메뉴 건너뛰기




Volumn 6, Issue , 2011, Pages

Human linker histones: Interplay between phosphorylation and O-β-GlcNAc to mediate chromatin structural modifications

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTA; HOMO SAPIENS; MAMMALIA;

EID: 79960179866     PISSN: None     EISSN: 17471028     Source Type: Journal    
DOI: 10.1186/1747-1028-6-15     Document Type: Article
Times cited : (8)

References (87)
  • 1
    • 0037072601 scopus 로고    scopus 로고
    • Molecular biology. Chromatin higher order folding-wrapping up transcription
    • 10.1126/science.1074200, 12228709
    • Horn PJ, Peterson CL. Molecular biology. Chromatin higher order folding-wrapping up transcription. Science 2002, 297:1824-1827. 10.1126/science.1074200, 12228709.
    • (2002) Science , vol.297 , pp. 1824-1827
    • Horn, P.J.1    Peterson, C.L.2
  • 3
    • 0034649663 scopus 로고    scopus 로고
    • Dynamic binding of histone H1 to chromatin in living cells
    • 10.1038/35048610, 11130729
    • Misteli T, Gunjan A, Hock R, Bustin M, Brown DT. Dynamic binding of histone H1 to chromatin in living cells. Nature 2000, 408:877-881. 10.1038/35048610, 11130729.
    • (2000) Nature , vol.408 , pp. 877-881
    • Misteli, T.1    Gunjan, A.2    Hock, R.3    Bustin, M.4    Brown, D.T.5
  • 4
    • 0033615555 scopus 로고    scopus 로고
    • Histone H1 and evolution of sperm nuclear basic proteins
    • 10.1074/jbc.274.44.31115, 10531297
    • Ausio J. Histone H1 and evolution of sperm nuclear basic proteins. J Biol Chem 1999, 274:31115-31118. 10.1074/jbc.274.44.31115, 10531297.
    • (1999) J Biol Chem , vol.274 , pp. 31115-31118
    • Ausio, J.1
  • 5
    • 0032564478 scopus 로고    scopus 로고
    • Nucleosomes, linker DNA, and Linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin
    • Bednar J, Horowitz AR, Grigoryev AS, Carruthers ML, Hansen CJ, Koster JA, Woodcock LC. Nucleosomes, linker DNA, and Linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin. Cell Biol 1998, 95:14173-14178.
    • (1998) Cell Biol , vol.95 , pp. 14173-14178
    • Bednar, J.1    Horowitz, A.R.2    Grigoryev, A.S.3    Carruthers, M.L.4    Hansen, C.J.5    Koster, J.A.6    Woodcock, L.C.7
  • 6
    • 0035883954 scopus 로고    scopus 로고
    • Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails
    • 10.1101/gad.927301, 11562345
    • Zhang Y, Reinberg D. Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. Genes Dev 2001, 15:2343-2360. 10.1101/gad.927301, 11562345.
    • (2001) Genes Dev , vol.15 , pp. 2343-2360
    • Zhang, Y.1    Reinberg, D.2
  • 7
    • 9544245803 scopus 로고    scopus 로고
    • Heterochromatin structure and function
    • 10.1016/j.biolcel.2004.06.003, 15519697
    • Dillon N. Heterochromatin structure and function. Biol Cell 2004, 96:631-637. 10.1016/j.biolcel.2004.06.003, 15519697.
    • (2004) Biol Cell , vol.96 , pp. 631-637
    • Dillon, N.1
  • 8
    • 34548664586 scopus 로고    scopus 로고
    • ISWI Regulates Higher-Order Chromatin Structure and Histone H1 Assembly In Vivo
    • 10.1371/journal.pbio.0050232, 1951781, 17760505
    • Corona DF, Siriaco G, Armstrong JA, Snarskaya N, McClymont SA, Scott MP, Tamkun JW. ISWI Regulates Higher-Order Chromatin Structure and Histone H1 Assembly In Vivo. PLoS Biol 2007, 5:e232. 10.1371/journal.pbio.0050232, 1951781, 17760505.
    • (2007) PLoS Biol , vol.5
    • Corona, D.F.1    Siriaco, G.2    Armstrong, J.A.3    Snarskaya, N.4    McClymont, S.A.5    Scott, M.P.6    Tamkun, J.W.7
  • 9
    • 17644391390 scopus 로고    scopus 로고
    • Linker histone variants control chromatin dynamics during early embrogenesis
    • 10.1073/pnas.0409824102, 556016, 15821029
    • Saeki H, Ohsumi K, Aihara H, Ito T, Hirose S, Ura K, Kaneda Y. Linker histone variants control chromatin dynamics during early embrogenesis. PNAS 2005, 102:5697-5702. 10.1073/pnas.0409824102, 556016, 15821029.
    • (2005) PNAS , vol.102 , pp. 5697-5702
    • Saeki, H.1    Ohsumi, K.2    Aihara, H.3    Ito, T.4    Hirose, S.5    Ura, K.6    Kaneda, Y.7
  • 10
    • 22544458450 scopus 로고    scopus 로고
    • Characterization of sequence variations in human histone H1.2 and H1.4 subtypes
    • 10.1111/j.1742-4658.2005.04793.x, 16008566
    • Sarg B, Green A, Soderkvist P, Helliger W, Rundquist L, Lindner HH. Characterization of sequence variations in human histone H1.2 and H1.4 subtypes. FEBS J 2005, 272:3673-3683. 10.1111/j.1742-4658.2005.04793.x, 16008566.
