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Volumn 34, Issue 12, 2006, Pages 3555-3567

The WD40-repeat protein Pwp1p associates in vivo with 25S ribosomal chromatin in a histone H4 tail-dependent manner

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE; MAGNESIUM; MICROCOCCAL NUCLEASE; NONHISTONE PROTEIN; PWP1 PROTEIN, S CEREVISIAE; RIBOSOME RNA; RNA, RIBOSOMAL, 25S; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 33746788651     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkl487     Document Type: Article
Times cited : (13)

References (66)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • DOI 10.1038/38444
    • Luger,K., Mader,A.W., Richmond,R.K., Sargent,D.F. and Richmond,T.J. (1997) Crystal structure of the nucleosome core particle at 2.8 Å 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
  • 2
    • 0036089388 scopus 로고    scopus 로고
    • Conformational dynamics of the chromatin fiber in solution: Determinants, mechanisms, and functions
    • Hansen,J.C. (2002) Conformational dynamics of the chromatin fiber in solution: determinants, mechanisms, and functions. Annu. Rev. Biophys. Biomol. Struct., 31, 361-392.
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 361-392
    • Hansen, J.C.1
  • 3
    • 25844484588 scopus 로고    scopus 로고
    • Salt-dependent intra- and internucleosomal interactions of the H3 tail domain in a model oligonucleosomal array
    • DOI 10.1074/jbc.M507241200
    • Zheng,C., Lu,X, Hansen,J.C. and Hayes,J.J. (2005) Salt-dependent intra- and internucleosomal interactions of the H3 tail domain in a model oligonucleosomal array. J. Biol. Chem., 280, 33552-33557. (Pubitemid 41397155)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.39 , pp. 33552-33557
    • Zheng, C.1    Lu, X.2    Hansen, J.C.3    Hayes, J.J.4
  • 4
    • 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,S.M. and 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
  • 5
    • 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,A.A., Milne,L. and 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
  • 6
    • 0037291695 scopus 로고    scopus 로고
    • Different sensitivities of bromodomain factors 1 and 2 to histone H4 acetylation
    • DOI 10.1016/S1097-2765(03)00033-9
    • Matangkasombut,O. and Buratowski,S. (2003) Different sensitivities of bromodomain factors 1 and 2 to histone H4 acetylation. Mol. Cell, 11, 353-363. (Pubitemid 36293830)
    • (2003) Molecular Cell , vol.11 , Issue.2 , pp. 353-363
    • Matangkasombut, O.1    Buratowski, S.2
  • 7
    • 0037291760 scopus 로고    scopus 로고
    • Bromodomains mediate an acetyl-histone encoded antisilencing function at heterochromatin boundaries
    • DOI 10.1016/S1097-2765(03)00035-2
    • Ladurner,A.G., Inouye,C., Jain,R. and Tjian,R. (2003) Bromodomains mediate an acetyl-histone encoded antisilencing function at heterochromatin boundaries. Mol. Cell, 11, 365-376. (Pubitemid 36293831)
    • (2003) Molecular Cell , vol.11 , Issue.2 , pp. 365-376
    • Ladurner, A.G.1    Inouye, C.2    Jain, R.3    Tjian, R.4
  • 8
    • 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. and 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
  • 9
    • 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. and 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
  • 10
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • DOI 10.1038/35065132
    • Lachner,M., O'Carroll,D., Rea,S., Mechtler,K. and Jenuwein,T. (2001) Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature, 410, 116-120. (Pubitemid 32225847)
