메뉴 건너뛰기




Volumn 105, Issue 34, 2008, Pages 12236-12241

Molecular basis for the autoregulation of the protein acetyl transferase Rtt109

Author keywords

DNA repair; Histone; Structure

Indexed keywords

ACETYL COENZYME A; ACYLTRANSFERASE; HISTONE; HISTONE CHAPERONE VPS75; LYSINE; PROTEIN ACETYL TRANSFERASE RTT109; UNCLASSIFIED DRUG;

EID: 50449091106     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0805813105     Document Type: Article
Times cited : (52)

References (30)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger K, Mader AW, Richmond RK, Sargent DF, Richmond TJ (1997) Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 389:251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 2
    • 34250201427 scopus 로고    scopus 로고
    • Lysine-specific demethylase 1 as a potential therapeutic target
    • Stavropoulos P, Hoelz A (2007) Lysine-specific demethylase 1 as a potential therapeutic target. Exp Opin Ther Targets 11:809-820.
    • (2007) Exp Opin Ther Targets , vol.11 , pp. 809-820
    • Stavropoulos, P.1    Hoelz, A.2
  • 3
    • 33745862395 scopus 로고    scopus 로고
    • Crystal structure and mechanism of human lysine-specific demethylase-1
    • Stavropoulos P, Blobel G, Hoelz A (2006) Crystal structure and mechanism of human lysine-specific demethylase-1. Nat Struct Mol Biol 13:626-632.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 626-632
    • Stavropoulos, P.1    Blobel, G.2    Hoelz, A.3
  • 4
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD (2001) Translating the histone code. Science 293:1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 5
    • 18844413266 scopus 로고    scopus 로고
    • Acetylation in histone H3 globular domain regulates gene expression in yeast
    • Xu F, Zhang K, Grunstein M (2005) Acetylation in histone H3 globular domain regulates gene expression in yeast. Cell 121:375-385.
    • (2005) Cell , vol.121 , pp. 375-385
    • Xu, F.1    Zhang, K.2    Grunstein, M.3
  • 6
    • 22444448143 scopus 로고    scopus 로고
    • A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
    • Masumoto H, Hawke D, Kobayashi R, Verreault A (2005) A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature 436:294-298.
    • (2005) Nature , vol.436 , pp. 294-298
    • Masumoto, H.1    Hawke, D.2    Kobayashi, R.3    Verreault, A.4
  • 7
    • 22544441929 scopus 로고    scopus 로고
    • Characterization of lysine 56 of histone H3 as an acetylation site in Saccharomyces cerevisiae
    • Ozdemir A, et al. (2005) Characterization of lysine 56 of histone H3 as an acetylation site in Saccharomyces cerevisiae. J Biol Chem 280:25949-25952.
    • (2005) J Biol Chem , vol.280 , pp. 25949-25952
    • Ozdemir, A.1
  • 8
    • 27644467857 scopus 로고    scopus 로고
    • Insights into the role of histone H3 and histone H4 core modifiable residues in Saccharomyces cerevisiae
    • Hyland EM, et al. (2005) Insights into the role of histone H3 and histone H4 core modifiable residues in Saccharomyces cerevisiae. Mol Cell Biol 25:10060-10070.
    • (2005) Mol Cell Biol , vol.25 , pp. 10060-10070
    • Hyland, E.M.1
  • 9
    • 33644702025 scopus 로고    scopus 로고
    • Chromatin assembly factor 1 interacts with histone H3 methylated at lysine 79 in the processes of epigenetic silencing and DNA repair
    • Zhou H, Madden BJ, Muddiman DC, Zhang Z (2006) Chromatin assembly factor 1 interacts with histone H3 methylated at lysine 79 in the processes of epigenetic silencing and DNA repair. Biochemistry 45:2852-2861.
    • (2006) Biochemistry , vol.45 , pp. 2852-2861
    • Zhou, H.1    Madden, B.J.2    Muddiman, D.C.3    Zhang, Z.4
  • 10
    • 33646472914 scopus 로고    scopus 로고
    • Histone chaperone Asf1 is required for histone H3 lysine 56 acetylation, a modification associated with S phase in mitosis and meiosis
    • Recht J, et al. (2006) Histone chaperone Asf1 is required for histone H3 lysine 56 acetylation, a modification associated with S phase in mitosis and meiosis. Proc Natl Acad Sci USA 103:6988-6993.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 6988-6993
    • Recht, J.1
  • 11
    • 33846796258 scopus 로고    scopus 로고
    • Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication
    • Han J, et al. (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315:653-655.
    • (2007) Science , vol.315 , pp. 653-655
    • Han, J.1
  • 12
    • 33846818840 scopus 로고    scopus 로고
    • Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56
    • Driscoll R, Hudson A, Jackson (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315:649-652.
    • (2007) Science , vol.315 , pp. 649-652
    • Driscoll, R.1    Hudson, A.2    Jackson3
  • 13
    • 33847412826 scopus 로고    scopus 로고
    • Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes
    • Tsubota T, et al. (2007) Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes. Mol Cell 25:703-712.
    • (2007) Mol Cell , vol.25 , pp. 703-712
    • Tsubota, T.1
  • 14
    • 0035692614 scopus 로고    scopus 로고
    • Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance
    • Scholes DT, Banerjee M, Bowen B, Curcio MJ (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159:1449-1465.
    • (2001) Genetics , vol.159 , pp. 1449-1465
    • Scholes, D.T.1    Banerjee, M.2    Bowen, B.3    Curcio, M.J.4
  • 15