    • (2005) FEBS J , vol.272 , pp. 3673-3683
    • Sarg, B.1    Green, A.2    Soderkvist, P.3    Helliger, W.4    Rundquist, L.5    Lindner, H.H.6
  • 11
    • 0030590378 scopus 로고    scopus 로고
    • Cloning of the cDNA encoding a novel subtype of histone H1
    • 10.1016/0378-1119(96)00020-0, 8964515
    • Yamamoto T, Horikoshi M. Cloning of the cDNA encoding a novel subtype of histone H1. Gene 1996, 173:281-285. 10.1016/0378-1119(96)00020-0, 8964515.
    • (1996) Gene , vol.173 , pp. 281-285
    • Yamamoto, T.1    Horikoshi, M.2
  • 12
    • 0035854055 scopus 로고    scopus 로고
    • Histone H1 diversity: bridging regulatory signals to linker histone function
    • 10.1016/S0378-1119(01)00495-4, 11410360
    • Khochbin S. Histone H1 diversity: bridging regulatory signals to linker histone function. Gene 2001, 271:1-12. 10.1016/S0378-1119(01)00495-4, 11410360.
    • (2001) Gene , vol.271 , pp. 1-12
    • Khochbin, S.1
  • 13
    • 0035173870 scopus 로고    scopus 로고
    • Origin of H1 linker histones
    • 10.1096/fj.00-0237rev, 11149891
    • Kasinsky HE, Lewis JD, Dacks JB, Ausio J. Origin of H1 linker histones. FASEB J 2001, 15:34-42. 10.1096/fj.00-0237rev, 11149891.
    • (2001) FASEB J , vol.15 , pp. 34-42
    • Kasinsky, H.E.1    Lewis, J.D.2    Dacks, J.B.3    Ausio, J.4
  • 14
    • 0029119093 scopus 로고    scopus 로고
    • Histone H1.4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner
    • 195
    • O'Neill LP, Turner BM. Histone H1.4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner. EMBO J 14:3946-57. 195.
    • EMBO J , vol.14 , pp. 3946-3957
    • O'Neill, L.P.1    Turner, B.M.2
  • 15
    • 0030999604 scopus 로고    scopus 로고
    • Histone octamer function in vivo: mutations in the dimmer-tetramer interfaces disrupt bith gene activation and repression
    • 10.1093/emboj/16.9.2493, 1169849, 9171362
    • Santisteban MS, Arents G, Moudrianakis EN, Smith MM. Histone octamer function in vivo: mutations in the dimmer-tetramer interfaces disrupt bith gene activation and repression. EMBO J 1997, 16:2493-2506. 10.1093/emboj/16.9.2493, 1169849, 9171362.
    • (1997) EMBO J , vol.16 , pp. 2493-2506
    • Santisteban, M.S.1    Arents, G.2    Moudrianakis, E.N.3    Smith, M.M.4
  • 16
    • 33846488609 scopus 로고    scopus 로고
    • Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue
    • Wisniewski JR, Zougman A, Kruger S, Mann M. Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue. Mol Cell Proteomics 2007, 6:72-87.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 72-87
    • Wisniewski, J.R.1    Zougman, A.2    Kruger, S.3    Mann, M.4
  • 17
    • 29244467484 scopus 로고    scopus 로고
    • Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length
    • 10.1007/s10577-005-1024-3, 16506093
    • Woodcock CL, Skoultchi IA, Fan Y. Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length. Chromosome Res 2006, 14:17-25. 10.1007/s10577-005-1024-3, 16506093.
    • (2006) Chromosome Res , vol.14 , pp. 17-25
    • Woodcock, C.L.1    Skoultchi, I.A.2    Fan, Y.3
  • 18
    • 0030068951 scopus 로고    scopus 로고
    • In vivo phosphorylation of histone H1 variants during the cell cycle
    • 10.1021/bi951914e, 8639656
    • Talasz H, Helliger W, Puschendorf B, Lindener H. In vivo phosphorylation of histone H1 variants during the cell cycle. Biochemistry 1996, 35:1761-1767. 10.1021/bi951914e, 8639656.
    • (1996) Biochemistry , vol.35 , pp. 1761-1767
    • Talasz, H.1    Helliger, W.2    Puschendorf, B.3    Lindener, H.4
  • 19
    • 1842294564 scopus 로고    scopus 로고
    • A mouse histone H1 variant, H1b, binds preferetionally to a regulatory sequence within a mouse H3.2 replication-dependent histon gene
    • 10.1074/jbc.272.24.15120, 9182532
    • Kaludov NK, Pabon-Pena L, Seavy M, Robinson G, Hurt MM. A mouse histone H1 variant, H1b, binds preferetionally to a regulatory sequence within a mouse H3.2 replication-dependent histon gene. J Biol Chem 1997, 272:15120-15127. 10.1074/jbc.272.24.15120, 9182532.
    • (1997) J Biol Chem , vol.272 , pp. 15120-15127
    • Kaludov, N.K.1    Pabon-Pena, L.2    Seavy, M.3    Robinson, G.4    Hurt, M.M.5
  • 20
    • 33750682358 scopus 로고    scopus 로고
    • Beyond the walls of the nucleus: the role of histones in cellular signaling and innate immunity
    • 10.1139/o06-082, 16936831
    • Parseghian MH, Luhrs KA. Beyond the walls of the nucleus: the role of histones in cellular signaling and innate immunity. Biochem Cell Biol 2006, 84:589-604. 10.1139/o06-082, 16936831.