    • (2001) Nature , vol.410 , Issue.6824 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 11
    • 0035282458 scopus 로고    scopus 로고
    • Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
    • DOI 10.1038/35065138
    • Bannister,A.J., Zegerman,P., Partridge,J.F., Miska,E.A., Thomas,J.O., Allshire,R.C. and Kouzarides,T. (2001) Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain. Nature, 410, 120-124. (Pubitemid 32225848)
    • (2001) Nature , vol.410 , Issue.6824 , pp. 120-124
    • Bannister, A.J.1    Zegerman, P.2    Partridge, J.F.3    Miska, E.A.4    Thomas, J.O.5    Allshire, R.C.6    Kouzarides, T.7
  • 12
    • 0036830642 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in polycomb-group silencing
    • DOI 10.1126/science.1076997
    • Cao,R., Wang,L., Wang,H., Xia,L., Erdjument-Bromage,H., Tempst,P., Jones,R.S. and Zhang,Y. (2002) Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science, 298, 1039-1043. (Pubitemid 35247314)
    • (2002) Science , vol.298 , Issue.5595 , pp. 1039-1043
    • Cao, R.1    Wang, L.2    Wang, H.3    Xia, L.4    Erdjument-Bromage, H.5    Tempst, P.6    Jones, R.S.7    Zhang, Y.8
  • 13
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • DOI 10.1126/science.1063127
    • Jenuwein,T. and Allis,C.D. (2001) Translating the histone code. Science, 293, 1074-1080. (Pubitemid 32758077)
    • (2001) Science , vol.293 , Issue.5532 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 14
    • 0037023681 scopus 로고    scopus 로고
    • Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex
    • DOI 10.1074/jbc.C200045200
    • Zegerman,P., Canas,B., Pappin,D. and Kouzarides,T. (2002) Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex. J. Biol. Chem., 277, 11621-11624. (Pubitemid 34952711)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.14 , pp. 11621-11624
    • Zegerman, P.1    Canas, B.2    Pappin, D.3    Kouzarides, T.4
  • 16
    • 2642536094 scopus 로고    scopus 로고
    • Direct binding of INHAT to H3 tails disrupted by modifications
    • DOI 10.1074/jbc.C400151200
    • Schneider,R., Bannister,A.J., Weise,C. and Kouzarides,T. (2004) Direct binding of INHAT to H3 tails disrupted by modifications. J. Biol. Chem., 279, 23859-23862. (Pubitemid 38725241)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.23 , pp. 23859-23862
    • Schneider, R.1    Bannister, A.J.2    Weise, C.3    Kouzarides, T.4
  • 17
    • 20444417108 scopus 로고    scopus 로고
    • WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development
    • DOI 10.1016/j.cell.2005.03.036, PII S0092867405003557
    • Wysocka,J., Swigut,T., Milne,T.A., Dou,Y., Zhang,X., Burlingame,A.L., Roeder,R.G., Brivanlou,A.H. and Allis,C.D. (2005) WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development. Cell, 121, 859-872. (Pubitemid 40806418)
    • (2005) Cell , vol.121 , Issue.6 , pp. 859-872
    • Wysocka, J.1    Swigut, T.2    Milne, T.A.3    Dou, Y.4    Zhang, X.5    Burlingame, A.L.6    Roeder, R.G.7    Brivanlou, A.H.8    Allis, C.D.9
  • 19
    • 0025736044 scopus 로고
    • Yeast histone H4 N-terminal sequence is required for promoter activation in vivo
    • Durrin,L.K., Mann,R.K., Kayne,P.S. and Grunstein,M. (1991) Yeast histone H4 N-terminal sequence is required for promoter activation in vivo. Cell, 65, 1023-1031. (Pubitemid 121001690)
    • (1991) Cell , vol.65 , Issue.6 , pp. 1023-1031
    • Durrin, L.K.1    Mann, R.K.2    Kayne, P.S.3    Grunstein, M.4
  • 20
    • 0035016612 scopus 로고    scopus 로고
