메뉴 건너뛰기




Volumn 6, Issue 4, 2011, Pages

The telomere binding protein trf2 induces chromatin compaction

Author keywords

[No Author keywords available]

Indexed keywords

AMINO TERMINAL TELOPEPTIDE; CARBOXY TERMINAL TELOPEPTIDE; HISTONE; SINGLE STRANDED DNA; TELOMERIC REPEAT BINDING FACTOR 2; DNA; MUTANT PROTEIN;

EID: 79955402377     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019124     Document Type: Article
Times cited : (27)

References (76)
  • 1
    • 77951976102 scopus 로고    scopus 로고
    • Higher-order chromatin structure in DSB induction, repair and misrepair
    • Falk M, Lukasova E, Kozubek S, (2010) Higher-order chromatin structure in DSB induction, repair and misrepair. Mutat Res 704: 88-100.
    • (2010) Mutat Res , vol.704 , pp. 88-100
    • Falk, M.1    Lukasova, E.2    Kozubek, S.3
  • 2
    • 0036089388 scopus 로고    scopus 로고
    • Conformational dynamics of the chromatin fiber in solution: determinants, mechanisms, and functions
    • Hansen JC, (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
    • 0037072601 scopus 로고    scopus 로고
    • Molecular biology. Chromatin higher order folding-wrapping up transcription
    • Horn PJ, Peterson CL, (2002) Molecular biology. Chromatin higher order folding-wrapping up transcription. Science 297: 1824-1827.
    • (2002) Science , vol.297 , pp. 1824-1827
    • Horn, P.J.1    Peterson, C.L.2
  • 4
    • 17044365726 scopus 로고    scopus 로고
    • Nucleosome and chromatin fiber dynamics
    • Luger K, Hansen JC, (2005) Nucleosome and chromatin fiber dynamics. Curr Opin Struct Biol 15: 188-196.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 188-196
    • Luger, K.1    Hansen, J.C.2
  • 5
    • 33750690705 scopus 로고    scopus 로고
    • In vitro chromatin self-association and its relevance to genome architecture
    • Lu X, Klonoski JM, Resch MG, Hansen JC, (2006) In vitro chromatin self-association and its relevance to genome architecture. Biochem Cell Biol 84: 411-417.
    • (2006) Biochem Cell Biol , vol.84 , pp. 411-417
    • Lu, X.1    Klonoski, J.M.2    Resch, M.G.3    Hansen, J.C.4
  • 7
    • 62849083222 scopus 로고    scopus 로고
    • The emerging role of nuclear architecture in DNA repair and genome maintenance
    • Misteli T, Soutoglou E, (2009) The emerging role of nuclear architecture in DNA repair and genome maintenance. Nat Rev Mol Cell Biol 10: 243-254.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 243-254
    • Misteli, T.1    Soutoglou, E.2
  • 8
    • 24944460598 scopus 로고    scopus 로고
    • Shelterin: the protein complex that shapes and safeguards human telomeres
    • de Lange T, (2005) Shelterin: the protein complex that shapes and safeguards human telomeres. Genes Dev 19: 2100-2110.
    • (2005) Genes Dev , vol.19 , pp. 2100-2110
    • de Lange, T.1
  • 10
    • 0027212790 scopus 로고
    • Nucleosomal organization of telomere-specific chromatin in rat
    • Makarov VL, Lejnine S, Bedoyan J, Langmore JP, (1993) Nucleosomal organization of telomere-specific chromatin in rat. Cell 73: 775-787.
    • (1993) Cell , vol.73 , pp. 775-787
    • Makarov, V.L.1    Lejnine, S.2    Bedoyan, J.3    Langmore, J.P.4
  • 11
    • 0028928198 scopus 로고
    • Conserved nucleoprotein structure at the ends of vertebrate and invertebrate chromosomes
    • Lejnine S, Makarov VL, Langmore JP, (1995) Conserved nucleoprotein structure at the ends of vertebrate and invertebrate chromosomes. Proc Natl Acad Sci U S A 92: 2393-2397.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 2393-2397
    • Lejnine, S.1    Makarov, V.L.2    Langmore, J.P.3
  • 12
    • 51349167747 scopus 로고    scopus 로고
    • No overt nucleosome eviction at deprotected telomeres
    • Wu P, de Lange T, (2008) No overt nucleosome eviction at deprotected telomeres. Mol Cell Biol 28: 5724-5735.