    • (2006) Biochem Cell Biol , vol.84 , pp. 589-604
    • Parseghian, M.H.1    Luhrs, K.A.2
  • 21
    • 0020961333 scopus 로고
    • Cyclin: a protein specified by maternal mRNA in sea urchin eggs that is destroyed at each cleavage division
    • 10.1016/0092-8674(83)90420-8, 6134587
    • Evans T, Rosenthal ET, Youngblom J, Distel D, Hunt T. Cyclin: a protein specified by maternal mRNA in sea urchin eggs that is destroyed at each cleavage division. Cell 1983, 33:389-396. 10.1016/0092-8674(83)90420-8, 6134587.
    • (1983) Cell , vol.33 , pp. 389-396
    • Evans, T.1    Rosenthal, E.T.2    Youngblom, J.3    Distel, D.4    Hunt, T.5
  • 22
    • 0842324788 scopus 로고    scopus 로고
    • Recycling the cell cycle: cyclins revisited
    • 10.1016/S0092-8674(03)01080-8, 14744433
    • Murray AM. Recycling the cell cycle: cyclins revisited. Cell 2004, 116:221-234. 10.1016/S0092-8674(03)01080-8, 14744433.
    • (2004) Cell , vol.116 , pp. 221-234
    • Murray, A.M.1
  • 24
    • 23944494616 scopus 로고    scopus 로고
    • The effect of carotenoids obtained from saffron on histone H1 structure and H1-DNA interaction
    • Ashrafi M, Bathaie SZ, Taqhikhani M, Moosavi-Movahedi AA. The effect of carotenoids obtained from saffron on histone H1 structure and H1-DNA interaction. Int J Biol Macromol 2005, 36:246-252.
    • (2005) Int J Biol Macromol , vol.36 , pp. 246-252
    • Ashrafi, M.1    Bathaie, S.Z.2    Taqhikhani, M.3    Moosavi-Movahedi, A.A.4
  • 25
    • 0242721659 scopus 로고    scopus 로고
    • The dynamic mobility of histone H1 is regulated by cyclin/CDK phosphorylation
    • 10.1128/MCB.23.23.8626-8636.2003, 262667, 14612406
    • Contreras A, Hale TK, Stenoien DL, Rosen JM, Mancini MA, Herrera RE. The dynamic mobility of histone H1 is regulated by cyclin/CDK phosphorylation. Mol Cell Biol 2003, 23:8626-8636. 10.1128/MCB.23.23.8626-8636.2003, 262667, 14612406.
    • (2003) Mol Cell Biol , vol.23 , pp. 8626-8636
    • Contreras, A.1    Hale, T.K.2    Stenoien, D.L.3    Rosen, J.M.4    Mancini, M.A.5    Herrera, R.E.6
  • 26
    • 0029953320 scopus 로고    scopus 로고
    • Evidence that the endogenous histone H1 phosphatase in HeLa mitotic chromosomes is protein phosphatase 1, not protein phosphatase 2A
    • Paulson JR, Patzlaff JS, Vallis AJ. Evidence that the endogenous histone H1 phosphatase in HeLa mitotic chromosomes is protein phosphatase 1, not protein phosphatase 2A. J Cell Sci 1996, 109:1437-1447.
    • (1996) J Cell Sci , vol.109 , pp. 1437-1447
    • Paulson, J.R.1    Patzlaff, J.S.2    Vallis, A.J.3
  • 27
    • 9244238763 scopus 로고    scopus 로고
    • Identification of the linker histone H1 as a protein kinase Cepsilon-binding protein in vascular smooth muscle
    • 10.1139/o04-053, 15499382
    • Zhao M, Sutherland C, Wilson DP, Deng J, Macdonald JA, Walsh MP. Identification of the linker histone H1 as a protein kinase Cepsilon-binding protein in vascular smooth muscle. Biochem Cell Biol 2004, 82:538-546. 10.1139/o04-053, 15499382.
    • (2004) Biochem Cell Biol , vol.82 , pp. 538-546
    • Zhao, M.1    Sutherland, C.2    Wilson, D.P.3    Deng, J.4    Macdonald, J.A.5    Walsh, M.P.6
  • 28
    • 0033637116 scopus 로고    scopus 로고
    • Phosphorylation of linker histone H1 regulates gene expression in vivo by creating a charge patch
    • 10.1016/S1097-2765(00)00024-1, 10983971
    • Dou Y, Gorovsly MA. Phosphorylation of linker histone H1 regulates gene expression in vivo by creating a charge patch. Mol Cell 2000, 6:225-231. 10.1016/S1097-2765(00)00024-1, 10983971.
    • (2000) Mol Cell , vol.6 , pp. 225-231
    • Dou, Y.1    Gorovsly, M.A.2
  • 30
    • 0029120154 scopus 로고
    • Increased phosphorylation of histone H1 in mouse fibroblasts transformed with oncogenes or constitutively active mitogen-activated protein kinase kinase
    • 10.1074/jbc.270.34.20098, 7650028
    • Chadee DN, Taylor WR, Hurta RA, Allis CD, Wright JA, Davie JR. Increased phosphorylation of histone H1 in mouse fibroblasts transformed with oncogenes or constitutively active mitogen-activated protein kinase kinase. J Biol Chem 1995, 270:20098-20105. 10.1074/jbc.270.34.20098, 7650028.
