메뉴 건너뛰기




Volumn 4, Issue 8, 2005, Pages 939-950

Histone dynamics in living cells revealed by photobleaching

Author keywords

Fluorescence recovery after photobleaching (FRAP); Green fluorescent protein (GFP); Histone exchange; Living cells; Molecular kinetics

Indexed keywords

CENTROMERE PROTEIN A; HISTONE; HISTONE H2A; HISTONE H2B; HISTONE H3; NUCLEAR PROTEIN; UNCLASSIFIED DRUG;

EID: 21844465956     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2005.04.012     Document Type: Review
Times cited : (83)

References (132)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 a resolution
    • K. Luger, A.W. Mader, R.K. Richimond, D.F. Sargent, and T.J. Richmond Crystal structure of the nucleosome core particle at 2.8 A resolution Nature 389 1997 251 260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richimond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 2
    • 0034659231 scopus 로고    scopus 로고
    • De novo nucleosome assembly: New pieces in old puzzle
    • A. Verreault De novo nucleosome assembly: new pieces in old puzzle Genes Dev. 14 2000 1430 1438
    • (2000) Genes Dev. , vol.14 , pp. 1430-1438
    • Verreault, A.1
  • 3
    • 0035313802 scopus 로고    scopus 로고
    • The ins and outs of nucleosome assembly
    • J.A. Mello, and G. Almouzni The ins and outs of nucleosome assembly Curr. Opin. Genet. Dev. 11 2001 136 141
    • (2001) Curr. Opin. Genet. Dev. , vol.11 , pp. 136-141
    • Mello, J.A.1    Almouzni, G.2
  • 4
    • 3042522654 scopus 로고    scopus 로고
    • Chromatin dynamics at DNA replication, transcription and repair
    • A.E. Ehrenhofer-Murray Chromatin dynamics at DNA replication, transcription and repair Eur. J. Biochem. 271 2004 2335 23249
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2335-23249
    • Ehrenhofer-Murray, A.E.1
  • 5
    • 0022393483 scopus 로고
    • Histone synthesis and deposition in the G1 and S phases of hepatoma tissue culture cells
    • V. Jackson, and R. Chalkley Histone synthesis and deposition in the G1 and S phases of hepatoma tissue culture cells Biochemistry 24 1985 6921 6930
    • (1985) Biochemistry , vol.24 , pp. 6921-6930
    • Jackson, V.1    Chalkley, R.2
  • 6
    • 0021796444 scopus 로고
    • Exchange of histones H1, H2A, and H2B in vivo
    • L. Louters, and R. Chalkley Exchange of histones H1, H2A, and H2B in vivo Biochemistry 4 1985 3080 3085
    • (1985) Biochemistry , vol.4 , pp. 3080-3085
    • Louters, L.1    Chalkley, R.2
  • 7
    • 0025134076 scopus 로고
    • In vivo studies on the dynamics of histone-DNA interaction: Evidence for nucleosome dissolution during replication and transcription and a low level of dissolution independent on both
    • V. Jackson In vivo studies on the dynamics of histone-DNA interaction: evidence for nucleosome dissolution during replication and transcription and a low level of dissolution independent on both Biochemistry 29 1990 719 731
    • (1990) Biochemistry , vol.29 , pp. 719-731
    • Jackson, V.1
  • 8
    • 0025089206 scopus 로고
    • Nucleosomal histones of transcriptionally active/competent chromatin preferentially exchange with newly synthesized histones in quiescent chicken erythrocytes
    • M.J. Hendzel, and J.R. Davie Nucleosomal histones of transcriptionally active/competent chromatin preferentially exchange with newly synthesized histones in quiescent chicken erythrocytes Biochem. J. 271 1990 67 73
    • (1990) Biochem. J. , vol.271 , pp. 67-73
    • Hendzel, M.J.1    Davie, J.R.2
  • 9
    • 0018842145 scopus 로고
    • Arginine-rich histones do not exchange between human and mouse chromosomes in hybrid cells
    • T. Manser, T. Thacher, and M. Rechsteiner Arginine-rich histones do not exchange between human and mouse chromosomes in hybrid cells Cell 19 1980 993 1003
    • (1980) Cell , vol.19 , pp. 993-1003
    • Manser, T.1    Thacher, T.2    Rechsteiner, M.3
  • 10
    • 0041668053 scopus 로고    scopus 로고
    • In vivo protein-protein and protein-DNA crosslinking for genomewide binding microarray
    • S.K. Krudistani, and M. Grunstein In vivo protein-protein and protein-DNA crosslinking for genomewide binding microarray Methods 31 2003 90 95
    • (2003) Methods , vol.31 , pp. 90-95
    • Krudistani, S.K.1    Grunstein, M.2
  • 11
    • 0041668072 scopus 로고    scopus 로고
    • Immunoprecipitation of native chromatin: NChIP
    • L.P. O'Neill, and B.M. Turner Immunoprecipitation of native chromatin: NChIP Methods 31 2003 76 82
    • (2003) Methods , vol.31 , pp. 76-82
    • O'Neill, L.P.1    Turner, B.M.2
  • 12
    • 0036850325 scopus 로고    scopus 로고
    • Cellular memory and the histone code
    • B.M. Turner Cellular memory and the histone code Cell 111 2002 285 291
    • (2002) Cell , vol.111 , pp. 285-291
    • Turner, B.M.1
  • 14
    • 1942439629 scopus 로고    scopus 로고
    • Mechanisms for ATP-dependent chromatin remodeling: Farewell to the tuna-can octamer?
