메뉴 건너뛰기




Volumn 30, Issue 13, 2011, Pages 2610-2621

A dual role of H4K16 acetylation in the establishment of yeast silent chromatin

Author keywords

H4K16; histone deacetylation; methylation; silent chromatin; SIR complex

Indexed keywords

HISTONE H3; HISTONE H4; LYSINE; SILENT INFORMATION REGULATOR PROTEIN;

EID: 79960072799     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2011.170     Document Type: Article
Times cited : (76)

References (84)
  • 1
    • 37349107849 scopus 로고    scopus 로고
    • Interplay of Chromatin Modifiers on a Short Basic Patch of Histone H4 Tail Defines the Boundary of Telomeric Heterochromatin
    • DOI 10.1016/j.molcel.2007.12.002, PII S1097276507008271
    • Altaf M, Utley RT, Lacoste N, Tan S, Briggs SD, Cote J (2007) Interplay of chromatin modifiers on a short basic patch of histone H4 tail defines the boundary of telomeric heterochromatin. Mol Cell 28: 1002-1014 (Pubitemid 350297030)
    • (2007) Molecular Cell , vol.28 , Issue.6 , pp. 1002-1014
    • Altaf, M.1    Utley, R.T.2    Lacoste, N.3    Tan, S.4    Briggs, S.D.5    Cote, J.6
  • 2
    • 0025900189 scopus 로고
    • Modifiers of position effect are shared between telomeric and silent mating-type loci in S. cerevisiae
    • Aparicio OM, Billington BL, Gottschling DE (1991) Modifiers of position effect are shared between telomeric and silent mating-type loci in S. cerevisiae. Cell 66: 1279-1287 (Pubitemid 121001416)
    • (1991) Cell , vol.66 , Issue.6 , pp. 1279-1287
    • Aparicio, O.M.1    Billington, B.L.2    Gottschling, D.E.3
  • 3
    • 0036229718 scopus 로고    scopus 로고
    • Mutations in Saccharomyces cerevisiae gene SIR2 can have differential effects on in vivo silencing phenotypes and in vitro histone deacetylation activity
    • DOI 10.1091/mbc.01-10-0482
    • Armstrong CM, Kaeberlein M, Imai SI, Guarente L (2002) Mutations in Saccharomyces cerevisiae gene SIR2 can have differential effects on in vivo silencing phenotypes and in vitro histone deacetylation activity. Mol Biol Cell 13: 1427-1438 (Pubitemid 34309634)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.4 , pp. 1427-1438
    • Armstrong, C.M.1    Kaeberlein, M.2    Ichiro Imai, S.3    Guarente, L.4
  • 4
    • 3343024449 scopus 로고    scopus 로고
    • +-dependent histone/protein deacetylases
    • DOI 10.1021/bi049592e
    • Borra MT, Langer MR, Slama JT, Denu JM (2004) Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-depen-dent histone/protein deacetylases. Biochemistry 43: 9877-9887 (Pubitemid 38993837)
    • (2004) Biochemistry , vol.43 , Issue.30 , pp. 9877-9887
    • Borra, M.T.1    Langer, M.R.2    Slama, J.T.3    Denu, J.M.4
  • 6
    • 0037085264 scopus 로고    scopus 로고
    • Acetylation of the yeast histone H4 N terminus regulates its binding to heterochromatin protein SIR3
    • DOI 10.1074/jbc.M110532200
    • Carmen AA, Milne L, Grunstein M (2002) Acetylation of the yeast histone H4 N terminus regulates its binding to heterochromatin protein SIR3. J Biol Chem 277: 4778-4781 (Pubitemid 34968510)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.7 , pp. 4778-4781
    • Carmen, A.A.1    Milne, L.2    Grunstein, M.3
  • 7
    • 33745520486 scopus 로고    scopus 로고
    • The sirtuins hst3 and Hst4p preserve genome integrity by controlling histone h3 lysine 56 deacetylation
    • DOI 10.1016/j.cub.2006.06.023, PII S0960982206017490
    • Celic I, Masumoto H, Griffith WP, Meluh P, Cotter RJ, Boeke JD, Verreault A (2006) The sirtuins hst3 and Hst4p preserve genome integrity by controlling histone h3 lysine 56 deacetylation. Curr Biol 16: 1280-1289 (Pubitemid 43977885)
    • (2006) Current Biology , vol.16 , Issue.13 , pp. 1280-1289
    • Celic, I.1    Masumoto, H.2    Griffith, W.P.3    Meluh, P.4    Cotter, R.J.5    Boeke, J.D.6    Verreault, A.7
  • 8
    • 70350150387 scopus 로고    scopus 로고
    • Collaboration between the essential Esa1 acetyltransferase and the Rpd3 deacetylase is mediated by H4K12 histone acetylation in Saccharomyces cerevisiae
    • Chang CS, Pillus L (2009) Collaboration between the essential Esa1 acetyltransferase and the Rpd3 deacetylase is mediated by H4K12 histone acetylation in Saccharomyces cerevisiae. Genetics 183: 149-160
    • (2009) Genetics , vol.183 , pp. 149-160
    • Chang, C.S.1    Pillus, L.2
  • 9
    • 11844303478 scopus 로고    scopus 로고
    • Mechanism of transcriptional silencing in yeast
    • DOI 10.1016/j.cell.2004.11.030, PII S0092867404010980