    • (1995) J Biol Chem , vol.270 , pp. 20098-20105
    • Chadee, D.N.1    Taylor, W.R.2    Hurta, R.A.3    Allis, C.D.4    Wright, J.A.5    Davie, J.R.6
  • 31
    • 0034816237 scopus 로고    scopus 로고
    • Identification of a nuclear variant of MGEA5, a cytoplasmic hyaluronidase and a beta-N-acetylglucosaminidase
    • Comtesse N, Maldner E, Meese E. Identification of a nuclear variant of MGEA5, a cytoplasmic hyaluronidase and a beta-N-acetylglucosaminidase. Biochem Biophysc Res Commun 2001, 283:634-640.
    • (2001) Biochem Biophysc Res Commun , vol.283 , pp. 634-640
    • Comtesse, N.1    Maldner, E.2    Meese, E.3
  • 32
    • 0027289130 scopus 로고
    • RNA polymerase II is a glycoprotein. Modification of the COOH-terminal domain by O-GlcNAc
    • Kelly WG, Dahmus ME, Hart GW. RNA polymerase II is a glycoprotein. Modification of the COOH-terminal domain by O-GlcNAc. J Biol Chem 1993, 268:10416-10424.
    • (1993) J Biol Chem , vol.268 , pp. 10416-10424
    • Kelly, W.G.1    Dahmus, M.E.2    Hart, G.W.3
  • 33
    • 0034718570 scopus 로고    scopus 로고
    • Alternative O-glycosylation/O-phosphorylation of the murine estrogen receptor beta
    • 10.1021/bi000755i, 10995228
    • Cheng X, Cole RN, Zaia J, Hart GW. Alternative O-glycosylation/O-phosphorylation of the murine estrogen receptor beta. Biochemistry 2000, 39:11609-11620. 10.1021/bi000755i, 10995228.
    • (2000) Biochemistry , vol.39 , pp. 11609-11620
    • Cheng, X.1    Cole, R.N.2    Zaia, J.3    Hart, G.W.4
  • 34
    • 0029049198 scopus 로고
    • C-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas
    • 10.1074/jbc.270.32.18961, 7642555
    • Chou TY, Hart GW, Dang CV. c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas. J Biol Chem 1995, 270:18961-18965. 10.1074/jbc.270.32.18961, 7642555.
    • (1995) J Biol Chem , vol.270 , pp. 18961-18965
    • Chou, T.Y.1    Hart, G.W.2    Dang, C.V.3
  • 35
    • 0842347416 scopus 로고    scopus 로고
    • Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability
    • 10.1128/MCB.24.4.1680-1690.2004, 344186, 14749383
    • O'Donnell N, Zachara NE, Hart GW, Marth JD. Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability. Mol Cell Biol 2004, 24:1680-1690. 10.1128/MCB.24.4.1680-1690.2004, 344186, 14749383.
    • (2004) Mol Cell Biol , vol.24 , pp. 1680-1690
    • O'Donnell, N.1    Zachara, N.E.2    Hart, G.W.3    Marth, J.D.4
  • 36
    • 0034705030 scopus 로고    scopus 로고
    • The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny
    • 10.1073/pnas.100471497, 18502, 10801981
    • Shafi R, Iyer SPN, Ellies LG, O'Donnell N, Marek KW, Chui D, Hart GW, Marth JD. The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny. Proc Natl Acad Sci USA 2000, 97:5735-5739. 10.1073/pnas.100471497, 18502, 10801981.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5735-5739
    • Shafi, R.1    Iyer, S.P.N.2    Ellies, L.G.3    O'Donnell, N.4    Marek, K.W.5    Chui, D.6    Hart, G.W.7    Marth, J.D.8
  • 38
    • 0035864384 scopus 로고    scopus 로고
    • Use of galactosyltansferase to assess the biological function of O-linked N-acetyl-d-glucosamine: a potential role for O-GlcNAc during cell division
    • Fang B, Miller MW. Use of galactosyltansferase to assess the biological function of O-linked N-acetyl-d-glucosamine: a potential role for O-GlcNAc during cell division. Exp Cell Res 2000, 263:243-253.
    • (2000) Exp Cell Res , vol.263 , pp. 243-253
    • Fang, B.1    Miller, M.W.2
  • 39
    • 0028085881 scopus 로고
    • Purification and characterization of an O-GlcNAc selective N-acetyl-beta_D-glucosaminidase from rat spleen cytosol
    • Dong DLY, Hart GW. Purification and characterization of an O-GlcNAc selective N-acetyl-beta_D-glucosaminidase from rat spleen cytosol. J Biol Chem 1994, 269:19321-19330.
    • (1994) J Biol Chem , vol.269 , pp. 19321-19330
    • Dong, D.L.Y.1    Hart, G.W.2
  • 40
    • 0032488979 scopus 로고    scopus 로고
    • Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O = GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene) amino-N-phenycarbamate
    • 10.1074/jbc.273.6.3611, 9452489
    • Haltiwanger RS, Grove K, Philipsberg GA. Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O = GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene) amino-N-phenycarbamate. J Biol Chem 1998, 273:3611-3617. 10.1074/jbc.273.6.3611, 9452489.
    • (1998) J Biol Chem , vol.273 , pp. 3611-3617
    • Haltiwanger, R.S.1    Grove, K.2    Philipsberg, G.A.3
  • 41
    • 0346688092 scopus 로고
    • Possible glycosylation of H1 histone in Murine liver nucleus
    • Kim TH, Park JY, Lee SH, Chang HI. Possible glycosylation of H1 histone in Murine liver nucleus. Korean Biochem J 1994, 27:240-244.