    • (2008) Mol Cell Biol , vol.28 , pp. 5724-5735
    • Wu, P.1    de Lange, T.2
  • 13
    • 58149085861 scopus 로고    scopus 로고
    • Purification of proteins associated with specific genomic Loci
    • Dejardin J, Kingston RE, (2009) Purification of proteins associated with specific genomic Loci. Cell 136: 175-186.
    • (2009) Cell , vol.136 , pp. 175-186
    • Dejardin, J.1    Kingston, R.E.2
  • 15
    • 27944496124 scopus 로고    scopus 로고
    • Functional human telomeres are recognized as DNA damage in G2 of the cell cycle
    • Verdun RE, Crabbe L, Haggblom C, Karlseder J, (2005) Functional human telomeres are recognized as DNA damage in G2 of the cell cycle. Mol Cell 20: 551-561.
    • (2005) Mol Cell , vol.20 , pp. 551-561
    • Verdun, R.E.1    Crabbe, L.2    Haggblom, C.3    Karlseder, J.4
  • 16
    • 33750801681 scopus 로고    scopus 로고
    • The DNA damage machinery and homologous recombination pathway act consecutively to protect human telomeres
    • Verdun RE, Karlseder J, (2006) The DNA damage machinery and homologous recombination pathway act consecutively to protect human telomeres. Cell 127: 709-720.
    • (2006) Cell , vol.127 , pp. 709-720
    • Verdun, R.E.1    Karlseder, J.2
  • 17
    • 0032489012 scopus 로고    scopus 로고
    • TRF2 protects human telomeres from end-to-end fusions
    • van Steensel B, Smogorzewska A, de Lange T, (1998) TRF2 protects human telomeres from end-to-end fusions. Cell 92: 401-413.
    • (1998) Cell , vol.92 , pp. 401-413
    • van Steensel, B.1    Smogorzewska, A.2    de Lange, T.3
  • 18
    • 0033605145 scopus 로고    scopus 로고
    • p53- and ATM-dependent apoptosis induced by telomeres lacking TRF2
    • Karlseder J, Broccoli D, Dai Y, Hardy S, de Lange T, (1999) p53- and ATM-dependent apoptosis induced by telomeres lacking TRF2. Science 283: 1321-1325.
    • (1999) Science , vol.283 , pp. 1321-1325
    • Karlseder, J.1    Broccoli, D.2    Dai, Y.3    Hardy, S.4    de Lange, T.5
  • 19
    • 7044232011 scopus 로고    scopus 로고
    • Homologous recombination generates T-loop-sized deletions at human telomeres
    • Wang RC, Smogorzewska A, de Lange T, (2004) Homologous recombination generates T-loop-sized deletions at human telomeres. Cell 119: 355-368.
    • (2004) Cell , vol.119 , pp. 355-368
    • Wang, R.C.1    Smogorzewska, A.2    de Lange, T.3
  • 20
    • 23044500389 scopus 로고    scopus 로고
    • POT1 protects telomeres from a transient DNA damage response and determines how human chromosomes end
    • Hockemeyer D, Sfeir AJ, Shay JW, Wright WE, de Lange T, (2005) POT1 protects telomeres from a transient DNA damage response and determines how human chromosomes end. Embo J 24: 2667-2678.
    • (2005) Embo J , vol.24 , pp. 2667-2678
    • Hockemeyer, D.1    Sfeir, A.J.2    Shay, J.W.3    Wright, W.E.4    de Lange, T.5
  • 21
    • 34548317418 scopus 로고    scopus 로고
    • Protection of telomeres through independent control of ATM and ATR by TRF2 and POT1
    • Denchi EL, de Lange T, (2007) Protection of telomeres through independent control of ATM and ATR by TRF2 and POT1. Nature 448: 1068-1071.
