIV-1 transactivator protein, Tat. Biochemistry 38: 8826-8830.
    • (1999) Biochemistry , vol.38 , pp. 8826-8830
    • Creaven, M.1    Hans, F.2    Mutskov, V.3    Col, E.4    Caron, C.5
  • 31
    • 0032467640 scopus 로고    scopus 로고
    • Tip60 acetylates six lysines of a specific class in core histones in vitro
    • Kimura A, Horikoshi M, (1998) Tip60 acetylates six lysines of a specific class in core histones in vitro. Genes Cells 3: 789-800.
    • (1998) Genes Cells , vol.3 , pp. 789-800
    • Kimura, A.1    Horikoshi, M.2
  • 33
    • 37549028411 scopus 로고    scopus 로고
    • DNA damage-induced acetylation of lysine 3016 of ATM activates ATM kinase activity
    • Sun Y, Xu Y, Roy K, Price BD, (2007) DNA damage-induced acetylation of lysine 3016 of ATM activates ATM kinase activity. Mol Cell Biol 27: 8502-8509.
    • (2007) Mol Cell Biol , vol.27 , pp. 8502-8509
    • Sun, Y.1    Xu, Y.2    Roy, K.3    Price, B.D.4
  • 34
    • 24944516931 scopus 로고    scopus 로고
    • A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM
    • Sun Y, Jiang X, Chen S, Fernandes N, Price BD, (2005) A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM. Proc Natl Acad Sci U S A 102: 13182-13187.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 13182-13187
    • Sun, Y.1    Jiang, X.2    Chen, S.3    Fernandes, N.4    Price, B.D.5
  • 35
    • 33845668241 scopus 로고    scopus 로고
    • Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis
    • Tang Y, Luo J, Zhang W, Gu W, (2006) Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis. Mol Cell 24: 827-839.
    • (2006) Mol Cell , vol.24 , pp. 827-839
    • Tang, Y.1    Luo, J.2    Zhang, W.3    Gu, W.4
  • 36
    • 33845656738 scopus 로고    scopus 로고
    • Acetylation of the p53 DNA-binding domain regulates apoptosis induction
    • Sykes SM, Mellert HS, Holbert MA, Li K, Marmorstein R, et al. (2006) Acetylation of the p53 DNA-binding domain regulates apoptosis induction. Mol Cell 24: 841-851.
    • (2006) Mol Cell , vol.24 , pp. 841-851
    • Sykes, S.M.1    Mellert, H.S.2    Holbert, M.A.3    Li, K.4    Marmorstein, R.5
  • 37
    • 0041590889 scopus 로고    scopus 로고
    • MYC recruits the TIP60 histone acetyltransferase complex to chromatin
    • Frank SR, Parisi T, Taubert S, Fernandez P, Fuchs M, et al. (2003) MYC recruits the TIP60 histone acetyltransferase complex to chromatin. EMBO Rep 4: 575-580.
    • (2003) EMBO Rep , vol.4 , pp. 575-580
    • Frank, S.R.1    Parisi, T.2    Taubert, S.3    Fernandez, P.4    Fuchs, M.5
  • 38
    • 33846940901 scopus 로고    scopus 로고
    • Histone deacetylase 3 interacts with and deacetylates myocyte enhancer factor 2
    • Gregoire S, Xiao L, Nie J, Zhang X, Xu M, et al. (2007) Histone deacetylase 3 interacts with and deacetylates myocyte enhancer factor 2. Mol Cell Biol 27: 1280-1295.
    • (2007) Mol Cell Biol , vol.27 , pp. 1280-1295
    • Gregoire, S.1    Xiao, L.2    Nie, J.3    Zhang, X.4    Xu, M.5
  • 39
    • 0037067655 scopus 로고    scopus 로고
    • Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and beta-amyloid precursor protein
    • Baek SH, Ohgi KA, Rose DW, Koo EH, Glass CK, et al. (2002) Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and beta-amyloid precursor protein. Cell 110: 55-67.
    • (2002) Cell , vol.110 , pp. 55-67
    • Baek, S.H.1    Ohgi, K.A.2    Rose, D.W.3    Koo, E.H.4    Glass, C.K.5
  • 40
    • 0033519690 scopus 로고    scopus 로고
    • The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators
    • Dechend R, Hirano F, Lehmann K, Heissmeyer V, Ansieau S, et al. (1999) The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators. Oncogene 18: 3316-3323.
    • (1999) Oncogene , vol.18 , pp. 3316-3323
    • Dechend, R.1    Hirano, F.2    Lehmann, K.3    Heissmeyer, V.4    Ansieau, S.5
  • 41
    • 1242339706 scopus 로고    scopus 로고
    • E2F and Sp1/Sp3 Synergize but are not sufficient to activate the MYCN gene in neuroblastomas
    • Kramps C, Strieder V, Sapetschnig A, Suske G, Lutz W, (2004) E2F and Sp1/Sp3 Synergize but are not sufficient to activate the MYCN gene in neuroblastomas. J Biol Chem 279: 5110-5117.