    • Interactions of Isw2 chromatin remodeling complex with nucleosomal arrays: Analyses using recombinant yeast histones and immobilized templates
    • DOI 10.1128/MCB.21.6.2098-2106.2001
    • Gelbart,M.E., Rechsteiner,T., Richmond,T.J. and Tsukiyama,T. (2001) Interactions of Isw2 chromatin remodeling complex with nucleosomal arrays: analyses using recombinant yeast histones and immobilized templates. Mol. Cell Biol., 21, 2098-2106. (Pubitemid 32479631)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.6 , pp. 2098-2106
    • Gelbart, M.E.1    Rechsteiner, T.2    Richmond, T.J.3    Tsukiyama, T.4
  • 21
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • DOI 10.1002/(SICI)1097-0061(199807)14:10<953::AID-YEA293>3.0.CO;2-U
    • Longtine,M.S., McKenzie,A.,III, Demarini,D.J., Shah,N.G., Wach,A., Brachat,A., Philippsen,P. and Pringle,J.R. (1998) Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast, 14, 953-961. (Pubitemid 28328001)
    • (1998) Yeast , vol.14 , Issue.10 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 22
    • 0031455421 scopus 로고    scopus 로고
    • Persistent initiation of DNA replication and chromatin-bound MCM proteins during the cell cycle in cdc6 mutants
    • Liang,C. and Stillman,B. (1997) Persistent initiation of DNA replication and chromatin-bound MCM proteins during the cell cycle in cdc6 mutants. Genes Dev., 11, 3375-3386. (Pubitemid 28024028)
    • (1997) Genes and Development , vol.11 , Issue.24 , pp. 3375-3386
    • Liang, C.1    Stillman, B.2
  • 23
    • 0033040839 scopus 로고    scopus 로고
    • Isolation of minichromosomes from yeast cells
    • DOI 10.1016/S0076-6879(99)04005-7
    • Alfieri,J.A. and Clark,D.J. (1999) Isolation of minichromosomes from yeast cells. Methods Enzymol., 304, 35-49. (Pubitemid 29268876)
    • (1999) Methods in Enzymology , vol.304 , pp. 35-49
    • Alfieri, J.A.1    Clark, D.J.2
  • 24
    • 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,A.A., Wu,J. and 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
  • 25
    • 0034721670 scopus 로고    scopus 로고
    • The Isw2 chromatin remodeling complex represses early meiotic genes upon recruitment by Ume6p
    • Goldmark,J.P., Fazzio,T.G., Estep,P.W., Church,G.M. and Tsukiyama,T. (2000) The Isw2 chromatin remodeling complex represses early meiotic genes upon recruitment by Ume6p. Cell, 103, 423-433.
    • (2000) Cell , vol.103 , pp. 423-433
    • Goldmark, J.P.1    Fazzio, T.G.2    Estep, P.W.3    Church, G.M.4    Tsukiyama, T.5
  • 26
    • 0029882454 scopus 로고    scopus 로고
    • Reversible oligonucleosome self-association: Dependence on divalent cations and core histone tail domains
    • DOI 10.1021/bi9525684
    • Schwarz,P.M., Felthauser,A., Fletcher,T.M. and Hansen,J.C. (1996) Reversible oligonucleosome self-association: dependence on divalent cations and core histone tail domains. Biochemistry, 35, 4009-4015. (Pubitemid 26113457)
    • (1996) Biochemistry , vol.35 , Issue.13 , pp. 4009-4015
    • Schwarz, P.M.1    Felthauser, A.2    Fletcher, T.M.3    Hansen, J.C.4
  • 30
    • 0032784327 scopus 로고    scopus 로고
    • The nuclear actin-related protein of Saccharomyces cerevisiae, Act3p/Arp4, interacts with core histones
    • Harata,M., Oma,Y., Mizuno,S., Jiang,Y.W., Stillman,D.J. and Wintersberger,U. (1999) The nuclear actin-related protein of Saccharomyces cerevisiae, Act3p/Arp4, interacts with core histones. Mol. Biol. Cell, 10, 2595-2605. (Pubitemid 29393513)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.8 , pp. 2595-2605
    • Harata, M.1    Oma, Y.2    Mizuno, S.3    Jiang, Y.W.4    Stillman, D.J.5    Wintersberger, U.6