    • Chen L, Widom J (2005) Mechanism of transcriptional silencing in yeast. Cell 120: 37-48 (Pubitemid 40094601)
    • (2005) Cell , vol.120 , Issue.1 , pp. 37-48
    • Chen, L.1    Widom, J.2
  • 10
    • 50249084505 scopus 로고    scopus 로고
    • Bypassing Sir2 and O-acetyl-ADP-ribose in transcriptional silencing
    • Chou CC, Li YC, Gartenberg MR (2008) Bypassing Sir2 and O-acetyl-ADP-ribose in transcriptional silencing. Mol Cell 31: 650-659
    • (2008) Mol Cell , vol.31 , pp. 650-659
    • Chou, C.C.1    Li, Y.C.2    Gartenberg, M.R.3
  • 11
    • 33644864706 scopus 로고    scopus 로고
    • A homotrimer-heterotrimer switch in Sir2 structure differentiates rDNA and telomeric silencing
    • DOI 10.1016/j.molcel.2006.02.006, PII S1097276506000864
    • Cubizolles F, Martino F, Perrod S, Gasser SM (2006) A homotrimer-heterotrimer switch in Sir2 structure differentiates rDNA and telomeric silencing. Mol Cell 21 : 825-836 (Pubitemid 43376132)
    • (2006) Molecular Cell , vol.21 , Issue.6 , pp. 825-836
    • Cubizolles, F.1    Martino, F.2    Perrod, S.3    Gasser, S.M.4
  • 12
    • 0036307707 scopus 로고    scopus 로고
    • Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 Å resolution
    • DOI 10.1016/S0022-2836(02)00386-8
    • Davey CA, Sargent DF, Luger K, Maeder AW, Richmond TJ (2002) Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 a resolution. J Mol Biol 319: 1097-1113 (Pubitemid 34729421)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.5 , pp. 1097-1113
    • Davey, C.A.1    Sargent, D.F.2    Luger, K.3    Maeder, A.W.4    Richmond, T.J.5
  • 13
    • 34249080596 scopus 로고    scopus 로고
    • Theoretical analysis of epigenetic cell memory by nucleosome modification
    • DOI 10.1016/j.cell.2007.02.053, PII S0092867407004588
    • Dodd IB, Micheelsen MA, Sneppen K, Thon G (2007) Theoretical analysis of epigenetic cell memory by nucleosome modification. Cell 129: 813-822 (Pubitemid 46802381)
    • (2007) Cell , vol.129 , Issue.4 , pp. 813-822
    • Dodd, I.B.1    Micheelsen, M.A.2    Sneppen, K.3    Thon, G.4
  • 14
    • 0030939235 scopus 로고    scopus 로고
    • The role of Sas2, an acetyltransferase homologue of Saccharomyces cerevisiae, in silencing and ORC function
    • Ehrenhofer-Murray AE, Rivier DH, Rine J (1997) The role of Sas2, an acetyltransferase homologue of Saccharomyces cerevisiae, in silencing and ORC function. Genetics 145: 923-934 (Pubitemid 27149100)
    • (1997) Genetics , vol.145 , Issue.4 , pp. 923-934
    • Ehrenhofer-Murray, A.E.1    Rivier, D.H.2    Rine, J.3
  • 16
    • 44949188488 scopus 로고    scopus 로고
    • Sir2 silences gene transcription by targeting the transition between RNA polymerase II initiation and elongation
    • DOI 10.1128/MCB.00019-08
    • Gao L, Gross DS (2008) Sir2 silences gene transcription by targeting the transition between RNA polymerase II initiation and elongation. Mol Cell Biol 28: 3979-3994 (Pubitemid 351812984)
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.12 , pp. 3979-3994
    • Gao, L.1    Gross, D.S.2
  • 17
    • 0035861202 scopus 로고    scopus 로고
    • The molecular biology of the SIR proteins
    • DOI 10.1016/S0378-1119(01)00741-7, PII S0378111901007417
    • Gasser SM, Cockell MM (2001) The molecular biology of the SIR proteins. Gene 279: 1-16 (Pubitemid 33145178)
    • (2001) Gene , vol.279 , Issue.1 , pp. 1-16
    • Gasser, S.M.1    Cockell, M.M.2
  • 18
    • 0035881504 scopus 로고    scopus 로고
    • Sir2p exists in two nucleosome-binding complexes with distinct deacetylase activities
    • DOI 10.1093/emboj/20.16.4522
    • Ghidelli S, Donze D, Dhillon N, Kamakaka RT (2001) Sir2p exists in two nucleosome-binding complexes with distinct deacetylase activities. EMBO J 20: 4522-4535 (Pubitemid 32772046)
    • (2001) EMBO Journal , vol.20 , Issue.16 , pp. 4522-4535
    • Ghidelli, S.1    Donze, D.2    Dhillon, N.3    Kamakaka, R.T.4
  • 19
    • 0026552380 scopus 로고
    • Telomere-proximal DNA in Saccharomyces cerevisiae is refractory to methyltransferase activity in vivo
    • Gottschling DE (1992) Telomere-proximal DNA in Saccharomyces cerevisiae is refractory to methyltransferase activity in vivo. Proc Natl Acad Sci USA 89: 4062-4065
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4062-4065
    • Gottschling, D.E.1
  • 20
    • 33846796258 scopus 로고    scopus 로고
    • Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication
    • DOI 10.1126/science.1133234
    • Han J, Zhou H, Horazdovsky B, Zhang K, Xu RM, Zhang Z (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315: 653-655 (Pubitemid 46214710)
    • (2007) Science , vol.315 , Issue.5812 , pp. 653-655
    • Han, J.1    Zhou, H.2    Horazdovsky, B.3    Zhang, K.4    Xu, R.-M.5    Zhang, Z.6
  • 21
    • 0028919756 scopus 로고
    • Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: A molecular model for the formation of heterochromatin in yeast
    • Hecht A, Laroche T, Strahl-Bolsinger S, Gasser SM, Grunstein M (1995) Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: a molecular model for the formation of heterochromatin in yeast. Cell 80: 583-592
    • (1995) Cell , vol.80 , pp. 583-592
    • Hecht, A.1    Laroche, T.2    Strahl-Bolsinger, S.3    Gasser, S.M.4    Grunstein, M.5
  • 22
    • 78650609911 scopus 로고    scopus 로고
    • Transcriptional silencing functions of the yeast protein Orc1/Sir3 subfunctionalized after gene duplication
    • Hickman MA, Rusche LN (2010) Transcriptional silencing functions of the yeast protein Orc1/Sir3 subfunctionalized after gene duplication. Proc Natl Acad Sci USA 107 : 19384-19389
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 19384-19389
    • Hickman, M.A.1    Rusche, L.N.2
  • 23
    • 0036261650 scopus 로고    scopus 로고
    • Steps in assembly of silent chromatin in yeast: Sir3-independent binding of a Sir2/Sir4 complex to silencers and role for Sir2-dependent deacetylation
    • DOI 10.1128/MCB.22.12.4167-4180.2002
    • Hoppe GJ, Tanny JC, Rudner AD, Gerber SA, Danaie S, Gygi SP, Moazed D (2002) Steps in assembly of silent chromatin in yeast: Sir3-independent binding of a Sir2/Sir4 complex to silencers and role for Sir2-dependent deacetylation. Mol Cell Biol 22: 4167-4180 (Pubitemid 34556587)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.12 , pp. 4167-4180
    • Hoppe, G.J.1    Tanny, J.C.2    Rudner, A.D.3    Gerber, S.A.4    Danaie, S.5    Gygi, S.P.6    Moazed, D.7
  • 24
    • 11844299709 scopus 로고    scopus 로고
    • A method for the in vitro reconstitution of a defined "30 nm" chromatin fibre containing stoichiometric amounts of the linker histone
    • DOI 10.1016/j.jmb.2004.10.075, PII S0022283604013968
    • Huynh VA, Robinson PJ, Rhodes D (2005) A method for the in vitro reconstitution of a defined '30 nm' chromatin fibre containing stoichiometric amounts of the linker histone. J Mol Biol 345: 957-968 (Pubitemid 40092217)
    • (2005) Journal of Molecular Biology , vol.345 , Issue.5 , pp. 957-968
    • Huynh, V.A.T.1    Robinson, P.J.J.2    Rhodes, D.3
  • 25
    • 27644467857 scopus 로고    scopus 로고
    • Insights into the role of histone H3 and histone H4 core modifiable residues in Saccharomyces cerevisiae
    • DOI 10.1128/MCB.25.22.10060-10070.2005
    • Hyland EM, Cosgrove MS, Molina H, Wang D, Pandey A, Cottee RJ, Boeke JD (2005) Insights into the role of histone H3 and histone H4 core modifiable residues in Saccharomyces cerevisiae. Mol Cell Biol 25: 10060-10070 (Pubitemid 41572751)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.22 , pp. 10060-10070
    • Hyland, E.M.1    Cosgrove, M.S.2    Molina, H.3    Wang, D.4    Pandey, A.5    Cottee, R.J.6    Boeke, J.D.7
  • 26
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • DOI 10.1038/35001622
    • Imai S, Armstrong CM, Kaeberlein M, Guarente L (2000) Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403: 795-800 (Pubitemid 30111843)
    • (2000) Nature , vol.403 , Issue.6771 , pp. 795-800
    • Imai, S.-I.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 28
    • 0026556122 scopus 로고
    • Identification of a non-basic domain in the histone H4 N-terminus required for repression of the yeast silent mating loci
    • Johnson LM, Fisher-Adams G, Grunstein M (1992) Identification of a non-basic domain in the histone H4 N-terminus required for repression of the yeast silent mating loci. EMBO J 11 : 2201-2209
    • (1992) EMBO J , vol.11 , pp. 2201-2209
    • Johnson, L.M.1    Fisher-Adams, G.2    Grunstein, M.3
  • 29
    • 0025002966 scopus 로고
    • Genetic evidence for an interaction between SIR3 and histone H4 in the repression of the silent mating loci in Saccharomyces cerevisiae
    • Johnson LM, Kayne PS, Kahn ES, Grunstein M (1990) Genetic evidence for an interaction between SIR3 and histone H4 in the repression of the silent mating loci in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 87: 6286-6290