    • (2007) Nature , vol.448 , pp. 1068-1071
    • Denchi, E.L.1    de Lange, T.2
  • 22
    • 43249105463 scopus 로고    scopus 로고
    • Cell cycle control of telomere protection and NHEJ revealed by a ts mutation in the DNA-binding domain of TRF2
    • Konishi A, de Lange T, (2008) Cell cycle control of telomere protection and NHEJ revealed by a ts mutation in the DNA-binding domain of TRF2. Genes Dev 22: 1221-1230.
    • (2008) Genes Dev , vol.22 , pp. 1221-1230
    • Konishi, A.1    de Lange, T.2
  • 23
    • 0035844082 scopus 로고    scopus 로고
    • Pot1, the putative telomere end-binding protein in fission yeast and humans
    • Baumann P, Cech TR, (2001) Pot1, the putative telomere end-binding protein in fission yeast and humans. Science 292: 1171-1175.
    • (2001) Science , vol.292 , pp. 1171-1175
    • Baumann, P.1    Cech, T.R.2
  • 24
    • 11144277882 scopus 로고    scopus 로고
    • Loss of hPot1 function leads to telomere instability and a cut-like phenotype
    • Veldman T, Etheridge KT, Counter CM, (2004) Loss of hPot1 function leads to telomere instability and a cut-like phenotype. Curr Biol 14: 2264-2270.
    • (2004) Curr Biol , vol.14 , pp. 2264-2270
    • Veldman, T.1    Etheridge, K.T.2    Counter, C.M.3
  • 25
    • 20744448037 scopus 로고    scopus 로고
    • Distinct requirements for Pot1 in limiting telomere length and maintaining chromosome stability
    • Bunch JT, Bae NS, Leonardi J, Baumann P, (2005) Distinct requirements for Pot1 in limiting telomere length and maintaining chromosome stability. Mol Cell Biol 25: 5567-5578.
    • (2005) Mol Cell Biol , vol.25 , pp. 5567-5578
    • Bunch, J.T.1    Bae, N.S.2    Leonardi, J.3    Baumann, P.4
  • 26
    • 84984754548 scopus 로고    scopus 로고
    • Telomeric localization of TRF2, a novel human telobox protein
    • Bilaud T, Brun C, Ancelin K, Koering CE, Laroche T, et al. (1997) Telomeric localization of TRF2, a novel human telobox protein. Nat Genet 17: 236-239.
    • (1997) Nat Genet , vol.17 , pp. 236-239
    • Bilaud, T.1    Brun, C.2    Ancelin, K.3    Koering, C.E.4    Laroche, T.5
  • 27
    • 84984775429 scopus 로고    scopus 로고
    • Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2
    • Broccoli D, Smogorzewska A, Chong L, de Lange T, (1997) Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2. Nat Genet 17: 231-235.
    • (1997) Nat Genet , vol.17 , pp. 231-235
    • Broccoli, D.1    Smogorzewska, A.2    Chong, L.3    de Lange, T.4
  • 29
    • 21444444520 scopus 로고    scopus 로고
    • How the human telomeric proteins TRF1 and TRF2 recognize telomeric DNA: a view from high-resolution crystal structures
    • Court R, Chapman L, Fairall L, Rhodes D, (2005) How the human telomeric proteins TRF1 and TRF2 recognize telomeric DNA: a view from high-resolution crystal structures. EMBO Rep 6: 39-45.
    • (2005) EMBO Rep , vol.6 , pp. 39-45
    • Court, R.1    Chapman, L.2    Fairall, L.3    Rhodes, D.4
  • 31
    • 0037192462 scopus 로고    scopus 로고
    • Senescence induced by altered telomere state, not telomere loss
    • Karlseder J, Smogorzewska A, de Lange T, (2002) Senescence induced by altered telomere state, not telomere loss. Science 295: 2446-2449.