  • 32
    • 0036464569 scopus 로고    scopus 로고
    • A critical epitope for substrate recognition by the nucleosome remodeling ATPase ISWI
    • Clapier,C.R., Nightingale,K.P. and Becker,P.B. (2002) A critical epitope for substrate recognition by the nucleosome remodeling ATPase ISWI. Nucleic Acids Res., 30, 649-655. (Pubitemid 34679629)
    • (2002) Nucleic Acids Research , vol.30 , Issue.3 , pp. 649-655
    • Clapier, C.R.1    Nightingale, K.P.2    Becker, P.B.3
  • 35
    • 0347510578 scopus 로고    scopus 로고
    • Involvement of two endonuclease III homologs in the base excision repair pathway for the processing of DNA alkylation damage in Saccharomyces cerevisiae
    • DOI 10.1016/j.dnarep.2003.09.005
    • Hanna,M., Chow,B.L., Morey,N.J., Jinks-Robertson,S., Doetsch,P.W. and Xiao,W. (2004) Involvement of two endonuclease III homologs in the base excision repair pathway for the processing of DNA alkylation damage in Saccharomyces cerevisiae. DNA Repair (Amst), 3, 51-59. (Pubitemid 38021995)
    • (2004) DNA Repair , vol.3 , Issue.1 , pp. 51-59
    • Hanna, M.1    Chow, B.L.2    Morey, N.J.3    Jinks-Robertson, S.4    Doetsch, P.W.5    Xiao, W.6
  • 36
    • 28444456705 scopus 로고    scopus 로고
    • The histone code at DNA breaks: A guide to repair?
    • van Attikum,H. and Gasser,S.M. (2005) The histone code at DNA breaks: a guide to repair? Nat. Rev. Mol. Cell Biol., 6, 757-765.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 757-765
    • Van Attikum, H.1    Gasser, S.M.2
  • 37
    • 1442286922 scopus 로고    scopus 로고
    • A nuclear FK506-binding protein is a histone chaperone regulating rDNA silencing
    • DOI 10.1038/nsmb733
    • Kuzuhara,T. and Horikoshi,M. (2004) A nuclear FK506-binding protein is a histone chaperone regulating rDNA silencing. Nat. Struct. Mol. Biol., 11, 275-283. (Pubitemid 38282774)
    • (2004) Nature Structural and Molecular Biology , vol.11 , Issue.3 , pp. 275-283
    • Kuzuhara, T.1    Horikoshi, M.2
  • 39
    • 0038105065 scopus 로고    scopus 로고
    • True XP group E patients have a defective UV-damaged DNA binding protein complex and mutations in DDB2 which reveal the functional domains of its p48 product
    • DOI 10.1093/hmg/ddg174
    • Rapic-Otrin,V., Navazza,V., Nardo,T., Botta,E., McLenigan,M., Bisi,D.C., Levine,A.S. and Stefanini,M. (2003) True XP group E patients have a defective UV-damaged DNA binding protein complex and mutations in DDB2 which reveal the functional domains of its p48 product. Hum. Mol. Genet., 12, 1507-1522. (Pubitemid 36857299)
    • (2003) Human Molecular Genetics , vol.12 , Issue.13 , pp. 1507-1522
    • Rapic-Otrin, V.1    Navazza, V.2    Nardo, T.3    Botta, E.4    McLenigan, M.5    Bisi, D.C.6    Levine, A.S.7    Stefanini, M.8
  • 40
    • 0001232093 scopus 로고    scopus 로고
    • p48 activates a UV-damaged-DNA binding factor and is defective in xeroderma pigmentosum group E cells that lack binding activity
    • Hwang,B.J., Toering,S., Francke,U. and Chu,G. (1998) p48 Activates a UV-damaged-DNA binding factor and is defective in xeroderma pigmentosum group E cells that lack binding activity. Mol. Cell. Biol., 18, 4391-4399. (Pubitemid 28287962)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.7 , pp. 4391-4399
    • Hwang, B.J.1    Toering, S.2    Francke, U.3    Chu, G.4
  • 41
    • 0034607991 scopus 로고    scopus 로고
    • Identification of two novel TAF subunits of the yeast Saccharomyces cerevisiae TFIID complex
    • DOI 10.1074/jbc.275.18.13895