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6286-6290
    • Johnson, L.M.1    Kayne, P.S.2    Kahn, E.S.3    Grunstein, M.4
  • 30
    • 21844454183 scopus 로고    scopus 로고
    • Heterochromatin formation involves changes in histone modifications over multiple cell generations
    • DOI 10.1038/sj.emboj.7600692
    • Katan-Khaykovich Y, Struhl K (2005) Heterochromatin formation involves changes in histone modifications over multiple cell generations. EMBO J 24: 2138-2149 (Pubitemid 40961798)
    • (2005) EMBO Journal , vol.24 , Issue.12 , pp. 2138-2149
    • Katan-Khaykovich, Y.1    Struhl, K.2
  • 31
    • 0036843170 scopus 로고    scopus 로고
    • Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing
    • DOI 10.1038/ng993
    • Kimura A, Umehara T, Horikoshi M (2002) Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing. Nat Genet 32: 370-377 (Pubitemid 35266110)
    • (2002) Nature Genetics , vol.32 , Issue.3 , pp. 370-377
    • Kimura, A.1    Umehara, T.2    Horikoshi, M.3
  • 32
    • 39549115045 scopus 로고    scopus 로고
    • Assembly of nucleosomal templates by salt dialysis
    • Chapter 21: Unit 21.6
    • Lee KM, Narlikar G (2001) Assembly of nucleosomal templates by salt dialysis. Curr Protoc Mol Biol Chapter 21: Unit 21.6
    • (2001) Curr Protoc Mol Biol
    • Lee, K.M.1    Narlikar, G.2
  • 33
    • 47549092547 scopus 로고    scopus 로고
    • Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly
    • DOI 10.1016/j.cell.2008.06.018, PII S0092867408007708
    • Li Q, Zhou H, Wurtele H, Davies B, Horazdovsky B, Verreault A, Zhang Z (2008) Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly. Cell 134: 244-255 (Pubitemid 352010333)
    • (2008) Cell , vol.134 , Issue.2 , pp. 244-255
    • Li, Q.1    Zhou, H.2    Wurtele, H.3    Davies, B.4    Horazdovsky, B.5    Verreault, A.6    Zhang, Z.7
  • 34
    • 19344377042 scopus 로고    scopus 로고
    • Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation
    • DOI 10.1016/j.cell.2005.03.035, PII S0092867405003545
    • Liou GG, Tanny JC, Kruger RG, Walz T, Moazed D (2005) Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation. Cell 121: 515-527 (Pubitemid 40720006)
    • (2005) Cell , vol.121 , Issue.4 , pp. 515-527
    • Liou, G.-G.1    Tanny, J.C.2    Kruger, R.G.3    Walz, T.4    Moazed, D.5
  • 35
    • 0028304836 scopus 로고
    • Silencers and domains of generalized repression
    • Loo S, Rine J (1994) Silencers and domains of generalized repression. Science 264: 1768-1771 (Pubitemid 24227759)
    • (1994) Science , vol.264 , Issue.5166 , pp. 1768-1771
    • Loo, S.1    Rine, J.2
  • 36
    • 0032512794 scopus 로고    scopus 로고
    • New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning
    • DOI 10.1006/jmbi.1997.1494
    • Lowary PT, Widom J (1998) New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleo-some positioning. J Mol Biol 276: 19-42 (Pubitemid 28085408)
    • (1998) Journal of Molecular Biology , vol.276 , Issue.1 , pp. 19-42
    • Lowary, P.T.1    Widom, J.2
  • 37
  • 38
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • DOI 10.1038/38444
    • Luger K, Mader AW, Richmond RK, Sargent DF, Richmond TJ (1997) Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 389: 251-260 (Pubitemid 27406632)
    • (1997) Nature , vol.389 , Issue.6648 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 39
    • 58149457091 scopus 로고    scopus 로고
    • A silencer promotes the assembly of silenced chromatin independently of recruitment
    • Lynch PJ, Rusche LN (2009) A silencer promotes the assembly of silenced chromatin independently of recruitment. Mol Cell Biol 29: 43-56
    • (2009) Mol Cell Biol , vol.29 , pp. 43-56
    • Lynch, P.J.1    Rusche, L.N.2
  • 40
    • 33745496607 scopus 로고    scopus 로고
    • Cell cycle and checkpoint regulation of histone H3 K56 acetylation by Hst3 and Hst4
    • DOI 10.1016/j.molcel.2006.06.006, PII S1097276506004114
    • Maas NL, Miller KM, DeFazio LG, Toczyski DP (2006) Cell cycle and checkpoint regulation of histone H3 K56 acetylation by Hst3 and Hst4. Mol Cell 23: 109-119 (Pubitemid 43963450)
    • (2006) Molecular Cell , vol.23 , Issue.1 , pp. 109-119
    • Maas, N.L.1    Miller, K.M.2    DeFazio, L.G.3    Toczyski, D.P.4
  • 42
    • 22444448143 scopus 로고    scopus 로고
    • A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
    • DOI 10.1038/nature03714