    • (2002) Science , vol.295 , pp. 2446-2449
    • Karlseder, J.1    Smogorzewska, A.2    de Lange, T.3
  • 32
    • 19344374569 scopus 로고    scopus 로고
    • The telomeric protein TRF2 binds the ATM kinase and can inhibit the ATM-dependent DNA damage response
    • Karlseder J, Hoke K, Mirzoeva OK, Bakkenist C, Kastan MB, et al. (2004) The telomeric protein TRF2 binds the ATM kinase and can inhibit the ATM-dependent DNA damage response. PLoS Biol 2: E240.
    • (2004) PLoS Biol , vol.2
    • Karlseder, J.1    Hoke, K.2    Mirzoeva, O.K.3    Bakkenist, C.4    Kastan, M.B.5
  • 33
    • 67349246601 scopus 로고    scopus 로고
    • The shelterin protein TRF2 inhibits Chk2 activity at telomeres in the absence of DNA damage
    • Buscemi G, Zannini L, Fontanella E, Lecis D, Lisanti S, et al. (2009) The shelterin protein TRF2 inhibits Chk2 activity at telomeres in the absence of DNA damage. Curr Biol 19: 874-879.
    • (2009) Curr Biol , vol.19 , pp. 874-879
    • Buscemi, G.1    Zannini, L.2    Fontanella, E.3    Lecis, D.4    Lisanti, S.5
  • 34
    • 27144515686 scopus 로고    scopus 로고
    • XPF nuclease-dependent telomere loss and increased DNA damage in mice overexpressing TRF2 result in premature aging and cancer
    • Munoz P, Blanco R, Flores JM, Blasco MA, (2005) XPF nuclease-dependent telomere loss and increased DNA damage in mice overexpressing TRF2 result in premature aging and cancer. Nat Genet 37: 1063-1071.
    • (2005) Nat Genet , vol.37 , pp. 1063-1071
    • Munoz, P.1    Blanco, R.2    Flores, J.M.3    Blasco, M.A.4
  • 36
    • 0035476710 scopus 로고    scopus 로고
    • T-loop assembly in vitro involves binding of TRF2 near the 3′ telomeric overhang
    • Stansel RM, de Lange T, Griffith JD, (2001) T-loop assembly in vitro involves binding of TRF2 near the 3′ telomeric overhang. Embo J 20: 5532-5540.
    • (2001) Embo J , vol.20 , pp. 5532-5540
    • Stansel, R.M.1    de Lange, T.2    Griffith, J.D.3
  • 39
    • 10944271790 scopus 로고    scopus 로고
    • Taz1 binding to a fission yeast model telomere: formation of telomeric loops and higher order structures
    • Tomaska L, Willcox S, Slezakova J, Nosek J, Griffith JD, (2004) Taz1 binding to a fission yeast model telomere: formation of telomeric loops and higher order structures. J Biol Chem 279: 50764-50772.
    • (2004) J Biol Chem , vol.279 , pp. 50764-50772
    • Tomaska, L.1    Willcox, S.2    Slezakova, J.3    Nosek, J.4    Griffith, J.D.5
  • 40
    • 34548737554 scopus 로고    scopus 로고
    • TRF2 is required for repair of nontelomeric DNA double-strand breaks by homologous recombination
    • Mao Z, Seluanov A, Jiang Y, Gorbunova V, (2007) TRF2 is required for repair of nontelomeric DNA double-strand breaks by homologous recombination. Proc Natl Acad Sci U S A 104: 13068-13073.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 13068-13073
    • Mao, Z.1    Seluanov, A.2    Jiang, Y.3    Gorbunova, V.4
  • 41
    • 33845987076 scopus 로고    scopus 로고
    • The basic domain of TRF2 directs binding to DNA junctions irrespective of the presence of TTAGGG repeats
    • Fouche N, Cesare AJ, Willcox S, Ozgur S, Compton SA, et al. (2006) The basic domain of TRF2 directs binding to DNA junctions irrespective of the presence of TTAGGG repeats. J Biol Chem 281: 37486-37495.
    • (2006) J Biol Chem , vol.281 , pp. 37486-37495
    • Fouche, N.1    Cesare, A.J.2    Willcox, S.3    Ozgur, S.4    Compton, S.A.5
  • 42
    • 0034847376 scopus 로고    scopus 로고
    • Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2
    • Fairall L, Chapman L, Moss H, de Lange T, Rhodes D, (2001) Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2. Mol Cell 8: 351-361.