    • Sanders,S.L. and Weil,P.A. (2000) Identification of two novel TAF subunits of the yeast Saccharomyces cerevisiae TFIID complex. J. Biol. Chem., 275, 13895-13900. (Pubitemid 30257465)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.18 , pp. 13895-13900
    • Sanders, S.L.1    Weil, P.A.2
  • 43
    • 0042671282 scopus 로고    scopus 로고
    • Involvement of actin-related proteins in ATP-dependent chromatin remodeling
    • DOI 10.1016/S1097-2765(03)00264-8
    • Shen,X., Ranallo,R., Choi,E. and Wu,C. (2003) Involvement of actin-related proteins in ATP-dependent chromatin remodeling. Mol. Cell, 12, 147-155. (Pubitemid 36945043)
    • (2003) Molecular Cell , vol.12 , Issue.1 , pp. 147-155
    • Shen, X.1    Ranallo, R.2    Choi, E.3    Wu, C.4
  • 45
    • 0030979570 scopus 로고    scopus 로고
    • A role for the divergent actin gene, ACT2, in nuclear pore structure and function
    • DOI 10.1093/emboj/16.12.3572
    • Yan,C., Leibowitz,N. and Melese,T. (1997) A role for the divergent actin gene, ACT2, in nuclear pore structure and function. EMBO J., 16, 3572-3586. (Pubitemid 27250051)
    • (1997) EMBO Journal , vol.16 , Issue.12 , pp. 3572-3586
    • Yan, C.1    Leibowitz, N.2    Melese, T.3
  • 46
    • 0029025345 scopus 로고
    • Identification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes
    • Enenkel,C., Blobel,G. and Rexach,M. (1995) Identification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes. J. Biol. Chem., 270, 16499-16502.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16499-16502
    • Enenkel, C.1    Blobel, G.2    Rexach, M.3
  • 47
    • 2342501365 scopus 로고    scopus 로고
    • Genome-wide localization of the nuclear transport machinery couples transcriptional status and nuclear organization
    • DOI 10.1016/S0092-8674(04)00448-9, PII S0092867404004489
    • Casolari,J.M., Brown,C.R., Komili,S., West,J., Hieronymus,H. and Silver,P.A. (2004) Genome-wide localization of the nuclear transport machinery couples transcriptional status and nuclear organization. Cell, 117, 427-439. (Pubitemid 38610229)
    • (2004) Cell , vol.117 , Issue.4 , pp. 427-439
    • Casolari, J.M.1    Brown, C.R.2    Komili, S.3    West, J.4    Hieronymus, H.5    Silver, P.A.6
  • 48
    • 2542499556 scopus 로고    scopus 로고
    • Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent protein kinase-like kinase Pkh1p and downstream signaling pathways Pkc1p and Ypk1p
    • DOI 10.1074/jbc.M400299200
    • Zhang,X., Lester,R.L. and Dickson,R.C. (2004) Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent protein kinaselike kinase Pkh1p and downstream signaling pathways Pkc1p and Ypk1p. J. Biol. Chem., 279, 22030-22038. (Pubitemid 38679394)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.21 , pp. 22030-22038
    • Zhang, X.1    Lester, R.L.2    Dickson, R.C.3
  • 49
    • 0035024077 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae suppressor of choline sensitivity (SCS2) gene is a multicopy suppressor of mec1 telomeric silencing defects
    • Craven,R.J. and Petes,T.D. (2001) The Saccharomyces cerevisiae suppressor of choline sensitivity (SCS2) gene is a multicopy suppressor of mec1 telomeric silencing defects. Genetics, 158, 145-154. (Pubitemid 32428637)
    • (2001) Genetics , vol.158 , Issue.1 , pp. 145-154
    • Craven, R.J.1    Petes, T.D.2
  • 50
    • 0024280881 scopus 로고
    • Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeast
    • Kayne,P.S., Kim,U.J., Han,M., Mullen,J.R., Yoshizaki,F. and Grunstein,M. (1988) Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeast. Cell, 55, 27-39.