    • (2004) J Biol Chem , vol.279 , pp. 5110-5117
    • Kramps, C.1    Strieder, V.2    Sapetschnig, A.3    Suske, G.4    Lutz, W.5
  • 43
    • 7244253057 scopus 로고    scopus 로고
    • Role of the histone acetyl transferase Tip60 in the p53 pathway
    • Legube G, Linares LK, Tyteca S, Caron C, Scheffner M, et al. (2004) Role of the histone acetyl transferase Tip60 in the p53 pathway. J Biol Chem 279: 44825-44833.
    • (2004) J Biol Chem , vol.279 , pp. 44825-44833
    • Legube, G.1    Linares, L.K.2    Tyteca, S.3    Caron, C.4    Scheffner, M.5
  • 44
    • 0034682736 scopus 로고    scopus 로고
    • Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis
    • Ikura T, Ogryzko VV, Grigoriev M, Groisman R, Wang J, et al. (2000) Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell 102: 463-473.
    • (2000) Cell , vol.102 , pp. 463-473
    • Ikura, T.1    Ogryzko, V.V.2    Grigoriev, M.3    Groisman, R.4    Wang, J.5
  • 45
    • 79958068204 scopus 로고    scopus 로고
    • Phosphorylation of Tip60 by GSK-3 determines the induction of PUMA and apoptosis by p53
    • Charvet C, Wissler M, Brauns-Schubert P, Wang SJ, Tang Y, et al. (2011) Phosphorylation of Tip60 by GSK-3 determines the induction of PUMA and apoptosis by p53. Molecular Cell 42: 584-596.
    • (2011) Molecular Cell , vol.42 , pp. 584-596
    • Charvet, C.1    Wissler, M.2    Brauns-Schubert, P.3    Wang, S.J.4    Tang, Y.5
  • 46
    • 35148894396 scopus 로고    scopus 로고
    • DNA damage-dependent acetylation and ubiquitination of H2AX enhances chromatin dynamics
    • Ikura T, Tashiro S, Kakino A, Shima H, Jacob N, et al. (2007) DNA damage-dependent acetylation and ubiquitination of H2AX enhances chromatin dynamics. Mol Cell Biol 27: 7028-7040.
    • (2007) Mol Cell Biol , vol.27 , pp. 7028-7040
    • Ikura, T.1    Tashiro, S.2    Kakino, A.3    Shima, H.4    Jacob, N.5
  • 47
    • 10844233155 scopus 로고    scopus 로고
    • Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions
    • Kusch T, Florens L, Macdonald WH, Swanson SK, Glaser RL, et al. (2004) Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions. Science 306: 2084-2087.
    • (2004) Science , vol.306 , pp. 2084-2087
    • Kusch, T.1    Florens, L.2    Macdonald, W.H.3    Swanson, S.K.4    Glaser, R.L.5
  • 48
    • 33747882071 scopus 로고    scopus 로고
    • Tip60 in DNA damage response and growth control: many tricks in one HAT
    • Squatrito M, Gorrini C, Amati B, (2006) Tip60 in DNA damage response and growth control: many tricks in one HAT. Trends Cell Biol 16: 433-442.
    • (2006) Trends Cell Biol , vol.16 , pp. 433-442
    • Squatrito, M.1    Gorrini, C.2    Amati, B.3
  • 49
    • 1842583739 scopus 로고    scopus 로고
    • A new class of C. elegans synMuv genes implicates a Tip60/NuA4-like HAT complex as a negative regulator of Ras signaling
    • Ceol CJ, Horvitz HR, (2004) A new class of C. elegans synMuv genes implicates a Tip60/NuA4-like HAT complex as a negative regulator of Ras signaling. Dev Cell 6: 563-576.
    • (2004) Dev Cell , vol.6 , pp. 563-576
    • Ceol, C.J.1    Horvitz, H.R.2
  • 50
    • 3042533087 scopus 로고    scopus 로고
    • Putative involvement of the histone acetyltransferase Tip60 in ribosomal gene transcription
    • Halkidou K, Logan IR, Cook S, Neal DE, Robson CN, (2004) Putative involvement of the histone acetyltransferase Tip60 in ribosomal gene transcription. Nucleic Acids Res 32: 1654-1665.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1654-1665
    • Halkidou, K.1    Logan, I.R.2    Cook, S.3    Neal, D.E.4    Robson, C.N.5
  • 51
    • 77951217683 scopus 로고    scopus 로고
    • SIRT1 regulates autoacetylation and histone acetyltransferase activity of TIP60
    • Wang J, Chen J, (2010) SIRT1 regulates autoacetylation and histone acetyltransferase activity of TIP60. J Biol Chem 285: 11458-11464.