    • (2001) Mol Cell , vol.8 , pp. 351-361
    • Fairall, L.1    Chapman, L.2    Moss, H.3    de Lange, T.4    Rhodes, D.5
  • 45
    • 68949198783 scopus 로고    scopus 로고
    • TERRA RNA binding to TRF2 facilitates heterochromatin formation and ORC recruitment at telomeres
    • Deng Z, Norseen J, Wiedmer A, Riethman H, Lieberman PM, (2009) TERRA RNA binding to TRF2 facilitates heterochromatin formation and ORC recruitment at telomeres. Mol Cell 35: 403-413.
    • (2009) Mol Cell , vol.35 , pp. 403-413
    • Deng, Z.1    Norseen, J.2    Wiedmer, A.3    Riethman, H.4    Lieberman, P.M.5
  • 46
    • 63249087946 scopus 로고    scopus 로고
    • The effect of the TRF2 N-terminal and TRFH regions on telomeric G-quadruplex structures
    • Pedroso IM, Hayward W, Fletcher TM, (2009) The effect of the TRF2 N-terminal and TRFH regions on telomeric G-quadruplex structures. Nucleic Acids Res 37: 1541-1554.
    • (2009) Nucleic Acids Res , vol.37 , pp. 1541-1554
    • Pedroso, I.M.1    Hayward, W.2    Fletcher, T.M.3
  • 47
    • 69849107002 scopus 로고    scopus 로고
    • The Myb/SANT domain of the telomere-binding protein TRF2 alters chromatin structure
    • Baker AM, Fu Q, Hayward W, Lindsay SM, Fletcher TM, (2009) The Myb/SANT domain of the telomere-binding protein TRF2 alters chromatin structure. Nucleic Acids Res 37: 5019-5031.
    • (2009) Nucleic Acids Res , vol.37 , pp. 5019-5031
    • Baker, A.M.1    Fu, Q.2    Hayward, W.3    Lindsay, S.M.4    Fletcher, T.M.5
  • 48
    • 18944387709 scopus 로고    scopus 로고
    • Recombination at long mutant telomeres produces tiny single- and double-stranded telomeric circles
    • Groff-Vindman C, Cesare AJ, Natarajan S, Griffith JD, McEachern MJ, (2005) Recombination at long mutant telomeres produces tiny single- and double-stranded telomeric circles. Mol Cell Biol 25: 4406-4412.
    • (2005) Mol Cell Biol , vol.25 , pp. 4406-4412
    • Groff-Vindman, C.1    Cesare, A.J.2    Natarajan, S.3    Griffith, J.D.4    McEachern, M.J.5
  • 51
    • 12844270590 scopus 로고    scopus 로고
    • DNA structure-dependent recruitment of telomeric proteins to single-stranded/double-stranded DNA junctions
    • Yanez GH, Khan SJ, Locovei AM, Pedroso IM, Fletcher TM, (2005) DNA structure-dependent recruitment of telomeric proteins to single-stranded/double-stranded DNA junctions. Biochem Biophys Res Commun 328: 49-56.
    • (2005) Biochem Biophys Res Commun , vol.328 , pp. 49-56
    • Yanez, G.H.1    Khan, S.J.2    Locovei, A.M.3    Pedroso, I.M.4    Fletcher, T.M.5
  • 52
    • 77957027468 scopus 로고
    • Basic analysis of transcription factor binding to nucleosomes
    • Methods in Molecular Genetics, Academic Press
    • Côté J, Utley RT, Workman JL, Kenneth WA, (1995) Basic analysis of transcription factor binding to nucleosomes. Methods in Molecular Genetics Academic Press pp. 108-128.
    • (1995) , pp. 108-128
    • Côté, J.1    Utley, R.T.2    Workman, J.L.3    Kenneth, W.A.4
  • 53
    • 0024468871 scopus 로고
    • Homogeneous reconstituted oligonucleosomes, evidence for salt-dependent folding in the absence of histone H1
    • Hansen JC, Ausio J, Stanik VH, van Holde KE, (1989) Homogeneous reconstituted oligonucleosomes, evidence for salt-dependent folding in the absence of histone H1. Biochemistry 28: 9129-9136.