    • A. Flaus, and T. Owen-Hughes Mechanisms for ATP-dependent chromatin remodeling: farewell to the tuna-can octamer? Curr. Opin. Genet. Dev. 14 2004 165 173
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 165-173
    • Flaus, A.1    Owen-Hughes, T.2
  • 15
    • 6044256118 scopus 로고    scopus 로고
    • Histones and histone modifications
    • C.L. Peterson, and M.A. Laniel Histones and histone modifications Curr. Biol. 14 2004 R546 R551
    • (2004) Curr. Biol. , vol.14
    • Peterson, C.L.1    Laniel, M.A.2
  • 16
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • R.Y. Tsien The green fluorescent protein Annu. Rev. Biochem. 67 1998 509 544
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 17
    • 0033082623 scopus 로고    scopus 로고
    • Photobleaching GFP reveals protein dynamics inside live cells
    • J. White, and E. Stelzer Photobleaching GFP reveals protein dynamics inside live cells Trends Cell Biol. 9 1999 61 65
    • (1999) Trends Cell Biol. , vol.9 , pp. 61-65
    • White, J.1    Stelzer, E.2
  • 18
    • 0035106336 scopus 로고    scopus 로고
    • Macromolecular dynamics in living cell nuclei revealed by fluorescence redistribution after photobleaching
    • A.B. Houtsmuller, and W. Vermeulen Macromolecular dynamics in living cell nuclei revealed by fluorescence redistribution after photobleaching Histochem. Cell Biol. 15 2001 13 21
    • (2001) Histochem. Cell Biol. , vol.15 , pp. 13-21
    • Houtsmuller, A.B.1    Vermeulen, W.2
  • 19
    • 0035654399 scopus 로고    scopus 로고
    • Kinetic modeling approaches to in vivo imaging
    • R.D. Phair, and T. Misteli Kinetic modeling approaches to in vivo imaging Nature Rev. Mol. Cell Biol. 2 2001 898 907
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 898-907
    • Phair, R.D.1    Misteli, T.2
  • 22
    • 1642494582 scopus 로고    scopus 로고
    • Measuring histone and polymerase dynamics in living cells
    • H. Kimura, M. Hieda, and M.P.R. Cook Measuring histone and polymerase dynamics in living cells Methods Enzymol. 375 2004 381 393
    • (2004) Methods Enzymol. , vol.375 , pp. 381-393
    • Kimura, H.1    Hieda, M.2    Cook, M.P.R.3
  • 23
    • 1642377367 scopus 로고    scopus 로고
    • Measurement of dynamic protein binding to chromatin in vivo, using photobleaching microscopy
    • R.D. Phair, S.A. Gorski, and S.A.T. Misteli Measurement of dynamic protein binding to chromatin in vivo, using photobleaching microscopy Methods Enzymol. 375 2004 393 414
    • (2004) Methods Enzymol. , vol.375 , pp. 393-414
    • Phair, R.D.1    Gorski, S.A.2    Misteli, S.A.T.3
  • 25
    • 3042760021 scopus 로고    scopus 로고
    • Global nature of dynamic protein-chromatin interactions in vivo: Three-dimensional genome scanning and dynamic interaction networks of chromatin proteins
    • R.D. Phair, P. Scaffidi, C. Elbi, J. Vecerova, A. Dey, K. Ozato, D.T. Brown, G. Hager, M. Bustin, and T. Misteli Global nature of dynamic protein-chromatin interactions in vivo: three-dimensional genome scanning and dynamic interaction networks of chromatin proteins Mol. Cell. Biol. 24 2004 6393 6402
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6393-6402
    • Phair, R.D.1    Scaffidi, P.2    Elbi, C.3    Vecerova, J.4    Dey, A.5    Ozato, K.6    Brown, D.T.7    Hager, G.8    Bustin, M.9    Misteli, T.10
  • 26
    • 2942690158 scopus 로고    scopus 로고
    • Analysis of binding reactions by fluorescence recovery after photobleaching
    • B.L. Sprague, R.L. Pego, D.A. Stavreva, and J.G. McNally Analysis of binding reactions by fluorescence recovery after photobleaching Biophys. J. 86 2004 3473 3495
    • (2004) Biophys. J. , vol.86 , pp. 3473-3495
    • Sprague, B.L.1    Pego, R.L.2    Stavreva, D.A.3    McNally, J.G.4
  • 29
    • 14044250885 scopus 로고    scopus 로고
    • Functional region of CENP-H interacts with the Nuf2 complex that localizes to centromere during mitosis
    • Y. Mikami, T. Hori, H. Kimura, and T. Fukagawa Functional region of CENP-H interacts with the Nuf2 complex that localizes to centromere during mitosis Mol. Cell. Biol. 25 2005 1958 1970
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 1958-1970
    • Mikami, Y.1    Hori, T.2    Kimura, H.3    Fukagawa, T.4
  • 30
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • R.D. Phair, and T. Misteli High mobility of proteins in the mammalian cell nucleus Nature 404 2000 604 609
    • (2000) Nature , vol.404 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 31
    • 0037049641 scopus 로고    scopus 로고
    • The transcription cycle of RNA polymerase II in living cells
    • H. Kimura, K. Sugaya, and P.R. Cook The transcription cycle of RNA polymerase II in living cells J. Cell Biol. 159 2002 777 782
    • (2002) J. Cell Biol. , vol.159 , pp. 777-782
    • Kimura, H.1    Sugaya, K.2    Cook, P.R.3
  • 32
    • 0035954427 scopus 로고    scopus 로고
    • Kinetics of core histones in living human cells: Little exchange of H3 and H4 and some rapid exchange of H2B
    • H. Kimura, and P.R. Cook Kinetics of core histones in living human cells: little exchange of H3 and H4 and some rapid exchange of H2B J. Cell Biol. 153 2001 1341 1353
    • (2001) J. Cell Biol. , vol.153 , pp. 1341-1353