    • (1994) Korean Biochem J , vol.27 , pp. 240-244
    • Kim, T.H.1    Park, J.Y.2    Lee, S.H.3    Chang, H.I.4
  • 42
    • 25444501339 scopus 로고    scopus 로고
    • Perturbations in O-linked β-N-Acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis
    • 10.1074/jbc.M503396200, 16027160
    • Salwson C, Zachara NE, Vosseller K, Cheung WD, Lane MD, Hart GE. Perturbations in O-linked β-N-Acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis. J Biol Chem 2005, 280:32944-32956. 10.1074/jbc.M503396200, 16027160.
    • (2005) J Biol Chem , vol.280 , pp. 32944-32956
    • Salwson, C.1    Zachara, N.E.2    Vosseller, K.3    Cheung, W.D.4    Lane, M.D.5    Hart, G.E.6
  • 43
    • 39049111685 scopus 로고    scopus 로고
    • Immediate-early gene regulation by interplay between different post-translational modifications on human histone H3
    • 10.1002/jcb.21454, 17668447
    • Kaleem A, Hoessli DC, Ahmad I, Walker-Nasir E, Nasim A, Shakoori AR, Nasir-ud-Din. Immediate-early gene regulation by interplay between different post-translational modifications on human histone H3. J Cell Biochem 2008, 103:835-851. 10.1002/jcb.21454, 17668447.
    • (2008) J Cell Biochem , vol.103 , pp. 835-851
    • Kaleem, A.1    Hoessli, D.C.2    Ahmad, I.3    Walker-Nasir, E.4    Nasim, A.5    Shakoori, A.R.6    Nasir-ud-Din7
  • 44
    • 0037166352 scopus 로고    scopus 로고
    • Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: alternative glycosylation/phosphorylation of THR-58, a known mutational hot spot of c-Myc in lymphomas, is regulated by mitogens
    • 10.1074/jbc.M201729200, 11904304
    • Kamemura K, Hayes BK, Comer FI, Hart GW. Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: alternative glycosylation/phosphorylation of THR-58, a known mutational hot spot of c-Myc in lymphomas, is regulated by mitogens. J Biol Chem 2002, 277:19229-19235. 10.1074/jbc.M201729200, 11904304.
    • (2002) J Biol Chem , vol.277 , pp. 19229-19235
    • Kamemura, K.1    Hayes, B.K.2    Comer, F.I.3    Hart, G.W.4
  • 45
    • 0036462599 scopus 로고    scopus 로고
    • The emerging significance of O-GlcNAc in cellular regulation
    • 10.1021/cr000406u, 11841249
    • Zachara NE, Hart GW. The emerging significance of O-GlcNAc in cellular regulation. Chem Rev 2002, 102:431-438. 10.1021/cr000406u, 11841249.
    • (2002) Chem Rev , vol.102 , pp. 431-438
    • Zachara, N.E.1    Hart, G.W.2
  • 46
    • 78049390185 scopus 로고    scopus 로고
    • O-GlcNAc transferase regulates mitotic chromatin dynamics
    • 10.1074/jbc.M110.158170, 20805223
    • Sakabe K, Hart GW. O-GlcNAc transferase regulates mitotic chromatin dynamics. J Biol Chem 2010, 285:34460-34468. 10.1074/jbc.M110.158170, 20805223.
    • (2010) J Biol Chem , vol.285 , pp. 34460-34468
    • Sakabe, K.1    Hart, G.W.2
  • 47
    • 78650447665 scopus 로고    scopus 로고
    • β-N-acetylglucosamine (O-GlcNAc) is part of the histone code
    • 10.1073/pnas.1009023107, 2993388, 21045127
    • Sakabe K, Wang Z, Hart GW. β-N-acetylglucosamine (O-GlcNAc) is part of the histone code. Proc Natl Acad Sci USA 2010, 107:19915-19920. 10.1073/pnas.1009023107, 2993388, 21045127.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 19915-19920
    • Sakabe, K.1    Wang, Z.2    Hart, G.W.3
  • 49
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • 10.1093/nar/25.17.3389, 146917, 9254694
    • AltschuL SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 1997, 25:3389-3402. 10.1093/nar/25.17.3389, 146917, 9254694.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • AltschuL, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 50
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • 10.1093/nar/22.22.4673, 308517, 7984417
    • Thompson JD, Higgins DJ, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994, 22:4673-46780. 10.1093/nar/22.22.4673, 308517, 7984417.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-46780
    • Thompson, J.D.1    Higgins, D.J.2    Gibson, T.J.3
  • 51
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
    • 10.1006/jmbi.1999.3310, 10600390
    • Blom N, Gammeltoft S, Brunk S. Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 1999, 294:1351-1362. 10.1006/jmbi.1999.3310, 10600390.
    • (1999) J Mol Biol , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunk, S.3
  • 52
    • 2942564430 scopus 로고    scopus 로고
    • Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence
    • 10.1002/pmic.200300771, 15174133
    • Blom N, Sicheritz-Ponten T, Gupta R, Gammeltoft S, Brunk S. Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics 2004, 4:1633-1649. 10.1002/pmic.200300771, 15174133.
    • (2004) Proteomics , vol.4 , pp. 1633-1649
    • Blom, N.1    Sicheritz-Ponten, T.2    Gupta, R.3    Gammeltoft, S.4    Brunk, S.5
  • 54
    • 31644448586 scopus 로고    scopus 로고
    • Oct-2 DNA binding transcription factor: functional consequences of phosphorylation and glycosylation
    • 10.1093/nar/gkj401, 1326018, 16431844
    • Ahmad I, Hoessli DC, Walker-Nasir E, Rafik SM, Shakoori AR, Nasir-ud-Din. Oct-2 DNA binding transcription factor: functional consequences of phosphorylation and glycosylation. Nucleic Acids Res 2006, 34:175-184. 10.1093/nar/gkj401, 1326018, 16431844.