    • (1989) Biochemistry , vol.28 , pp. 9129-9136
    • Hansen, J.C.1    Ausio, J.2    Stanik, V.H.3    van Holde, K.E.4
  • 54
    • 0024720506 scopus 로고
    • The sieving of spheres during agarose gel electrophoresis: quantitation and modeling
    • Griess GA, Moreno ET, Easom RA, Serwer P, (1989) The sieving of spheres during agarose gel electrophoresis: quantitation and modeling. Biopolymers 28: 1475-1484.
    • (1989) Biopolymers , vol.28 , pp. 1475-1484
    • Griess, G.A.1    Moreno, E.T.2    Easom, R.A.3    Serwer, P.4
  • 55
    • 0028331878 scopus 로고
    • Quantitative agarose gel electrophoresis of chromatin: nucleosome-dependent changes in charge, sharp, and deformability at low ionic strength
    • Fletcher TM, Krishnan U, Serwer P, Hansen JC, (1994) Quantitative agarose gel electrophoresis of chromatin: nucleosome-dependent changes in charge, sharp, and deformability at low ionic strength. Biochemistry 33: 2226-2233.
    • (1994) Biochemistry , vol.33 , pp. 2226-2233
    • Fletcher, T.M.1    Krishnan, U.2    Serwer, P.3    Hansen, J.C.4
  • 56
    • 0036931098 scopus 로고    scopus 로고
    • Glutaraldehyde modified mica: A new surface for atomic force microscopy of chromatin
    • Wang H, Bash R, Yodh JG, Hager GH, Lohr D, et al. (2002) Glutaraldehyde modified mica: A new surface for atomic force microscopy of chromatin. Biophys J 83: 3619-3625.
    • (2002) Biophys J , vol.83 , pp. 3619-3625
    • Wang, H.1    Bash, R.2    Yodh, J.G.3    Hager, G.H.4    Lohr, D.5
  • 57
    • 0018531367 scopus 로고
    • Acidic polypeptides can assemble both histones and chromatin in vitro at physiological ionic strength
    • Stein A, Whitlock JP Jr, Bina M, (1979) Acidic polypeptides can assemble both histones and chromatin in vitro at physiological ionic strength. Proc Natl Acad Sci U S A 76: 5000-5004.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 5000-5004
    • Stein, A.1    Whitlock Jr., J.P.2    Bina, M.3
  • 58
    • 0031194492 scopus 로고    scopus 로고
    • Analysis of transcription factor-mediated remodeling of nucleosomal arrays in a purified system
    • Steger DJ, Owen-Hughes T, John S, Workman JL, (1997) Analysis of transcription factor-mediated remodeling of nucleosomal arrays in a purified system. Methods 12: 276-285.
    • (1997) Methods , vol.12 , pp. 276-285
    • Steger, D.J.1    Owen-Hughes, T.2    John, S.3    Workman, J.L.4
  • 59
    • 0029882454 scopus 로고    scopus 로고
    • Reversible oligonucleosome self-association: dependence on divalent cations and core histone tail domains
    • Schwarz PM, Felthauser A, Fletcher TM, Hansen JC, (1996) Reversible oligonucleosome self-association: dependence on divalent cations and core histone tail domains. Biochemistry 35: 4009-4015.
    • (1996) Biochemistry , vol.35 , pp. 4009-4015
    • Schwarz, P.M.1    Felthauser, A.2    Fletcher, T.M.3    Hansen, J.C.4
  • 60
    • 0028288557 scopus 로고
    • A role for histones H2A/H2B in chromatin folding and transcriptional repression
    • Hansen JC, Wolffe AP, (1994) A role for histones H2A/H2B in chromatin folding and transcriptional repression. Proc Natl Acad Sci U S A 91: 2339-2343.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 2339-2343
    • Hansen, J.C.1    Wolffe, A.P.2
  • 61
    • 0032553013 scopus 로고    scopus 로고
    • Linker histones stabilize the intrinsic salt-dependent folding of nucleosomal arrays: mechanistic ramifications for higher-order chromatin folding
    • Carruthers LM, Bednar J, Woodcock CL, Hansen JC, (1998) Linker histones stabilize the intrinsic salt-dependent folding of nucleosomal arrays: mechanistic ramifications for higher-order chromatin folding. Biochemistry 37: 14776-14787.