    • (1988) Cell , vol.55 , pp. 27-39
    • Kayne, P.S.1    Kim, U.J.2    Han, M.3    Mullen, J.R.4    Yoshizaki, F.5    Grunstein, M.6
  • 52
    • 0042822279 scopus 로고    scopus 로고
    • Association of the RENT complex with nontranscribed and coding regions of rDNA and a regional requirement for the replication fork block protein Fob1 in rDNA silencing
    • DOI 10.1101/gad.1108403
    • Huang,J. and Moazed,D. (2003) Association of the RENT complex with nontranscribed and coding regions of rDNA and a regional requirement for the replication fork block protein Fob1 in rDNA silencing. Genes Dev., 17, 2162-2176. (Pubitemid 37052295)
    • (2003) Genes and Development , vol.17 , Issue.17 , pp. 2162-2176
    • Huang, J.1    Moazed, D.2
  • 53
    • 0029817763 scopus 로고    scopus 로고
    • Spreading of transcriptional repressor SIR3 from telomeric heterochromatin
    • DOI 10.1038/383092a0
    • Hecht,A., Strahl-Bolsinger,S. and Grunstein,M. (1996) Spreading of transcriptional repressor SIR3 from telomeric heterochromatin. Nature, 383, 92-96. (Pubitemid 26296468)
    • (1996) Nature , vol.383 , Issue.6595 , pp. 92-96
    • Hecht, A.1    Strahl-Bolsinger, S.2    Grunstein, M.3
  • 54
  • 55
    • 1942472057 scopus 로고    scopus 로고
    • Hif1 is a component of yeast histone acetyltransferase B, a complex mainly localized in the nucleus
    • Poveda,A., Pamblanco,M., Tafrov,S., Tordera,V., Sternglanz,R. and Sendra,R. (2004) Hif1 is a component of yeast histone acetyltransferase B, a complex mainly localized in the nucleus. J. Biol. Chem., 279, 6033-6043.
    • (2004) J. Biol. Chem. , vol.279 , pp. 6033-6043
    • Poveda, A.1    Pamblanco, M.2    Tafrov, S.3    Tordera, V.4    Sternglanz, R.5    Sendra, R.6
  • 56
    • 0034490962 scopus 로고    scopus 로고
    • Thirty-plus functional families from a single motif
    • Yu,L., Gaitatzes,C., Neer,E. and Smith,T.F. (2000) Thirty-plus functional families from a single motif. Protein Sci., 9, 2470-2476. (Pubitemid 32105729)
    • (2000) Protein Science , vol.9 , Issue.12 , pp. 2470-2476
    • Yu, L.1    Gaitatzes, C.2    Neer, E.3    Smith, T.F.4
  • 57
    • 0030003051 scopus 로고    scopus 로고
    • Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4
    • Edmondson,D.G., Smith,M.M. and Roth,S.Y. (1996) Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4. Genes Dev., 10, 1247-1259. (Pubitemid 26171105)
    • (1996) Genes and Development , vol.10 , Issue.10 , pp. 1247-1259
    • Edmondson, D.G.1    Smith, M.M.2    Roth, S.Y.3
  • 58
    • 0030720332 scopus 로고    scopus 로고
    • The Groucho/transducin-like enhancer of split transcriptional repressors interact with the genetically defined amino-terminal silencing domain of histone H3
    • DOI 10.1074/jbc.272.42.26604
    • Palaparti,A., Baratz,A. and Stifani,S. (1997) The Groucho/transducinlike enhancer of split transcriptional repressors interact with the genetically defined amino-terminal silencing domain of histone H3. J. Biol. Chem., 272, 26604-26610. (Pubitemid 27458883)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.42 , pp. 26604-26610
    • Palaparti, A.1    Baratz, A.2    Stifani, S.3