    • 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 (Pubitemid 41021284)
    • (2005) Nature , vol.436 , Issue.7048 , pp. 294-298
    • Masumoto, H.1    Hawke, D.2    Kobayashi, R.3    Verreault, A.4
  • 43
    • 0025093599 scopus 로고
    • Genetic analysis of histone H4: Essential role of lysines subject to reversible acetylation
    • Megee PC, Morgan BA, Mittman BA, Smith MM (1990) Genetic analysis of histone H4: essential role of lysines subject to reversible acetylation. Science 247: 841-845
    • (1990) Science , vol.247 , pp. 841-845
    • Megee, P.C.1    Morgan, B.A.2    Mittman, B.A.3    Smith, M.M.4
  • 44
    • 0035577669 scopus 로고    scopus 로고
    • The silencing complex SAS-I links histone acetylation to the assembly of repressed chromatin by CAF-I and Asf1 in Saccharomyces cerevisiae
    • DOI 10.1101/gad.929001
    • Meijsing SH, Ehrenhofer-Murray AE (2001) The silencing complex SAS-I links histone acetylation to the assembly of repressed chromatin by CAF-I and Asf1 in Saccharomyces cerevisiae. Genes Dev 15: 3169-3182 (Pubitemid 33115680)
    • (2001) Genes and Development , vol.15 , Issue.23 , pp. 3169-3182
    • Meijsing, S.H.1    Ehrenhofer-Murray, A.E.2
  • 46
    • 23044489367 scopus 로고    scopus 로고
    • Acetylation of yeast histone H4 lysine 16: A switch for protein interactions in heterochromatin and euchromatin
    • DOI 10.1101/sqb.2004.69.193
    • Millar CB, Kurdistani SK, Grunstein M (2004) Acetylation of yeast histone H4 lysine 16: a switch for protein interactions in hetero-chromatin and euchromatin. Cold Spring Harb Symp Quant Biol 69: 193-200 (Pubitemid 41056554)
    • (2004) Cold Spring Harbor Symposia on Quantitative Biology , vol.69 , pp. 193-200
    • Millar, C.B.1    Kurdistani, S.K.2    Grunstein, M.3
  • 47
    • 0030951007 scopus 로고    scopus 로고
    • Silent information regulator protein complexes in Saccharomyces cerevisiae: A SIR2/SIR4 complex and evidence for a regulatory domain in SIR4 that inhibits its interaction with SIR3
    • DOI 10.1073/pnas.94.6.2186
    • Moazed D, Kistler A, Axelrod A, Rine J, Johnson AD (1997) Silent information regulator protein complexes in Saccharomyces cere-visiae: a SIR2/SIR4 complex and evidence for a regulatory domain in SIR4 that inhibits its interaction with SIR3. Proc Natl Acad Sci USA 94: 2186-2191 (Pubitemid 27136849)
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , Issue.6 , pp. 2186-2191
    • Moazed, D.1    Kistler, A.2    Axelrod, A.3    Rine, J.4    Johnson, A.D.5
  • 48
    • 77957264732 scopus 로고    scopus 로고
    • Locus dependence in epigenetic chromatin silencing
    • Mukhopadhyay S, Nagaraj VH, Sengupta AM (2010) Locus dependence in epigenetic chromatin silencing. Biosystems 102: 49-54
    • (2010) Biosystems , vol.102 , pp. 49-54
    • Mukhopadhyay, S.1    Nagaraj, V.H.2    Sengupta, A.M.3
  • 50
    • 40949099577 scopus 로고    scopus 로고
    • ε-acetyllysine in recombinant proteins
    • DOI 10.1038/nchembio.73, PII NCHEMBIO73
    • Neumann H, Peak-Chew SY, Chin JW (2008) Genetically encoding N(epsilon)-acetyllysine in recombinant proteins. Nat Chem Biol 4: 232-234 (Pubitemid 351414829)
    • (2008) Nature Chemical Biology , vol.4 , Issue.4 , pp. 232-234
    • Neumann, H.1    Peak-Chew, S.Y.2    Chin, J.W.3
  • 52
    • 0037098044 scopus 로고    scopus 로고
    • Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association
    • DOI 10.1101/gad.1001502
    • Ng HH, Feng Q, Wang H, Erdjument-Bromage H, Tempst P, Zhang Y, Struhl K (2002) Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association. Genes Dev 16: 1518-1527 (Pubitemid 34686333)
    • (2002) Genes and Development , vol.16 , Issue.12 , pp. 1518-1527
    • Ng, H.H.1    Feng, Q.2    Wang, H.3    Erdjument-Bromage, H.4    Tempst, P.5    Zhang, Y.6    Struhl, K.7
  • 53
    • 58149165025 scopus 로고    scopus 로고
    • Compensatory interactions between Sir3p and the nucleosomal LRS surface imply their direct interaction
    • Norris A, Bianchet MA, Boeke JD (2008) Compensatory interactions between Sir3p and the nucleosomal LRS surface imply their direct interaction. PLoS Genet 4: e1000301
    • (2008) PLoS Genet , vol.4
    • Norris, A.1    Bianchet, M.A.2    Boeke, J.D.3
  • 54
    • 37349033583 scopus 로고    scopus 로고
    • Role of the conserved Sir3-BAH domain in nucleosome binding and silent chromatin assembly
    • DOI 10.1016/j.molcel.2007.12.004, PII S1097276507008416