    • (1998) Biochemistry , vol.37 , pp. 14776-14787
    • Carruthers, L.M.1    Bednar, J.2    Woodcock, C.L.3    Hansen, J.C.4
  • 62
    • 33947201778 scopus 로고    scopus 로고
    • The H3 tail domain participates in multiple interactions during folding and self-association of nucleosome arrays
    • Kan PY, Lu X, Hansen JC, Hayes JJ, (2007) The H3 tail domain participates in multiple interactions during folding and self-association of nucleosome arrays. Mol Cell Biol 27: 2084-2091.
    • (2007) Mol Cell Biol , vol.27 , pp. 2084-2091
    • Kan, P.Y.1    Lu, X.2    Hansen, J.C.3    Hayes, J.J.4
  • 63
    • 58549094957 scopus 로고    scopus 로고
    • Chromatin condensing functions of the linker histone C-terminal domain are mediated by specific amino acid composition and intrinsic protein disorder
    • Lu X, Hamkalo B, Parseghian MH, Hansen JC, (2009) Chromatin condensing functions of the linker histone C-terminal domain are mediated by specific amino acid composition and intrinsic protein disorder. Biochemistry 48: 164-172.
    • (2009) Biochemistry , vol.48 , pp. 164-172
    • Lu, X.1    Hamkalo, B.2    Parseghian, M.H.3    Hansen, J.C.4
  • 64
    • 26644471508 scopus 로고    scopus 로고
    • The core histone N-terminal tail domains function independently and additively during salt-dependent oligomerization of nucleosomal arrays
    • Gordon F, Luger K, Hansen JC, (2005) The core histone N-terminal tail domains function independently and additively during salt-dependent oligomerization of nucleosomal arrays. J Biol Chem 280: 33701-33706.
    • (2005) J Biol Chem , vol.280 , pp. 33701-33706
    • Gordon, F.1    Luger, K.2    Hansen, J.C.3
  • 65
    • 0028074481 scopus 로고
    • Quantitative analysis of macromolecular conformational changes using agarose gel electrophoresis: application to chromatin folding
    • Fletcher TM, Serwer P, Hansen JC, (1994) Quantitative analysis of macromolecular conformational changes using agarose gel electrophoresis: application to chromatin folding. Biochemistry 33: 10859-10863.
    • (1994) Biochemistry , vol.33 , pp. 10859-10863
    • Fletcher, T.M.1    Serwer, P.2    Hansen, J.C.3
  • 66
    • 0025327471 scopus 로고
    • Electrostatic mechanism of chromatin folding
    • Clark DJ, Kimura T, (1990) Electrostatic mechanism of chromatin folding. J Mol Biol 211: 883-896.
    • (1990) J Mol Biol , vol.211 , pp. 883-896
    • Clark, D.J.1    Kimura, T.2
  • 67
    • 0018266771 scopus 로고
    • Structure of the chromatosome, a chromatin particle containing 160 base pairs of DNA and all the histones
    • Simpson RT, (1978) Structure of the chromatosome, a chromatin particle containing 160 base pairs of DNA and all the histones. Biochemistry 17: 5524-5531.
    • (1978) Biochemistry , vol.17 , pp. 5524-5531
    • Simpson, R.T.1
  • 68
    • 34948908780 scopus 로고    scopus 로고
    • MeCP2-chromatin interactions include the formation of chromatosome-like structures and are altered in mutations causing Rett syndrome
    • Nikitina T, Ghosh RP, Horowitz-Scherer RA, Hansen JC, Grigoryev SA, et al. (2007) MeCP2-chromatin interactions include the formation of chromatosome-like structures and are altered in mutations causing Rett syndrome. J Biol Chem 282: 28237-28245.