    • Kimura, H.1    Cook, P.R.2
  • 33
    • 0035691790 scopus 로고    scopus 로고
    • SnRNP protein expression enhances the formation of Cajal bodies containing p80-coilin and SMN
    • J.E. Sleeman, P. Ajuh, and A.I. Lamond snRNP protein expression enhances the formation of Cajal bodies containing p80-coilin and SMN J. Cell Sci. 114 2001 4407 4419
    • (2001) J. Cell Sci. , vol.114 , pp. 4407-4419
    • Sleeman, J.E.1    Ajuh, P.2    Lamond, A.I.3
  • 34
    • 0032568321 scopus 로고    scopus 로고
    • Histone-GFP fusion protein enables sensitive analysis of chromosome dynamics in living mammalian cells
    • T. Kanda, K.F. Sullivan, and K.F.G.M. Wahl Histone-GFP fusion protein enables sensitive analysis of chromosome dynamics in living mammalian cells Curr. Biol. 8 1998 377 385
    • (1998) Curr. Biol. , vol.8 , pp. 377-385
    • Kanda, T.1    Sullivan, K.F.2    Wahl, K.F.G.M.3
  • 35
    • 0034449565 scopus 로고    scopus 로고
    • The dynamics of acentric chromosomes in cancer cells revealed by GFP-based chromosome labeling strategies
    • T. Kanda, and G.M. Wahl The dynamics of acentric chromosomes in cancer cells revealed by GFP-based chromosome labeling strategies J. Cell. Biochem. Suppl 35 2000 107 114
    • (2000) J. Cell. Biochem. , Issue.35 SUPPL. , pp. 107-114
    • Kanda, T.1    Wahl, G.M.2
  • 36
    • 0034649663 scopus 로고    scopus 로고
    • Dynamic binding of histone H1 to chromatin in living cells
    • T. Misteli, A. Gunjan, R. Hock, M Bustin, and D.T. Brown Dynamic binding of histone H1 to chromatin in living cells Nature 408 2000 877 881
    • (2000) Nature , vol.408 , pp. 877-881
    • Misteli, T.1    Gunjan, A.2    Hock, R.3    Bustin, M.4    Brown, D.T.5
  • 37
    • 0037144862 scopus 로고    scopus 로고
    • Phosphorylation and an ATP-dependent process increase the dynamic exchange of H1 in chromatin
    • Y. Dou, J. Bowen, Y. Liu, and M.A. Gorovsky Phosphorylation and an ATP-dependent process increase the dynamic exchange of H1 in chromatin J. Cell Biol. 158 2002 1161 1170
    • (2002) J. Cell Biol. , vol.158 , pp. 1161-1170
    • Dou, Y.1    Bowen, J.2    Liu, Y.3    Gorovsky, M.A.4
  • 38
    • 0034649621 scopus 로고    scopus 로고
    • Rapid exchange of histone H1.1 on chromatin in living human cells
    • M.A. Lever, X. Th'ng, M.J. Sun, and M.J. Hendzel Rapid exchange of histone H1.1 on chromatin in living human cells Nature 408 2000 873 876
    • (2000) Nature , vol.408 , pp. 873-876
    • Lever, M.A.1    Th'Ng, X.2    Sun, M.J.3    Hendzel, M.J.4
  • 41
    • 0036668636 scopus 로고    scopus 로고
    • Competition between histone H1 and HMGN proteins for chromatin binding sites
    • F. Catez, D.T. Brown, T. Misteli, and M. Bustin Competition between histone H1 and HMGN proteins for chromatin binding sites EMBO Rep. 3 2002 760 766
    • (2002) EMBO Rep. , vol.3 , pp. 760-766
    • Catez, F.1    Brown, D.T.2    Misteli, T.3    Bustin, M.4
  • 42
    • 0345830411 scopus 로고    scopus 로고
    • Rapid replacement of somatic linker histones with the oocyte-specific liker histone H1foo in nuclear transfer
    • T. Teranishi, M. Tanaka, S. Kimoto, Y. Ono, K. Miyakoshi, T. Kono, and Y. Yoshimura Rapid replacement of somatic linker histones with the oocyte-specific liker histone H1foo in nuclear transfer Dev. Biol. 266 2004 76 86
    • (2004) Dev. Biol. , vol.266 , pp. 76-86
    • Teranishi, T.1    Tanaka, M.2    Kimoto, S.3    Ono, Y.4    Miyakoshi, K.5    Kono, T.6    Yoshimura, Y.7
  • 44
    • 12144283465 scopus 로고    scopus 로고
    • Condensed mitotic chromatin is accessible to transcription factors and chromatin structural proteins
    • D. Chen, M. Dundr, C. Wang, A. Leung, A. Lamond, T. Misteli, and S. Huang Condensed mitotic chromatin is accessible to transcription factors and chromatin structural proteins J. Cell Biol. 168 2005 41 54
    • (2005) J. Cell Biol. , vol.168 , pp. 41-54
    • Chen, D.1    Dundr, M.2    Wang, C.3    Leung, A.4    Lamond, A.5    Misteli, T.6    Huang, S.7
  • 45
    • 0022551060 scopus 로고
    • Histone hyperacetylation: Its effects on nucleosome conformation and stability
    • J. Ausió, and K.E. van Holde Histone hyperacetylation: its effects on nucleosome conformation and stability Biochemistry 22 1986 1421 1428
    • (1986) Biochemistry , vol.22 , pp. 1421-1428
    • Ausió, J.1    Van Holde, K.E.2
  • 46
    • 0034634558 scopus 로고    scopus 로고
    • Acetylation increases the a-helical content of the histone tails of the nucleosome
    • X. Wang, S.C. Moore, M. Laszckzak, and J. Ausió Acetylation increases the a-helical content of the histone tails of the nucleosome J. Biol. Chem. 275 2000 35013 35020
    • (2000) J. Biol. Chem. , vol.275 , pp. 35013-35020
    • Wang, X.1    Moore, S.C.2    Laszckzak, M.3    Ausió, J.4
  • 47
    • 0027716843 scopus 로고
    • Effects of histone acetylation, ubiquitination and variants on nucleosome stability
    • W. Li, S. Nagaraja, G.P. Delcuve, M.J. Hendzel, and J.R. Davie Effects of histone acetylation, ubiquitination and variants on nucleosome stability Biochem. J. 296 1993 737 744
    • (1993) Biochem. J. , vol.296 , pp. 737-744
    • Li, W.1    Nagaraja, S.2    Delcuve, G.P.3    Hendzel, M.J.4    Davie, J.R.5
  • 48