    • (2010) J Biol Chem , vol.285 , pp. 11458-11464
    • Wang, J.1    Chen, J.2
  • 52
    • 0042827840 scopus 로고    scopus 로고
    • The acetyltransferase 60 kDa trans-acting regulatory protein of HIV type 1-interacting protein (Tip60) interacts with the translocation E26 transforming-specific leukaemia gene (TEL) and functions as a transcriptional co-repressor
    • Nordentoft I, Jorgensen P, (2003) The acetyltransferase 60 kDa trans-acting regulatory protein of HIV type 1-interacting protein (Tip60) interacts with the translocation E26 transforming-specific leukaemia gene (TEL) and functions as a transcriptional co-repressor. Biochem J 374: 165-173.
    • (2003) Biochem J , vol.374 , pp. 165-173
    • Nordentoft, I.1    Jorgensen, P.2
  • 53
    • 0036830560 scopus 로고    scopus 로고
    • The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate
    • Yan Y, Harper S, Speicher DW, Marmorstein R, (2002) The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate. Nat Struct Biol 9: 862-869.
    • (2002) Nat Struct Biol , vol.9 , pp. 862-869
    • Yan, Y.1    Harper, S.2    Speicher, D.W.3    Marmorstein, R.4
  • 55
    • 79961209537 scopus 로고    scopus 로고
    • Regulation of the histone acetyltransferase activity of hMOF via autoacetylation of Lys274
    • Sun B, Guo S, Tang Q, Li C, Zeng R, et al. (2011) Regulation of the histone acetyltransferase activity of hMOF via autoacetylation of Lys274. Cell Res 21: 1262-1266.
    • (2011) Cell Res , vol.21 , pp. 1262-1266
    • Sun, B.1    Guo, S.2    Tang, Q.3    Li, C.4    Zeng, R.5
  • 56
    • 79551625231 scopus 로고    scopus 로고
    • Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1
    • Kadlec J, Hallacli E, Lipp M, Holz H, Sanchez-Weatherby J, et al. (2011) Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1. Nat Struct Mol Biol 18: 142-149.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 142-149
    • Kadlec, J.1    Hallacli, E.2    Lipp, M.3    Holz, H.4    Sanchez-Weatherby, J.5
  • 59
    • 33846026402 scopus 로고    scopus 로고
    • Kinetic and mass spectrometric analysis of p300 histone acetyltransferase domain autoacetylation
    • Karanam B, Jiang L, Wang L, Kelleher NL, Cole PA, (2006) Kinetic and mass spectrometric analysis of p300 histone acetyltransferase domain autoacetylation. J Biol Chem 281: 40292-40301.
    • (2006) J Biol Chem , vol.281 , pp. 40292-40301
    • Karanam, B.1    Jiang, L.2    Wang, L.3    Kelleher, N.L.4    Cole, P.A.5
  • 60
    • 53049105934 scopus 로고    scopus 로고
    • Structural insights into histone H3 lysine 56 acetylation by Rtt109
    • Lin C, Yuan YA, (2008) Structural insights into histone H3 lysine 56 acetylation by Rtt109. Structure 16: 1503-1510.
    • (2008) Structure , vol.16 , pp. 1503-1510
    • Lin, C.1    Yuan, Y.A.2
  • 61
    • 50449091106 scopus 로고    scopus 로고
    • Molecular basis for the autoregulation of the protein acetyl transferase Rtt109
    • Stavropoulos P, Nagy V, Blobel G, Hoelz A, (2008) Molecular basis for the autoregulation of the protein acetyl transferase Rtt109. Proc Natl Acad Sci U S A 105: 12236-12241.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 12236-12241
    • Stavropoulos, P.1    Nagy, V.2    Blobel, G.3    Hoelz, A.4
  • 62
    • 46449118856 scopus 로고    scopus 로고
    • Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP
    • Tang Y, Holbert MA, Wurtele H, Meeth K, Rocha W, et al. (2008) Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP. Nat Struct Mol Biol 15: 738-745.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 738-745
    • Tang, Y.1    Holbert, M.A.2    Wurtele, H.3    Meeth, K.4    Rocha, W.5
  • 63
    • 79960138904 scopus 로고    scopus 로고
    • Autoacetylation of the histone acetyltransferase Rtt109
    • Albaugh BN, Arnold KM, Lee S, Denu JM, (2011) Autoacetylation of the histone acetyltransferase Rtt109. J Biol Chem 286: 24694-24701.
    • (2011) J Biol Chem , vol.286 , pp. 24694-24701
    • Albaugh, B.N.1    Arnold, K.M.2    Lee, S.3    Denu, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.