    • (2007) J Biol Chem , vol.282 , pp. 28237-28245
    • Nikitina, T.1    Ghosh, R.P.2    Horowitz-Scherer, R.A.3    Hansen, J.C.4    Grigoryev, S.A.5
  • 69
    • 77954958609 scopus 로고    scopus 로고
    • TRF2 and apollo cooperate with topoisomerase 2alpha to protect human telomeres from replicative damage
    • Ye J, Lenain C, Bauwens S, Rizzo A, Saint-Leger A, et al. (2010) TRF2 and apollo cooperate with topoisomerase 2alpha to protect human telomeres from replicative damage. Cell 142: 230-242.
    • (2010) Cell , vol.142 , pp. 230-242
    • Ye, J.1    Lenain, C.2    Bauwens, S.3    Rizzo, A.4    Saint-Leger, A.5
  • 72
    • 77952318828 scopus 로고    scopus 로고
    • The human telomeric protein hTRF1 induces telomere-specific nucleosome mobility
    • Pisano S, Leoni D, Galati A, Rhodes D, Savino M, et al. (2010) The human telomeric protein hTRF1 induces telomere-specific nucleosome mobility. Nucleic Acids Res 38: 2247-2255.
    • (2010) Nucleic Acids Res , vol.38 , pp. 2247-2255
    • Pisano, S.1    Leoni, D.2    Galati, A.3    Rhodes, D.4    Savino, M.5
  • 73
    • 33745226438 scopus 로고    scopus 로고
    • The Human Telomeric Protein TRF1 Specifically Recognizes Nucleosomal Binding Sites and Alters Nucleosome Structure
    • Galati A, Rossetti L, Pisano S, Chapman L, Rhodes D, et al. (2006) The Human Telomeric Protein TRF1 Specifically Recognizes Nucleosomal Binding Sites and Alters Nucleosome Structure. J Mol Biol 360: 377-385.
    • (2006) J Mol Biol , vol.360 , pp. 377-385
    • Galati, A.1    Rossetti, L.2    Pisano, S.3    Chapman, L.4    Rhodes, D.5
  • 74
    • 0037175018 scopus 로고    scopus 로고
    • Telomere-binding protein TRF2 binds to and stimulates the Werner and Bloom syndrome helicases
    • Opresko PL, von Kobbe C, Laine JP, Harrigan J, Hickson ID, et al. (2002) Telomere-binding protein TRF2 binds to and stimulates the Werner and Bloom syndrome helicases. J Biol Chem 277: 41110-41119.
    • (2002) J Biol Chem , vol.277 , pp. 41110-41119
    • Opresko, P.L.1    von Kobbe, C.2    Laine, J.P.3    Harrigan, J.4    Hickson, I.D.5
  • 75
    • 2942637828 scopus 로고    scopus 로고
    • The Werner Syndrome Helicase and Exonuclease Cooperate to Resolve Telomeric D Loops in a Manner Regulated by TRF1 and TRF2
    • Opresko PL, Otterlei M, Graakjaer J, Bruheim P, Dawut L, et al. (2004) The Werner Syndrome Helicase and Exonuclease Cooperate to Resolve Telomeric D Loops in a Manner Regulated by TRF1 and TRF2. Mol Cell 14: 763-774.
    • (2004) Mol Cell , vol.14 , pp. 763-774
    • Opresko, P.L.1    Otterlei, M.2    Graakjaer, J.3    Bruheim, P.4    Dawut, L.5
  • 76
    • 77955070324 scopus 로고    scopus 로고
    • Telomeric protein TRF2 protects Holliday junctions with telomeric arms from displacement by the Werner syndrome helicase
    • Nora GJ, Buncher NA, Opresko PL, (2010) Telomeric protein TRF2 protects Holliday junctions with telomeric arms from displacement by the Werner syndrome helicase. Nucleic Acids Res 38: 3984-3998.
    • (2010) Nucleic Acids Res , vol.38 , pp. 3984-3998
    • Nora, G.J.1    Buncher, N.A.2    Opresko, P.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.