    • 0023807950 scopus 로고
    • Effects of histone acetylation on nucleosome properties as evaluated by polyacrylamide gel electrophoresis and hydroxylapatite dissociation chromatography
    • M. Hirose Effects of histone acetylation on nucleosome properties as evaluated by polyacrylamide gel electrophoresis and hydroxylapatite dissociation chromatography J. Biochem. (Tokyo) 103 1988 31 35
    • (1988) J. Biochem. (Tokyo) , vol.103 , pp. 31-35
    • Hirose, M.1
  • 49
    • 0025779831 scopus 로고
    • Histone acetylation and control of gene expression
    • B.M. Turner Histone acetylation and control of gene expression J. Cell Sci. 99 1991 13 20
    • (1991) J. Cell Sci. , vol.99 , pp. 13-20
    • Turner, B.M.1
  • 50
    • 0021470855 scopus 로고
    • Purification and initial characterization of a protein which facilitates assembly of nucleosome-like structure from mammalian cells
    • Y. Ishimi, J. Hirosumi, K. Sato, K. Sugasawa, S. Yokota, F. Hanaoka, and M. Yamada Purification and initial characterization of a protein which facilitates assembly of nucleosome-like structure from mammalian cells Eur. J. Biochem. 142 1984 431 439
    • (1984) Eur. J. Biochem. , vol.142 , pp. 431-439
    • Ishimi, Y.1    Hirosumi, J.2    Sato, K.3    Sugasawa, K.4    Yokota, S.5    Hanaoka, F.6    Yamada, M.7
  • 51
    • 1542298307 scopus 로고    scopus 로고
    • Histone chaperones, a supporting role in the limelight
    • A. Loyola, and G. Almouzni Histone chaperones, a supporting role in the limelight Biochim. Biophys. Acta 1677 2004 3 11
    • (2004) Biochim. Biophys. Acta , vol.1677 , pp. 3-11
    • Loyola, A.1    Almouzni, G.2
  • 52
    • 0033898468 scopus 로고    scopus 로고
    • P300-mediated acetylation facilitates the transfer of histone H2A-H2B dimers from nucleosomes to a histone chaperone
    • T. Ito, T. Ikehara, T. Nakagawa, W.L. Kraus, and M. Muramatsu p300-mediated acetylation facilitates the transfer of histone H2A-H2B dimers from nucleosomes to a histone chaperone Genes Dev. 14 2000 1899 1907
    • (2000) Genes Dev. , vol.14 , pp. 1899-1907
    • Ito, T.1    Ikehara, T.2    Nakagawa, T.3    Kraus, W.L.4    Muramatsu, M.5
  • 53
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • B.D. Strahl, and C.D. Allis The language of covalent histone modifications Nature 403 2000 41 45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 54
    • 12544258222 scopus 로고    scopus 로고
    • Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding
    • Y.-J. Park, J.V. Chodaparambil, Y. Bao, S.J. McBryant, and K. Luger Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding J. Biol. Chem. 280 2005 1817 1825
    • (2005) J. Biol. Chem. , vol.280 , pp. 1817-1825
    • Park, Y.-J.1    Chodaparambil, J.V.2    Bao, Y.3    McBryant, S.J.4    Luger, K.5
  • 55
  • 56
    • 0036203807 scopus 로고    scopus 로고
    • Nucleosome remodeling induced by RNA polymerase II: Loss of the H2A/H2B dimer during transcription
    • M.L. Kireeva, W. Walter, V. Tchernajenko, V. Bondarenko, M. Kashlev, and V.M. Studitsky Nucleosome remodeling induced by RNA polymerase II: loss of the H2A/H2B dimer during transcription Mol. Cell 9 2002 541 552
    • (2002) Mol. Cell , vol.9 , pp. 541-552
    • Kireeva, M.L.1    Walter, W.2    Tchernajenko, V.3    Bondarenko, V.4    Kashlev, M.5    Studitsky, V.M.6
  • 57
    • 0023663417 scopus 로고
    • Nucleosomes inhibit the initiation of transcription but allow chain elongation with the displacement of histones
    • Y. Lorch, J.W. LaPointe, and R.D. Kornberg Nucleosomes inhibit the initiation of transcription but allow chain elongation with the displacement of histones Cell 49 1987 203 210
    • (1987) Cell , vol.49 , pp. 203-210
    • Lorch, Y.1    Lapointe, J.W.2    Kornberg, R.D.3
  • 58
    • 0026733468 scopus 로고
    • A nucleosome core is transferred out of the path of a transcribing polymerase
    • D.J. Clark, and G. Felsenfeld A nucleosome core is transferred out of the path of a transcribing polymerase Cell 71 1992 11 22
    • (1992) Cell , vol.71 , pp. 11-22
    • Clark, D.J.1    Felsenfeld, G.2
  • 59
    • 0036964090 scopus 로고    scopus 로고
    • Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway: Polymerase passage may degrade chromatin structure
    • T. Formosa, S. Roune, M.D. Adams, A.E. Olsen, P. Eriksson, Y. Yu, A.R. Rhoades, P.D. Kaufman, and D.J. Stillman Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin structure Genetics 162 2002 1557 1571
    • (2002) Genetics , vol.162 , pp. 1557-1571
    • Formosa, T.1    Roune, S.2    Adams, M.D.3    Olsen, A.E.4    Eriksson, P.5    Yu, Y.6    Rhoades, A.R.7    Kaufman, P.D.8    Stillman, D.J.9
  • 61
    • 0242579933 scopus 로고    scopus 로고
    • The FACT complex travels with elongating RNA polymerase II and is important for the fidelity of transcriptional initiation in vivo
    • P.B. Mason, and K. Struhl The FACT complex travels with elongating RNA polymerase II and is important for the fidelity of transcriptional initiation in vivo Mol. Cell. Biol. 23 2003 8323 8333
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8323-8333
    • Mason, P.B.1    Struhl, K.2
  • 63
    • 0026713778 scopus 로고
    • What happens to nucleosomes during transcription?