    • (2006) Nucleic Acids Res , vol.34 , pp. 175-184
    • Ahmad, I.1    Hoessli, D.C.2    Walker-Nasir, E.3    Rafik, S.M.4    Shakoori, A.R.5    Nasir-ud-Din6
  • 55
  • 56
    • 40449107851 scopus 로고    scopus 로고
    • In silico modulation of HMGN-1 binding to histones and gene expression by interplay of phosphorylation and O-GlcNAc modification
    • Ahmad I, Khan TS, Hoessli DC, Walker-Nasir E, Kaleem A, Shakoori AR, Nasir-ud-Din. In silico modulation of HMGN-1 binding to histones and gene expression by interplay of phosphorylation and O-GlcNAc modification. Protein Pept Lett 2008, 15:193-199.
    • (2008) Protein Pept Lett , vol.15 , pp. 193-199
    • Ahmad, I.1    Khan, T.S.2    Hoessli, D.C.3    Walker-Nasir, E.4    Kaleem, A.5    Shakoori, A.R.6    Nasir-ud-Din7
  • 57
    • 0003396310 scopus 로고    scopus 로고
    • Bioinformatics: The machine learning Approach
    • Cambridge, MA, 2
    • Baldi P, Brunak S. Bioinformatics: The machine learning Approach. MIT Press 2002, Cambridge, MA, 2.
    • (2002) MIT Press
    • Baldi, P.1    Brunak, S.2
  • 59
    • 0021759125 scopus 로고
    • Differences in evolutionary stability among mammalian H1 subtypes. Implications for the roles of H1 subtypes in chromatin
    • Lennox RW. Differences in evolutionary stability among mammalian H1 subtypes. Implications for the roles of H1 subtypes in chromatin. J Biol Chem 1984, 259:669-672.
    • (1984) J Biol Chem , vol.259 , pp. 669-672
    • Lennox, R.W.1
  • 60
    • 0028052069 scopus 로고
    • Developmentally regulated expression of linker-histone variants in vertebrates
    • 10.1111/j.1432-1033.1994.00501.x, 7957165
    • Khochbin S, Wolffe AP. Developmentally regulated expression of linker-histone variants in vertebrates. Eur J Biochem 1994, 225:501-510. 10.1111/j.1432-1033.1994.00501.x, 7957165.
    • (1994) Eur J Biochem , vol.225 , pp. 501-510
    • Khochbin, S.1    Wolffe, A.P.2
  • 61
    • 0027074659 scopus 로고
    • Alteration in proportions of histone H1 variants during the differentiation of murine erythroleukaemic cells
    • 1131949, 1471988
    • Helliger W, Lindner H, Grubl-Knosp O, Puschendorf B. Alteration in proportions of histone H1 variants during the differentiation of murine erythroleukaemic cells. Biochem J 1992, 288:747-51. 1131949, 1471988.
    • (1992) Biochem J , vol.288 , pp. 747-751
    • Helliger, W.1    Lindner, H.2    Grubl-Knosp, O.3    Puschendorf, B.4
  • 62
    • 0031574027 scopus 로고    scopus 로고
    • Differential effect of H1 variant overproduction on gene expression is due to differences in the central globular domain
    • 10.1093/nar/25.24.5003, 147167, 9396808
    • Brown DT, Gunjan A, Alexander BT, Sittman DB. Differential effect of H1 variant overproduction on gene expression is due to differences in the central globular domain. Nucleic Acids Res 1997, 25:5003-5009. 10.1093/nar/25.24.5003, 147167, 9396808.
    • (1997) Nucleic Acids Res , vol.25 , pp. 5003-5009
    • Brown, D.T.1    Gunjan, A.2    Alexander, B.T.3    Sittman, D.B.4
  • 63
    • 0037129959 scopus 로고    scopus 로고
    • Identification of a 34 amino acid stretch within the C-terminus of histone H1 as the DNA-condensing domain by site-directed mutagenesis
    • 10.1021/bi025773+, 12056893
    • Bharath MM, Ramesh S, Chandra NR, Rao MR. Identification of a 34 amino acid stretch within the C-terminus of histone H1 as the DNA-condensing domain by site-directed mutagenesis. Biochemistry 2002, 41:7617-7627. 10.1021/bi025773+, 12056893.
    • (2002) Biochemistry , vol.41 , pp. 7617-7627
    • Bharath, M.M.1    Ramesh, S.2    Chandra, N.R.3    Rao, M.R.4
  • 64
    • 53149096921 scopus 로고    scopus 로고
    • Mouse Dnmt3a Preferentially Methylates Linker DNA and Is Inhibited by Histone H1
    • 10.1016/j.jmb.2008.03.001, 18823905
    • Takeshima H, Suetake I, Tajima S. Mouse Dnmt3a Preferentially Methylates Linker DNA and Is Inhibited by Histone H1. J Mol Biol 2008, 383:810-821. 10.1016/j.jmb.2008.03.001, 18823905.