  • 59
    • 0344405718 scopus 로고    scopus 로고
    • Purification and functional characterization of the human N-CoR complex: The roles of HDAC3, TBL1 and TBLR1
    • DOI 10.1093/emboj/cdg120
    • Yoon,H.G., Chan,D.W., Huang,Z.Q., Li,J., Fondell,J.D., Qin,J. and Wong,J. (2003) Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1. EMBO J., 22, 1336-1346. (Pubitemid 36362697)
    • (2003) EMBO Journal , vol.22 , Issue.6 , pp. 1336-1346
    • Yoon, H.-G.1    Chan, D.W.2    Huang, Z.-Q.3    Li, J.4    Fondell, J.D.5    Qin, J.6    Wong, J.7
  • 60
    • 0035801407 scopus 로고    scopus 로고
    • NoRC - A novel member of mammalian ISWI-containing chromatin remodeling machines
    • DOI 10.1093/emboj/20.17.4892
    • Strohner,R., Nemeth,A., Jansa,P., Hofmann-Rohrer,U., Santoro,R., Langst,G. and Grummt,I. (2001) NoRC-a novel member of mammalian ISWI-containing chromatin remodeling machines. EMBO J., 20, 4892-4900. (Pubitemid 32848641)
    • (2001) EMBO Journal , vol.20 , Issue.17 , pp. 4892-4900
    • Strohner, R.1    Nemeth, A.2    Jansa, P.3    Hofmann-Rohrer, U.4    Santoro, R.5    Langst, G.6    Grummt, I.7
  • 61
    • 23244448558 scopus 로고    scopus 로고
    • The PHD finger/bromodomain of NoRC interacts with acetylated histone H4K16 and is sufficient for rDNA silencing
    • DOI 10.1016/j.cub.2005.06.057, PII S0960982205006925
    • Zhou,Y. and Grummt,I. (2005) The PHD finger/bromodomain of NoRC interacts with acetylated histone H4K16 and is sufficient for rDNA silencing. Curr. Biol., 15, 1434-1438. (Pubitemid 41097550)
    • (2005) Current Biology , vol.15 , Issue.15 , pp. 1434-1438
    • Zhou, Y.1    Grummt, I.2
  • 62
    • 0033574603 scopus 로고    scopus 로고
    • Net1, a Sir2-associated nucleolar protein required for rDNA silencing and nucleolar integrity
    • Straight,A.F., Shou,W., Dowd,G.J., Turck,C.W., Deshaies,R.J., Johnson,A.D. and Moazed,D. (1999) Net1, a Sir2-associated nucleolar protein required for rDNA silencing and nucleolar integrity. Cell, 97, 245-256. (Pubitemid 29194275)
    • (1999) Cell , vol.97 , Issue.2 , pp. 245-256
    • Straight, A.F.1    Shou, W.2    Dowd, G.J.3    Turck, C.W.4    Deshaies, R.J.5    Johnson, A.D.6    Moazed, D.7
  • 64
    • 3543038804 scopus 로고    scopus 로고
    • Budding yeast silencing complexes and regulation of Sir2 activity by protein-protein interactions
    • DOI 10.1128/MCB.24.16.6931-6946.2004
    • Tanny,J.C., Kirkpatrick,D.S., Gerber,S.A., Gygi,S.P. and Moazed,D. (2004) Budding yeast silencing complexes and regulation of Sir2 activity by protein-protein interactions. Mol. Cell Biol., 24, 6931-6946. (Pubitemid 39014422)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.16 , pp. 6931-6946
    • Tanny, J.C.1    Kirkpatrick, D.S.2    Gerber, S.A.3    Gygi, S.P.4    Moazed, D.5
  • 66
    • 0033790431 scopus 로고    scopus 로고
    • Chromosome cohesion, condensation, and separation
    • Hirano,T. (2000) Chromosome cohesion, condensation, and separation. Annu. Rev. Biochem., 69, 115-144.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 115-144
    • Hirano, T.1


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