    • Onishi M, Liou GG, Buchberger JR, Walz T, Moazed D (2007) Role of the conserved Sir3-BAH domain in nucleosome binding and silent chromatin assembly. Mol Cell 28: 1015-1028 (Pubitemid 350297032)
    • (2007) Molecular Cell , vol.28 , Issue.6 , pp. 1015-1028
    • Onishi, M.1    Liou, G.-G.2    Buchberger, J.R.3    Walz, T.4    Moazed, D.5
  • 55
    • 67649846287 scopus 로고    scopus 로고
    • The establishment of gene silencing at single-cell resolution
    • Osborne EA, Dudoit S, Rine J (2009) The establishment of gene silencing at single-cell resolution. Nat Genet 41 : 800-806
    • (2009) Nat Genet , vol.41 , pp. 800-806
    • Osborne, E.A.1    Dudoit, S.2    Rine, J.3
  • 56
    • 0025110835 scopus 로고
    • Point mutations in the yeast histone H4 gene prevent silencing of the silent mating type locus HML
    • Park EC, Szostak JW (1990) Point mutations in the yeast histone H4 gene prevent silencing of the silent mating type locus HML. Mol Cell Biol 10 : 4932-4934
    • (1990) Mol Cell Biol , vol.10 , pp. 4932-4934
    • Park, E.C.1    Szostak, J.W.2
  • 57
    • 0024424452 scopus 로고
    • Epigenetic inheritance of transcriptional states in S. cerevisiae
    • DOI 10.1016/0092-8674(89)90009-3
    • Pillus L, Rine J (1989) Pigenetic inheritance of transcriptional states in S. cerevisiae. Cell 59: 637-647 (Pubitemid 19282870)
    • (1989) Cell , vol.59 , Issue.4 , pp. 637-647
    • Pillus, L.1    Rine, J.2
  • 58
    • 0029741343 scopus 로고    scopus 로고
    • Yeast SAS silencing genes and human genes associated with AML and HIV-1 Tat interactions are homologous with acetyltransferases
    • Reifsnyder C, Lowell J, Clarke A, Pillus L (1996) Yeast SAS silencing genes and human genes associated with AML and HIV-1 Tat interactions are homologous with acetyltransferases. Nat Genet 14: 42-49
    • (1996) Nat Genet , vol.14 , pp. 42-49
    • Reifsnyder, C.1    Lowell, J.2    Clarke, A.3    Pillus, L.4
  • 59
    • 0023340731 scopus 로고
    • Four genes responsible for a position effect on expression from HML and HMR in Saccharomyces cerevisiae
    • Rine J, Herskowitz I (1987) Four genes responsible for a position effect on expression from HML and HMR in Saccharomyces cerevisiae. Genetics 116: 9-22
    • (1987) Genetics , vol.116 , pp. 9-22
    • Rine, J.1    Herskowitz, I.2
  • 60
    • 48449106172 scopus 로고    scopus 로고
    • 30nm chromatin fibre decompaction requires both H4-K16 acetylation and linker histone eviction
    • Robinson PJ, An W, Routh A, Martino F, Chapman L, Roeder RG, Rhodes D (2008) 30nm chromatin fibre decompaction requires both H4-K16 acetylation and linker histone eviction. J Mol Biol 381: 816-825
    • (2008) J Mol Biol , vol.381 , pp. 816-825
    • Robinson, P.J.1    An, W.2    Routh, A.3    Martino, F.4    Chapman, L.5    Roeder, R.G.6    Rhodes, D.7
  • 61
    • 18944384374 scopus 로고    scopus 로고
    • A nonhistone protein-protein interaction required for assembly of the SIR complex and silent chromatin
    • DOI 10.1128/MCB.25.11.4514-4528.2005
    • Rudner AD, Hall BE, Ellenberger T, Moazed D (2005) A nonhistone protein-protein interaction required for assembly of the SIR complex and silent chromatin. Mol Cell Biol 25: 4514-4528 (Pubitemid 40705757)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.11 , pp. 4514-4528
    • Rudner, A.D.1    Hall, B.E.2    Ellenberger, T.3    Moazed, D.4
  • 62
    • 0037636027 scopus 로고    scopus 로고
    • The establishment, inheritance, and function of silenced chromatin in Saccharomyces cerevisiae
    • DOI 10.1146/annurev.biochem.72.121801.161547
    • Rusche LN, Kirchmaier AL, Rine J (2003) The establishment, inheritance, and function of silenced chromatin in Saccharomyces cere-visiae. Annu Rev Biochem 72: 481-516 (Pubitemid 36930453)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 481-516
    • Rusche, L.N.1    Kirchmaier, A.L.2    Rine, J.3
  • 63
    • 66349093144 scopus 로고    scopus 로고
    • Mutational analysis of the Sir3 BAH domain reveals multiple points of interaction with nucleosomes
    • Sampath V, Yuan P, Wang IX, Prugar E, van Leeuwen F, Sternglanz R (2009) Mutational analysis of the Sir3 BAH domain reveals multiple points of interaction with nucleosomes. Mol Cell Biol 29: 2532-2545
    • (2009) Mol Cell Biol , vol.29 , pp. 2532-2545
    • Sampath, V.1    Yuan, P.2    Wang, I.X.3    Prugar, E.4    Van Leeuwen, F.5    Sternglanz, R.6
  • 64
    • 33846023720 scopus 로고    scopus 로고