    • K.E. van Holde, D.E. Lohr, and C. Robert What happens to nucleosomes during transcription? J. Biol. Chem. 267 1992 2837 2840
    • (1992) J. Biol. Chem. , vol.267 , pp. 2837-2840
    • Van Holde, K.E.1    Lohr, D.E.2    Robert, C.3
  • 64
    • 8644287437 scopus 로고    scopus 로고
    • Evidence for eviction and rapid deposition of histones upon transcriptional elongation by RNA polymerase II
    • M.A. Schwabish, and K. Struhl Evidence for eviction and rapid deposition of histones upon transcriptional elongation by RNA polymerase II Mol. Cell. Biol. 24 2004 10111 10117
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10111-10117
    • Schwabish, M.A.1    Struhl, K.2
  • 65
    • 1542267778 scopus 로고    scopus 로고
    • Histone release during transcription: NAP1 forms a complex with H2A and H2B and facilitates a topologically dependent release of H3 and H4 from the nucleosome
    • V. Levchenko, and V. Jackson Histone release during transcription: NAP1 forms a complex with H2A and H2B and facilitates a topologically dependent release of H3 and H4 from the nucleosome Biochemistry 43 2004 2359 2372
    • (2004) Biochemistry , vol.43 , pp. 2359-2372
    • Levchenko, V.1    Jackson, V.2
  • 66
    • 0031813779 scopus 로고    scopus 로고
    • Numbers and organization of RNA polymerases, nascent transcripts and transcription units in HeLa nuclei
    • D.A. Jackson, F.J. Iborra, E.M.M. Manders, and P.R. Cook Numbers and organization of RNA polymerases, nascent transcripts and transcription units in HeLa nuclei Mol. Biol. Cell 9 1998 1523 1536
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1523-1536
    • Jackson, D.A.1    Iborra, F.J.2    Manders, E.M.M.3    Cook, P.R.4
  • 67
    • 0032562720 scopus 로고    scopus 로고
    • Visualization of single RNA transcripts in situ
    • A.M. Femino, F.S. Fay, K. Fogarty, and R.H. Singer Visualization of single RNA transcripts in situ Science 280 1998 585 590
    • (1998) Science , vol.280 , pp. 585-590
    • Femino, A.M.1    Fay, F.S.2    Fogarty, K.3    Singer, R.H.4
  • 68
    • 0036299092 scopus 로고    scopus 로고
    • The histone variant H3.3 marks active chromatin by replication- independent nucleosome assembly
    • K. Ahmad, and S. Henikoff The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly Mol. Cell 9 2002 1191 1200
    • (2002) Mol. Cell , vol.9 , pp. 1191-1200
    • Ahmad, K.1    Henikoff, S.2
  • 70
    • 0742304304 scopus 로고    scopus 로고
    • Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis
    • H. Tagami, D. Ray-Gallet, G. Almouzni, and Y. Nakatani Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis Cell 116 2004 51 61
    • (2004) Cell , vol.116 , pp. 51-61
    • Tagami, H.1    Ray-Gallet, D.2    Almouzni, G.3    Nakatani, Y.4
  • 71
    • 0033582544 scopus 로고    scopus 로고
    • Replication-dependent marking of DNA by PCNA facilitates CAF-1-coupled inheritance of chromatin
    • K. Shibahara, and B. Stillman Replication-dependent marking of DNA by PCNA facilitates CAF-1-coupled inheritance of chromatin Cell 96 1999 575 585
    • (1999) Cell , vol.96 , pp. 575-585
    • Shibahara, K.1    Stillman, B.2
  • 73
    • 1242342240 scopus 로고    scopus 로고
    • Histone H3.3 is enriched in covalent modifications associated with active chromatin
    • E. McKittrick, P.R. Gafken, K. Ahmad, and S. Henikoff Histone H3.3 is enriched in covalent modifications associated with active chromatin Proc. Natl. Acad. Sci. U.S.A. 101 2004 1525 1530
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 1525-1530
    • McKittrick, E.1    Gafken, P.R.2    Ahmad, K.3    Henikoff, S.4
  • 74
    • 0036591877 scopus 로고    scopus 로고
    • Centromeres and variant histones: What, where, when and why?