    • 33846023720 scopus 로고    scopus 로고
    • Rtt109 is required for proper H3K56 acetylation: A chromatin mark associated with the elongating RNA polymerase II
    • Schneider J, Bajwa P, Johnson FC, Bhaumik SR, Shilatifard A (2006) Rtt109 is required for proper H3K56 acetylation: A chromatin mark associated with the elongating RNA polymerase II. J Biol Chem 281:37270-37274.
    • (2006) J Biol Chem , vol.281 , pp. 37270-37274
    • Schneider, J.1    Bajwa, P.2    Johnson, F.C.3    Bhaumik, S.R.4    Shilatifard, A.5
  • 16
    • 35348970835 scopus 로고    scopus 로고
    • Acetylation of lysine 56 of histone H3 catalyzed by RTT109 and regulated by ASF1 is required for replisome integrity
    • Han J, Zhou H, Li Z, Xu RM, Zhang Z (2007) Acetylation of lysine 56 of histone H3 catalyzed by RTT109 and regulated by ASF1 is required for replisome integrity. J Biol Chem 282:28587-28596.
    • (2007) J Biol Chem , vol.282 , pp. 28587-28596
    • Han, J.1    Zhou, H.2    Li, Z.3    Xu, R.M.4    Zhang, Z.5
  • 17
    • 34347258162 scopus 로고    scopus 로고
    • The Rtt109-Vps75 histone acetyltransferase complex acetylates non-nucleosomal histone H3
    • Han J, Zhou H, Li Z, Xu RM, Zhang Z (2007) The Rtt109-Vps75 histone acetyltransferase complex acetylates non-nucleosomal histone H3. J Biol Chem 282:14158-14164.
    • (2007) J Biol Chem , vol.282 , pp. 14158-14164
    • Han, J.1    Zhou, H.2    Li, Z.3    Xu, R.M.4    Zhang, Z.5
  • 18
    • 34447508456 scopus 로고    scopus 로고
    • Regulation of histone H3 lysine 56 acetylation in Schizosaccharomyces pombe
    • Xhemalce B, et al. (2007) Regulation of histone H3 lysine 56 acetylation in Schizosaccharomyces pombe. J Biol Chem 282:15040-15047.
    • (2007) J Biol Chem , vol.282 , pp. 15040-15047
    • Xhemalce, B.1
  • 19
    • 0033529845 scopus 로고    scopus 로고
    • Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator
    • Trievel RC, et al. (1999) Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc Natl Acad Sci USA 96:8931-8936.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8931-8936
    • Trievel, R.C.1
  • 20
    • 0033635283 scopus 로고    scopus 로고
    • Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases
    • Yan Y, Barlev NA, Haley RH, Berger SL, Marmorstein R (2000) Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases. Mol Cell 6:1195-1205.
    • (2000) Mol Cell , vol.6 , pp. 1195-1205
    • Yan, Y.1    Barlev, N.A.2    Haley, R.H.3    Berger, S.L.4    Marmorstein, R.5
  • 21
    • 39149109887 scopus 로고    scopus 로고
    • The structural basis of protein acetylation by the p300/CBP transcriptional coactivator
    • Liu X, et al. (2008) The structural basis of protein acetylation by the p300/CBP transcriptional coactivator. Nature 451:846-850.
    • (2008) Nature , vol.451 , pp. 846-850
    • Liu, X.1
  • 22
    • 34547911052 scopus 로고    scopus 로고
    • Chemistry of acetyl transfer by histone modifying enzymes: Structure, mechanism and implications for effector design
    • Hodawadekar SC, Marmorstein R (2007) Chemistry of acetyl transfer by histone modifying enzymes: Structure, mechanism and implications for effector design. Oncogene 26:5528-5540.
    • (2007) Oncogene , vol.26 , pp. 5528-5540
    • Hodawadekar, S.C.1    Marmorstein, R.2
  • 23
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases; controlling activity through activation segment conformation
    • Nolen B, Taylor S, Ghosh G (2004) Regulation of protein kinases; controlling activity through activation segment conformation. Mol Cell 15:661-675.
    • (2004) Mol Cell , vol.15 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 24
    • 33751539464 scopus 로고    scopus 로고
    • Protein-protein interactions in the allosteric regulation of protein kinases
    • Pellicena P, Kuriyan J (2006) Protein-protein interactions in the allosteric regulation of protein kinases. Curr Opin Struct Biol 16:702-709.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 702-709
    • Pellicena, P.1    Kuriyan, J.2
  • 25
    • 34250309212 scopus 로고    scopus 로고
    • Vps75, a new yeast member of the NAP histone chaperone family
    • Selth L, Svejstrup JQ (2007) Vps75, a new yeast member of the NAP histone chaperone family. J Biol Chem 282:12358-12362.
    • (2007) J Biol Chem , vol.282 , pp. 12358-12362
    • Selth, L.1    Svejstrup, J.Q.2
  • 27
    • 0001006942 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods
    • La Fortelle ED, Bricogne G (1997) Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods. Methods Enzymol 276:476-494.
    • (1997) Methods Enzymol , vol.276 , pp. 476-494
    • La Fortelle, E.D.1    Bricogne, G.2
  • 28
    • 0028103275 scopus 로고    scopus 로고
    • CCP4 (1994) Collaborative Computational Project, Number 4, The CCP4 Suite: Programs for Protein Crystallography. Acta Crystallogr D 50:760-763.
    • CCP4 (1994) Collaborative Computational Project, Number 4, The CCP4 Suite: Programs for Protein Crystallography. Acta Crystallogr D 50:760-763.
  • 29
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 30
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger AT, et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D 54:905-921.
    • (1998) Acta Crystallogr D , vol.54 , pp. 905-921
    • Brünger, A.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.