    • Rtt109 is required for proper H3K56 acetylation: A chromatin mark associated with the elongating RNA polymerase II
    • DOI 10.1074/jbc.C600265200
    • 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 (Pubitemid 46042030)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.49 , pp. 37270-37274
    • Schneider, J.1    Bajwa, P.2    Johnson, F.C.3    Bhaumik, S.R.4    Shilatifard, A.5
  • 65
    • 77953004689 scopus 로고    scopus 로고
    • Heterochromatin protein 1 (HP1) modulates replication timing of the Drosophila genome
    • Schwaiger M, Kohler H, Oakeley EJ, Stadler MB, Schubeler D (2010) Heterochromatin protein 1 (HP1) modulates replication timing of the Drosophila genome. Genome Res 20: 771-780
    • (2010) Genome Res , vol.20 , pp. 771-780
    • Schwaiger, M.1    Kohler, H.2    Oakeley, E.J.3    Stadler, M.B.4    Schubeler, D.5
  • 66
    • 0035805063 scopus 로고    scopus 로고
    • Silenced chromatin is permissive to activator binding and PIC recruitment
    • DOI 10.1016/S0092-8674(01)00329-4
    • Sekinger EA, Gross DS (2001) Silenced chromatin is permissive to activator binding and PIC recruitment. Cell 105: 403-414 (Pubitemid 32455346)
    • (2001) Cell , vol.105 , Issue.3 , pp. 403-414
    • Sekinger, E.A.1    Gross, D.S.2
  • 67
    • 32444434989 scopus 로고    scopus 로고
    • Histone H4-K16 acetylation controls chromatin structure and protein interactions
    • DOI 10.1126/science.1124000
    • Shogren-Knaak M, Ishii H, Sun JM, Pazin MJ, Davie JR, Peterson CL (2006) Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 311: 844-847 (Pubitemid 43228847)
    • (2006) Science , vol.311 , Issue.5762 , pp. 844-847
    • Shogren-Knaak, M.1    Ishii, H.2    Sun, J.-M.3    Pazin, M.J.4    Davie, J.R.5    Peterson, C.L.6
  • 68
    • 0037402422 scopus 로고    scopus 로고
    • Mass spectrometric quantification of acetylation at specific lysines within the amino-terminal tail of histone H4
    • DOI 10.1016/S0003-2697(03)00032-0
    • Smith CM, Gafken PR, Zhang Z, Gottschling DE, Smith JB, Smith DL (2003) Mass spectrometric quantification of acetylation at specific lysines within the amino-terminal tail of histone H4. Anal Biochem 316: 23-33 (Pubitemid 36407629)
    • (2003) Analytical Biochemistry , vol.316 , Issue.1 , pp. 23-33
    • Smith, C.M.1    Gafken, P.R.2    Zhang, Z.3    Gottschling, D.E.4    Smith, J.B.5    Smith, D.L.6
  • 70
    • 0031027431 scopus 로고    scopus 로고
    • SIR2 and SIR4 interactions differ in core and extended telomeric heterochromatin in yeast
    • Strahl-Bolsinger S, Hecht A, Luo K, Grunstein M (1997) SIR2 and SIR4 interactions differ in core and extended telomeric hetero-chromatin in yeast. Genes Dev 11 : 83-93 (Pubitemid 27043826)
    • (1997) Genes and Development , vol.11 , Issue.1 , pp. 83-93
    • Strahl-Bolsinger, S.1    Hecht, A.2    Luo, K.3    Grunstein, M.4
  • 71
    • 0036842129 scopus 로고    scopus 로고
    • Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine16 and spreading of heterochromatin
    • DOI 10.1038/ng1017
    • Suka N, Luo K, Grunstein M (2002) Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine16 and spreading of heterochromatin. Nat Genet 32: 378-383 (Pubitemid 35266111)
    • (2002) Nature Genetics , vol.32 , Issue.3 , pp. 378-383
    • Suka, N.1    Luo, K.2    Grunstein, M.3
  • 72
    • 0034839973 scopus 로고    scopus 로고
    • Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin
    • DOI 10.1016/S1097-2765(01)00301-X
    • Suka N, Suka Y, Carmen AA, Wu J, Grunstein M (2001) Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin. Mol Cell 8: 473-479 (Pubitemid 32831564)
    • (2001) Molecular Cell , vol.8 , Issue.2 , pp. 473-479
    • Suka, N.1    Suka, Y.2    Carmen, A.A.3    Wu, J.4    Grunstein, M.5
  • 73
    • 0033598942 scopus 로고    scopus 로고
    • An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing
    • Tanny JC, Dowd GJ, Huang J, Hilz H, Moazed D (1999) An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing. Cell 99: 735-745 (Pubitemid 30017644)
    • (1999) Cell , vol.99 , Issue.7 , pp. 735-745
    • Tanny, J.C.1    Dowd, G.J.2    Huang, J.3    Hilz, H.4    Moazed, D.5
  • 74
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • DOI 10.1016/S0092-8674(02)00759-6
    • van Leeuwen F, Gafken PR, Gottschling DE (2002) Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell 109: 745-756 (Pubitemid 34727348)
    • (2002) Cell , vol.109 , Issue.6 , pp. 745-756