    • M.M. Smith Centromeres and variant histones: what, where, when and why? Curr. Opin. Cell Biol. 14 2002 279 285
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 279-285
    • Smith, M.M.1
  • 75
    • 2142809838 scopus 로고    scopus 로고
    • Assembly of kinetochores in vertebrate cells
    • T. Fukagawa Assembly of kinetochores in vertebrate cells Exp. Cell Res. 296 2004 21 27
    • (2004) Exp. Cell Res. , vol.296 , pp. 21-27
    • Fukagawa, T.1
  • 76
    • 0035921425 scopus 로고    scopus 로고
    • Centromere identity in Drosophila is not determined in vivo by replication timing
    • B. Sullivan, and G. Karpen Centromere identity in Drosophila is not determined in vivo by replication timing J. Cell Biol. 154 2001 683 690
    • (2001) J. Cell Biol. , vol.154 , pp. 683-690
    • Sullivan, B.1    Karpen, G.2
  • 77
    • 4544275776 scopus 로고    scopus 로고
    • Mis16 and Mis18 are required for CENP-A loading and histone deacetylation at centromeres
    • T. Hayashi, Y. Fujita, O. Iwasaki, Y. Adachi, K. Takahashi, and M. Yanagida Mis16 and Mis18 are required for CENP-A loading and histone deacetylation at centromeres Cell 118 2004 715 729
    • (2004) Cell , vol.118 , pp. 715-729
    • Hayashi, T.1    Fujita, Y.2    Iwasaki, O.3    Adachi, Y.4    Takahashi, K.5    Yanagida, M.6
  • 79
    • 0032507949 scopus 로고    scopus 로고
    • Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals
    • C. Costanzi, and J.R. Pehrson Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals Nature 393 1998 599 601
    • (1998) Nature , vol.393 , pp. 599-601
    • Costanzi, C.1    Pehrson, J.R.2
  • 81
    • 0029954395 scopus 로고    scopus 로고
    • Essential and nonessential histone H2A variants in Tetrahymena thermophila
    • X. Liu, B. Li, and M.A. Gorovsky Essential and nonessential histone H2A variants in Tetrahymena thermophila Mol. Cell. Biol. 16 1996 4305 4311
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4305-4311
    • Liu, X.1    Li, B.2    Gorovsky, M.A.3
  • 82
    • 0027058961 scopus 로고
    • A histone variant, H2AvD, is essential in Drosophila melanogaster
    • A. van Daal, and S.C. Elgin A histone variant, H2AvD, is essential in Drosophila melanogaster Mol. Biol. Cell 3 1992 593 602
    • (1992) Mol. Biol. Cell , vol.3 , pp. 593-602
    • Van Daal, A.1    Elgin, S.C.2
  • 84
    • 0027759372 scopus 로고
    • Temporal and spatial association of histone H2A variant hv1 with transcriptionally competent chromatin during nuclear development in Tetrahymena thermophila
    • L.A. Stargell, J. Bowen, C.A. Dadd, P.C. Dedon, M. Davis, R.G. Cook, C.D. Allis, and M.A. Gorovsky Temporal and spatial association of histone H2A variant hv1 with transcriptionally competent chromatin during nuclear development in Tetrahymena thermophila Genes Dev. 7 1993 2641 2651
    • (1993) Genes Dev. , vol.7 , pp. 2641-2651
    • Stargell, L.A.1    Bowen, J.2    Dadd, C.A.3    Dedon, P.C.4    Davis, M.5    Cook, R.G.6    Allis, C.D.7    Gorovsky, M.A.8
  • 85
    • 0037423930 scopus 로고    scopus 로고
    • Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin
    • M.D. Meneghini, M. Wu, and H.D. Madhani Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin Cell 112 2003 725 736
    • (2003) Cell , vol.112 , pp. 725-736
    • Meneghini, M.D.1    Wu, M.2    Madhani, H.D.3
  • 86
    • 0035834777 scopus 로고    scopus 로고
    • Characterization of the stability and folding of H2A.Z chromatin particles: Implications for transcriptional activation
    • D. Wade Abbott, V.S. Ivanova, X. Wang, W.M. Bonner, and J. Ausió Characterization of the stability and folding of H2A.Z chromatin particles: implications for transcriptional activation J. Biol. Chem. 276 2001 41945 41949
    • (2001) J. Biol. Chem. , vol.276 , pp. 41945-41949
    • Wade Abbott, D.1    Ivanova, V.S.2    Wang, X.3    Bonner, W.M.4    Ausió, J.5
  • 87
    • 0036183219 scopus 로고    scopus 로고
    • The essential histone variant H2A.Z regulates the equilibrium between different chromatin conformational states
    • J.Y. Fan, F. Gordon, K. Luger, J.C. Hansen, and D.J. Tremethick The essential histone variant H2A.Z regulates the equilibrium between different chromatin conformational states Nature Struct. Biol. 9 2002 172 176
    • (2002) Nature Struct. Biol. , vol.9 , pp. 172-176
    • Fan, J.Y.1    Gordon, F.2    Luger, K.3    Hansen, J.C.4    Tremethick, D.J.5
  • 90
    • 0348184963 scopus 로고    scopus 로고
    • ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex
    • G. Mizuguchi, X. Shen, J. Landry, W.-H. Wu, S. Sen, and C. Wu ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex Science 303 2004 343 348
    • (2004) Science , vol.303 , pp. 343-348
    • Mizuguchi, G.1    Shen, X.2    Landry, J.3    Wu, W.-H.4    Sen, S.5    Wu, C.6
  • 91
    • 0037291760 scopus 로고    scopus 로고
    • Bromodomains mediate an acetyl-histone encoded antisilincing function at heterochromatin boundaries
    • A.G. Ladurner, C. Inouye, R. Jain, and R. Tjian Bromodomains mediate an acetyl-histone encoded antisilincing function at heterochromatin boundaries Mol. Cell 11 2003 365 376