    • (2008) J Mol Biol , vol.383 , pp. 810-821
    • Takeshima, H.1    Suetake, I.2    Tajima, S.3
  • 66
    • 0031046649 scopus 로고    scopus 로고
    • Condensation of DNA and chromatin by an SPKK-containing octapeptide repeat motif present in the C-terminus of histone H1
    • 10.1021/bi961617p, 9033394
    • Khadake JR, Rao MR. Condensation of DNA and chromatin by an SPKK-containing octapeptide repeat motif present in the C-terminus of histone H1. Biochemistry 1997, 36:1041-1051. 10.1021/bi961617p, 9033394.
    • (1997) Biochemistry , vol.36 , pp. 1041-1051
    • Khadake, J.R.1    Rao, M.R.2
  • 67
    • 33645281420 scopus 로고    scopus 로고
    • The long and the short of it: linker histone H1 is required for metaphase chromosome compaction
    • 10.4161/cc.5.6.2581, 16582611
    • Maresca TJ, Heald R. The long and the short of it: linker histone H1 is required for metaphase chromosome compaction. Cell Cycle 2006, 5:589-591. 10.4161/cc.5.6.2581, 16582611.
    • (2006) Cell Cycle , vol.5 , pp. 589-591
    • Maresca, T.J.1    Heald, R.2
  • 68
    • 29244449333 scopus 로고    scopus 로고
    • Histone H1 depletion in mammals alters global chromatin structure but causes specific changes in gene regulation
    • 10.1016/j.cell.2005.10.028, 16377562
    • Fan Y, Nikitina T, Zhao J, Fleury TJ, Bhattacharyya R, Bouhassira EE, Stein A, Woodcock CL, Skoultchi AI. Histone H1 depletion in mammals alters global chromatin structure but causes specific changes in gene regulation. Cell 2005, 123:1199-1212. 10.1016/j.cell.2005.10.028, 16377562.
    • (2005) Cell , vol.123 , pp. 1199-1212
    • Fan, Y.1    Nikitina, T.2    Zhao, J.3    Fleury, T.J.4    Bhattacharyya, R.5    Bouhassira, E.E.6    Stein, A.7    Woodcock, C.L.8    Skoultchi, A.I.9
  • 69
    • 0027082560 scopus 로고
    • Histone H1 and transcription: still an enigma?
    • 1992
    • Zlatanova J, van Holde K. Histone H1 and transcription: still an enigma?. J Cell Sci 1992, 103:889-895. 1992.
    • (1992) J Cell Sci , vol.103 , pp. 889-895
    • Zlatanova, J.1    van Holde, K.2
  • 70
    • 0031104747 scopus 로고    scopus 로고
    • What do linker histone do in chromatin?
    • 10.1002/bies.950190311, 9080775
    • Wolffe AP, Khochbin S, Dimitrov S. What do linker histone do in chromatin?. Bioessays 1997, 19:249-255. 10.1002/bies.950190311, 9080775.
    • (1997) Bioessays , vol.19 , pp. 249-255
    • Wolffe, A.P.1    Khochbin, S.2    Dimitrov, S.3
  • 71
    • 0033610814 scopus 로고    scopus 로고
    • In vitro binding of H1 histone subtypes to nucleosomal organized mouse mammary tumor virus long terminal repeat promotor
    • 10.1074/jbc.273.48.32236, 9822702
    • Talasz H, Sapojnikova N, Helliger W, Lindner H, Puschendorf B. In vitro binding of H1 histone subtypes to nucleosomal organized mouse mammary tumor virus long terminal repeat promotor. J Biol Chem 1998, 273:32236-32243. 10.1074/jbc.273.48.32236, 9822702.
    • (1998) J Biol Chem , vol.273 , pp. 32236-32243
    • Talasz, H.1    Sapojnikova, N.2    Helliger, W.3    Lindner, H.4    Puschendorf, B.5
  • 72
    • 0025764058 scopus 로고
    • Histone-DNA interactions and their modulation by phosphorylation of -Ser-Pro-X-Lys/Arg- motifs
    • 452869, 2050127
    • Hill CS, Rimmer JM, Green BN, Finch JT, Thomas JO. Histone-DNA interactions and their modulation by phosphorylation of -Ser-Pro-X-Lys/Arg- motifs. EMBO J 1991, 10:1939-1948. 452869, 2050127.
    • (1991) EMBO J , vol.10 , pp. 1939-1948
    • Hill, C.S.1    Rimmer, J.M.2    Green, B.N.3    Finch, J.T.4    Thomas, J.O.5
  • 73
    • 33744548700 scopus 로고    scopus 로고
    • Phosphorylation of the linker histone H1 by CDK regulates its binding to HP1alpha
    • 10.1016/j.molcel.2006.04.016, 16762841
    • Hale TK, Contreras A, Morrison AJ, Herrera RE. Phosphorylation of the linker histone H1 by CDK regulates its binding to HP1alpha. Mol Cell 2006, 22:693-699. 10.1016/j.molcel.2006.04.016, 16762841.
    • (2006) Mol Cell , vol.22 , pp. 693-699
    • Hale, T.K.1    Contreras, A.2    Morrison, A.J.3    Herrera, R.E.4
  • 74
    • 0026545414 scopus 로고
    • Chromatin condensation: does histone H1 dephosphorylation play a role?
    • Roth SY, Allis CD. Chromatin condensation: does histone H1 dephosphorylation play a role?. Trends Biochem Sci 1992, 17:8-93.
    • (1992) Trends Biochem Sci , vol.17 , pp. 8-93
    • Roth, S.Y.1    Allis, C.D.2
  • 75
    • 0034665758 scopus 로고    scopus 로고
    • Where the cell cycle and histone meet
    • 10.1101/gad.842100, 10995383
    • Ewen ME. Where the cell cycle and histone meet. Genes Dev 2000, 14:2265-2270. 10.1101/gad.842100, 10995383.