    • Van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 75
    • 77749325109 scopus 로고    scopus 로고
    • Acetylation of H3 K56 is required for RNA polymerase II transcript elongation through heterochromatin in yeast
    • Varv S, Kristjuhan K, Peil K, Looke M, Mahlakoiv T, Paapsi K, Kristjuhan A (2010) Acetylation of H3 K56 is required for RNA polymerase II transcript elongation through heterochromatin in yeast. Mol Cell Biol 30: 1467-1477
    • (2010) Mol Cell Biol , vol.30 , pp. 1467-1477
    • Varv, S.1    Kristjuhan, K.2    Peil, K.3    Looke, M.4    Mahlakoiv, T.5    Paapsi, K.6    Kristjuhan, A.7
  • 76
    • 68949190829 scopus 로고    scopus 로고
    • Multiple histone modifications in euchromatin promote heterochromatin formation by redundant mechanisms in Saccharomyces cerevisiae
    • Verzijlbergen KF, Faber AW, Stulemeijer IJ, van Leeuwen F (2009) Multiple histone modifications in euchromatin promote heterochromatin formation by redundant mechanisms in Saccharomyces cerevisiae. BMC Mol Biol 10: 76
    • (2009) BMC Mol Biol , vol.10 , pp. 76
    • Verzijlbergen, K.F.1    Faber, A.W.2    Stulemeijer, I.J.3    Van Leeuwen, F.4
  • 77
    • 48249148195 scopus 로고    scopus 로고
    • Acetylation in the globular core of histone H3 on lysine-56 promotes chromatin disassembly during transcriptional activation
    • Williams SK, Truong D, Tyler JK (2008) Acetylation in the globular core of histone H3 on lysine-56 promotes chromatin disassembly during transcriptional activation. Proc Natl Acad Sci USA 105: 9000-9005
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 9000-9005
    • Williams, S.K.1    Truong, D.2    Tyler, J.K.3
  • 79
    • 18844413266 scopus 로고    scopus 로고
    • Acetylation in histone H3 globular domain regulates gene expression in yeast
    • DOI 10.1016/j.cell.2005.03.011, PII S0092867405002837
    • Xu F, Zhang K, Grunstein M (2005) Acetylation in histone H3 globular domain regulates gene expression in yeast. Cell 121: 375-385 (Pubitemid 40692298)
    • (2005) Cell , vol.121 , Issue.3 , pp. 375-385
    • Xu, F.1    Zhang, K.2    Grunstein, M.3
  • 80
    • 34748909429 scopus 로고    scopus 로고
    • Sir2 deacety-lates histone H3 lysine 56 to regulate telomeric heterochromatin structure in yeast
    • DOI 10.1016/j.molcel.2007.07.021, PII S1097276507004947
    • Xu F, Zhang Q, Zhang K, Xie W, Grunstein M (2007) Sir2 deacety-lates histone H3 lysine 56 to regulate telomeric heterochromatin structure in yeast. Mol Cell 27: 890-900 (Pubitemid 47488183)
    • (2007) Molecular Cell , vol.27 , Issue.6 , pp. 890-900
    • Xu, F.1    Zhang, Q.2    Zhang, K.3    Xie, W.4    Grunstein, M.5
  • 81
    • 48449102453 scopus 로고    scopus 로고
    • Insights into the impact of histone acetylation and methylation on Sir protein recruitment, spreading, and silencing in Saccharomyces cerevisiae
    • Yang B, Britton J, Kirchmaier AL (2008a) Insights into the impact of histone acetylation and methylation on Sir protein recruitment, spreading, and silencing in Saccharomyces cerevisiae. J Mol Biol 381: 826-844
    • (2008) J Mol Biol , vol.381 , pp. 826-844
    • Yang, B.1    Britton, J.2    Kirchmaier, A.L.3
  • 82
    • 33845393998 scopus 로고    scopus 로고
    • Bypassing the catalytic activity of SIR2 for SIR protein spreading in Saccharomyces cerevisiae
    • DOI 10.1091/mbc.E06-08-0669
    • Yang B, Kirchmaier AL (2006) Bypassing the catalytic activity of SIR2 for SIR protein spreading in Saccharomyces cerevisiae. Mol Biol Cell 17: 5287-5297 (Pubitemid 44907369)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.12 , pp. 5287-5297
    • Yang, B.1    Kirchmaier, A.L.2
  • 83
    • 58149293992 scopus 로고    scopus 로고
    • HST3/HST4-dependent deacetylation of lysine 56 of histone H3 in silent chromatin
    • Yang B, Miller A, Kirchmaier AL (2008b) HST3/HST4-dependent deacetylation of lysine 56 of histone H3 in silent chromatin. Mol Biol Cell 19: 4993-5005
    • (2008) Mol Biol Cell , vol.19 , pp. 4993-5005
    • Yang, B.1    Miller, A.2    Kirchmaier, A.L.3
  • 84
    • 52649105525 scopus 로고    scopus 로고
    • Positive roles of SAS2 in DNA replication and transcriptional silencing in yeast
    • Zou Y, Bi X (2008) Positive roles of SAS2 in DNA replication and transcriptional silencing in yeast. Nucleic Acids Res 36: 5189-5200
    • (2008) Nucleic Acids Res , vol.36 , pp. 5189-5200
    • Zou, Y.1    Bi, X.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.