    • (2003) Mol. Cell , vol.11 , pp. 365-376
    • Ladurner, A.G.1    Inouye, C.2    Jain, R.3    Tjian, R.4
  • 92
    • 0035931749 scopus 로고    scopus 로고
    • A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome
    • B.P. Chadwick, and H.F. Willard A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome J. Cell Biol. 152 2001 375 384
    • (2001) J. Cell Biol. , vol.152 , pp. 375-384
    • Chadwick, B.P.1    Willard, H.F.2
  • 100
    • 0035793376 scopus 로고    scopus 로고
    • Protein dynamics: Implications for nuclear architecture and gene expression
    • T. Misteli Protein dynamics: implications for nuclear architecture and gene expression Science 291 2001 843 847
    • (2001) Science , vol.291 , pp. 843-847
    • Misteli, T.1
  • 101
    • 0036928181 scopus 로고    scopus 로고
    • The transcription cycle in vivo: A blind watchmaker at work
    • W. Vermeulen, and A.B. Houtsmuller The transcription cycle in vivo: a blind watchmaker at work Mol. Cell 10 2002 1264 1266
    • (2002) Mol. Cell , vol.10 , pp. 1264-1266
    • Vermeulen, W.1    Houtsmuller, A.B.2
  • 102
    • 0036929125 scopus 로고    scopus 로고
    • DNA polymerase clamp shows little turnover at established replication sites but sequential de novo assembly at adjacent origin clusters
    • A. Sporbert, A. Gahl, R. Ankerhold, H. Leonhardt, and M.C. Cardoso DNA polymerase clamp shows little turnover at established replication sites but sequential de novo assembly at adjacent origin clusters Mol. Cell 10 2002 1355 1365
    • (2002) Mol. Cell , vol.10 , pp. 1355-1365
    • Sporbert, A.1    Gahl, A.2    Ankerhold, R.3    Leonhardt, H.4    Cardoso, M.C.5
  • 103
    • 0037376678 scopus 로고    scopus 로고
    • Nuclear choreography: Interpretations from living cells
    • S.M. Janiki, and D.L. Spector Nuclear choreography: interpretations from living cells Curr. Opin. Cell Biol. 15 2003 149 157
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 149-157
    • Janiki, S.M.1    Spector, D.L.2
  • 104
    • 4143131124 scopus 로고    scopus 로고
    • Dynamic targeting of the replication machinery to site of DNA damage
    • D.A. Solomon, C.M. Cardoso, and E.S. Knudsen Dynamic targeting of the replication machinery to site of DNA damage J. Cell Biol. 166 2004 455 463
    • (2004) J. Cell Biol. , vol.166 , pp. 455-463
    • Solomon, D.A.1    Cardoso, C.M.2    Knudsen, E.S.3
  • 108
    • 0036498909 scopus 로고    scopus 로고
    • Transient association of Ku with nuclear substrates characterized using fluorescence photobleaching
    • W. Rodgers, S. Jordan, and J.D. Capra Transient association of Ku with nuclear substrates characterized using fluorescence photobleaching J. Immunol. 168 2002 2348 2355
    • (2002) J. Immunol. , vol.168 , pp. 2348-2355
    • Rodgers, W.1    Jordan, S.2    Capra, J.D.3
  • 109
    • 2442637866 scopus 로고    scopus 로고
    • Visualization of inositol phosphate-dependent mobility of Ku: Depletion of the DNA-PK cofactor InsP6 inhibits Ku mobility
    • J. Byrum, S. Jordan, S.T. Safrany, and W. Rodgers Visualization of inositol phosphate-dependent mobility of Ku: depletion of the DNA-PK cofactor InsP6 inhibits Ku mobility Nucleic Acids Res. 32 2004 2776 2784
    • (2004) Nucleic Acids Res. , vol.32 , pp. 2776-2784
    • Byrum, J.1    Jordan, S.2    Safrany, S.T.3    Rodgers, W.4
  • 110
    • 0022049737 scopus 로고
    • A general method for preparing chromatin containing intact DNA
    • D.A. Jackson, and P.R. Cook A general method for preparing chromatin containing intact DNA EMBO J. 4 1985 913 918
    • (1985) EMBO J. , vol.4 , pp. 913-918
    • Jackson, D.A.1    Cook, P.R.2
  • 111
    • 0025083331 scopus 로고
    • Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors
    • S.A. Adam, R.S. Marr, and L. Gerace Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors J. Cell Biol. 111 1990 807 816
    • (1990) J. Cell Biol. , vol.111 , pp. 807-816
    • Adam, S.A.1    Marr, R.S.2    Gerace, L.3
  • 112
    • 0028338617 scopus 로고
    • Sites in human nuclei where damage induced by ultraviolet light is repaired: Localization relative to transcription sites and concentrations of proliferating cell nuclear antigen and the tumour suppressor protein, p53
    • D.A. Jackson, A.B. Hassan, R.J. Errington, and P.R. Cook Sites in human nuclei where damage induced by ultraviolet light is repaired: localization relative to transcription sites and concentrations of proliferating cell nuclear antigen and the tumour suppressor protein, p53 J. Cell Sci. 107 1994 1753 1760
    • (1994) J. Cell Sci. , vol.107 , pp. 1753-1760
    • Jackson, D.A.1    Hassan, A.B.2    Errington, R.J.3    Cook, P.R.4
  • 113
    • 0033561153 scopus 로고    scopus 로고
    • Regional specialization in human nuclei: Visualization of discrete sites of transcription by RNA polymerase III
    • A. Pombo, D.A. Jackson, M. Hollinshead, Z. Wang, R.G. Roeder, and P.R. Cook Regional specialization in human nuclei: visualization of discrete sites of transcription by RNA polymerase III EMBO J. 18 1999 2241 2253
    • (1999) EMBO J. , vol.18 , pp. 2241-2253