    • (2000) Genes Dev , vol.14 , pp. 2265-2270
    • Ewen, M.E.1
  • 76
    • 33646569673 scopus 로고    scopus 로고
    • Histone H1 phosphorylation occurs site-specifically during interphase and mitosis: identification of a novel phosphorylation site on histone H1
    • Sarg B, Helliger W, Talasz H, Forg B, Lindner HH. Histone H1 phosphorylation occurs site-specifically during interphase and mitosis: identification of a novel phosphorylation site on histone H1. J Biol Chem 2005, 281:6573-6580.
    • (2005) J Biol Chem , vol.281 , pp. 6573-6580
    • Sarg, B.1    Helliger, W.2    Talasz, H.3    Forg, B.4    Lindner, H.H.5
  • 77
    • 0031866460 scopus 로고    scopus 로고
    • Evolution of the vertebrate H1 histone class: evidence for the functional differentiation of the subtypes
    • Ponte I, Vidal-Taboada JM, Suau P. Evolution of the vertebrate H1 histone class: evidence for the functional differentiation of the subtypes. Mol Biol Evol 1998, 15:702-708.
    • (1998) Mol Biol Evol , vol.15 , pp. 702-708
    • Ponte, I.1    Vidal-Taboada, J.M.2    Suau, P.3
  • 78
    • 23044489675 scopus 로고    scopus 로고
    • H1 family histones in the nucleus. Control of binding and localization by the C-terminal domain
    • 10.1074/jbc.M501627200, 15911621
    • Th'ng JP, Sung R, Ye M, Hendzel MJ. H1 family histones in the nucleus. Control of binding and localization by the C-terminal domain. J Biol Chem 2005, 280:27809-27814. 10.1074/jbc.M501627200, 15911621.
    • (2005) J Biol Chem , vol.280 , pp. 27809-27814
    • Th'ng, J.P.1    Sung, R.2    Ye, M.3    Hendzel, M.J.4
  • 79
    • 2442574861 scopus 로고    scopus 로고
    • The C-terminal domain of histone H1 binding to chromatin in vivo.
    • 10.1074/jbc.M400070200, 14985337
    • Hendzel MJ, Lever MA, Crawford E, Th'ng JP. The C-terminal domain of histone H1 binding to chromatin in vivo. J Biol Chem 2004, 279:20028-20034. 10.1074/jbc.M400070200, 14985337.
    • (2004) J Biol Chem , vol.279 , pp. 20028-20034
    • Hendzel, M.J.1    Lever, M.A.2    Crawford, E.3    Th'ng, J.P.4
  • 80
    • 0028820336 scopus 로고
    • Characterization of the mitotic specific phosphorylation site of histone H1. Absence of a consensus sequence for the p34cdc2/cyclin B kinase
    • 10.1074/jbc.270.46.27653, 7499230
    • Gurley LR, Valdez JG, Buchanan JS. Characterization of the mitotic specific phosphorylation site of histone H1. Absence of a consensus sequence for the p34cdc2/cyclin B kinase. J Biol Chem 1995, 270:27653-27660. 10.1074/jbc.270.46.27653, 7499230.
    • (1995) J Biol Chem , vol.270 , pp. 27653-27660
    • Gurley, L.R.1    Valdez, J.G.2    Buchanan, J.S.3
  • 81
    • 42249098495 scopus 로고    scopus 로고
    • Histone tail modifications and noncanonical functions of histones: perspectives in cancer epigenetics
    • Hadnagy A, Beaulieu R, Balicki D. Histone tail modifications and noncanonical functions of histones: perspectives in cancer epigenetics. Mol Cancer Ther 2008, 7:740-748.
    • (2008) Mol Cancer Ther , vol.7 , pp. 740-748
    • Hadnagy, A.1    Beaulieu, R.2    Balicki, D.3
  • 82
    • 0037197991 scopus 로고    scopus 로고
    • Regulation of transcription by H1 phosphorylation in Tetrahymena is position independent and requires clustered sites
    • 10.1073/pnas.092029599, 122916, 11972045
    • Dou Y, Gorovsky MA. Regulation of transcription by H1 phosphorylation in Tetrahymena is position independent and requires clustered sites. Proc Natl Acad Sci USA 2002, 99:6142-6146. 10.1073/pnas.092029599, 122916, 11972045.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6142-6146
    • Dou, Y.1    Gorovsky, M.A.2
  • 83
    • 33750456519 scopus 로고    scopus 로고
    • Global in vivo, and site specific phosphorylation dynamics in singling networks
    • 10.1016/j.cell.2006.09.026, 17081983
    • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Manm M. Global in vivo, and site specific phosphorylation dynamics in singling networks. Cell 2006, 127:635-648. 10.1016/j.cell.2006.09.026, 17081983.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Manm, M.7
  • 86
    • 25444501339 scopus 로고    scopus 로고
    • Perturbations in O-linked β-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis
    • 10.1074/jbc.M503396200, 16027160
    • Slawson C, Zachara NE, Vosseller K, Cheung WD, Lane MD, Hart GW. Perturbations in O-linked β-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis. J Biol Chem 2005, 280:32944-32956. 10.1074/jbc.M503396200, 16027160.
    • (2005) J Biol Chem , vol.280 , pp. 32944-32956
    • Slawson, C.1    Zachara, N.E.2    Vosseller, K.3    Cheung, W.D.4    Lane, M.D.5    Hart, G.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.