    • Pombo, A.1    Jackson, D.A.2    Hollinshead, M.3    Wang, Z.4    Roeder, R.G.5    Cook, P.R.6
  • 114
    • 1642303197 scopus 로고    scopus 로고
    • In vitro FRAP reveals the ATP-dependent nuclear mobilization of the exon junction complex protein SRm160
    • S. Wagner, S. Chiosea, M. Ivshina, and J.A. Nickerson In vitro FRAP reveals the ATP-dependent nuclear mobilization of the exon junction complex protein SRm160 J. Cell Biol. 164 2004 843 850
    • (2004) J. Cell Biol. , vol.164 , pp. 843-850
    • Wagner, S.1    Chiosea, S.2    Ivshina, M.3    Nickerson, J.A.4
  • 118
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • N.C. Shaner, R.E. Campbell, P.A. Steinbach, B.N. Giepmans, A.E. Palmer, and R.Y. Tsien Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein Nature Biotechnol. 22 2004 1567 1572
    • (2004) Nature Biotechnol. , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.4    Palmer, A.E.5    Tsien, R.Y.6
  • 120
    • 0037343944 scopus 로고    scopus 로고
    • Visualization of the spatial and temporal dynamics of intracellular signaling
    • A. Miyawaki Visualization of the spatial and temporal dynamics of intracellular signaling Dev. Cell 4 2003 295 305
    • (2003) Dev. Cell , vol.4 , pp. 295-305
    • Miyawaki, A.1
  • 121
    • 1842578717 scopus 로고    scopus 로고
    • Dynamic interaction between BAF and emerin revealed by FRAP, FLIP, and FRET analyses in living HeLa cells
    • T. Shimi, T. Koujin, M. Segura-Totten, K.L. Wilson, T. Haraguchi, and Y. Hiraoka Dynamic interaction between BAF and emerin revealed by FRAP, FLIP, and FRET analyses in living HeLa cells J. Struct. Biol. 147 2004 31 41
    • (2004) J. Struct. Biol. , vol.147 , pp. 31-41
    • Shimi, T.1    Koujin, T.2    Segura-Totten, M.3    Wilson, K.L.4    Haraguchi, T.5    Hiraoka, Y.6
  • 122
    • 4644309827 scopus 로고    scopus 로고
    • Detection of snRNP assembly intermediates in Cajal bodies by fluorescence resonance energy transfer
    • D. Stanek, and K.M. Neugebauer Detection of snRNP assembly intermediates in Cajal bodies by fluorescence resonance energy transfer J. Cell Biol. 166 2004 1015 1025
    • (2004) J. Cell Biol. , vol.166 , pp. 1015-1025
    • Stanek, D.1    Neugebauer, K.M.2
  • 124
    • 0035421133 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer analysis of cell surface receptor interactions and signaling using spectral variants of the green fluorescent protein
    • F.K. Chan, R.M. Siegel, D. Zacharias, R. Swofford, K.L. Holms, R.Y. Tsien, and M.J. Lenardo Fluorescence resonance energy transfer analysis of cell surface receptor interactions and signaling using spectral variants of the green fluorescent protein Cytometry 44 2001 361 368
    • (2001) Cytometry , vol.44 , pp. 361-368
    • Chan, F.K.1    Siegel, R.M.2    Zacharias, D.3    Swofford, R.4    Holms, K.L.5    Tsien, R.Y.6    Lenardo, M.J.7
  • 125
    • 1642564551 scopus 로고    scopus 로고
    • Selective recognition of acetylated histones by bromodomain proteins visualized in living cells
    • T. Kanno, Y. Kanno, R.M. Siegel, M.K. Jang, M.J. Lenardo, and K. Ozato Selective recognition of acetylated histones by bromodomain proteins visualized in living cells Mol. Cell 13 2004 33 43
    • (2004) Mol. Cell , vol.13 , pp. 33-43
    • Kanno, T.1    Kanno, Y.2    Siegel, R.M.3    Jang, M.K.4    Lenardo, M.J.5    Ozato, K.6
  • 126
    • 0037072602 scopus 로고    scopus 로고
    • A photoactivatable GFP for selective photolabeling of proteins and cells
    • G.H. Patterson, and J. Lippincott-Schwartz A photoactivatable GFP for selective photolabeling of proteins and cells Science 297 2002 1873 1877
    • (2002) Science , vol.297 , pp. 1873-1877
    • Patterson, G.H.1    Lippincott-Schwartz, J.2
  • 128
    • 8844260411 scopus 로고    scopus 로고
    • Regulated fast nucleocytoplasmic shuttling observed by reversible protein highlighting
    • R. Ando, H. Mizuno, and A. Miyawaki Regulated fast nucleocytoplasmic shuttling observed by reversible protein highlighting Science 306 2004 1370 1373
    • (2004) Science , vol.306 , pp. 1370-1373
    • Ando, R.1    Mizuno, H.2    Miyawaki, A.3
  • 129
    • 0036789916 scopus 로고    scopus 로고
    • An optical marker based on the UV-induced green-to-red photoconversion of a fluorescent protein
    • R. Ando, H. Hama, M. Yamamoto-Hino, H. Mizuno, and A. Miyawaki An optical marker based on the UV-induced green-to-red photoconversion of a fluorescent protein Proc. Natl. Acad. Sci. U.S.A. 99 2002 12651 12656
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 12651-12656
    • Ando, R.1    Hama, H.2    Yamamoto-Hino, M.3    Mizuno, H.4    Miyawaki, A.5
  • 132
    • 17644373758 scopus 로고    scopus 로고
    • Reversal of the cellular phenotype in the premature aging disease Hutchinson-Gilford progeria syndrome
    • P. Scaffidi, and T. Misteli Reversal of the cellular phenotype in the premature aging disease Hutchinson-Gilford progeria syndrome Nature Med. 11 2005 440 445
    • (2005) Nature Med. , vol.11 , pp. 440-445
    • Scaffidi, P.1    Misteli, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.