메뉴 건너뛰기




Volumn 41, Issue 7, 2013, Pages 4026-4035

Linker histone H1.0 interacts with an extensive network of proteins found in the nucleolus

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; FACT PROTEIN; H1 BINDING PROTEIN; RECOMBINANT PROTEIN; REGULATOR PROTEIN; RIBOSOME PROTEIN; RIBOSOME RNA; SF2 PROTEIN; U2AF65 PROTEIN; UNCLASSIFIED DRUG;

EID: 84876557218     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt104     Document Type: Article
Times cited : (70)

References (42)
  • 1
    • 29244467484 scopus 로고    scopus 로고
    • Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length
    • Woodcock, C.L., Skoultchi, A.I. and Fan, Y. (2006) Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length. Chromosome Res., 14, 17-25.
    • (2006) Chromosome Res. , vol.14 , pp. 17-25
    • Woodcock, C.L.1    Skoultchi, A.I.2    Fan, Y.3
  • 2
    • 23044489675 scopus 로고    scopus 로고
    • H1 family histones in the nucleus: Control of binding and localization by the C-terminal domain
    • DOI 10.1074/jbc.M501627200
    • Th'ng, J.P.H., Sung, R., Ye, M. and Hendzel, M.J. (2005) H1 family histones in the nucleus. Control of binding and localization by the C-terminal domain. J. Biol. Chem., 280, 27809-27814. (Pubitemid 41076896)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.30 , pp. 27809-27814
    • Th'ng, J.P.H.1    Sung, R.2    Ye, M.3    Hendzel, M.J.4
  • 3
    • 0036089388 scopus 로고    scopus 로고
    • Conformational dynamics of the chromatin fiber in solution: Determinants, mechanisms, and functions
    • DOI 10.1146/annurev.biophys.31.101101.140858
    • Hansen, J.C. (2002) Conformational dynamics of the chromatin fiber in solution: determinants, mechanisms, and functions. Annu. Rev. Biophys. Biomol. Struct., 31, 361-392. (Pubitemid 34666838)
    • (2002) Annual Review of Biophysics and Biomolecular Structure , vol.31 , pp. 361-392
    • Hansen, J.C.1
  • 4
    • 77952097668 scopus 로고    scopus 로고
    • Multifunctionality of the linker histones: An emerging role for protein-protein interactions
    • McBryant, S.J., Lu, X. and Hansen, J.C. (2010) Multifunctionality of the linker histones: an emerging role for protein-protein interactions. Cell Res., 20, 519-528.
    • (2010) Cell Res , vol.20 , pp. 519-528
    • McBryant, S.J.1    Lu, X.2    Hansen, J.C.3
  • 5
    • 0027402969 scopus 로고
    • Crystal structure of globular domain of histone H5 and its implications for nucleosome binding
    • DOI 10.1038/362219a0
    • Ramakrishnan, V., Finch, J., Graziano, V., Lee, P. and Sweet, R. (1993) Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature, 362, 219-223. (Pubitemid 23093625)
    • (1993) Nature , vol.362 , Issue.6417 , pp. 219-223
    • Ramakrishnan, V.1    Finch, J.T.2    Graziano, V.3    Lee, P.L.4    Sweet, R.M.5
  • 6
    • 0023355070 scopus 로고
    • The polypeptide fold of the globular domain of histone H5 in solution. A study using nuclear magnetic resonance distance geometry and restrained molecular dynamics
    • Clore, G.M., Gronenborn, A.M., Nilges, M., Sukumaran, D.K. and Zarbock, J. (1987) The polypeptide fold of the globular domain of histone H5 in solution. A study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics. EMBO J, 6, 1833-1842.
    • (1987) EMBO J , vol.6 , pp. 1833-1842
    • Clore, G.M.1    Gronenborn, A.M.2    Nilges, M.3    Sukumaran, D.K.4    Zarbock, J.5
  • 7
    • 0033151772 scopus 로고    scopus 로고
    • Histone H1: Location and role
    • DOI 10.1016/S0955-0674(99)80042-8
    • Thomas, J. (1999) Histone H1: location and role. Curr. Opin. Cell Biol., 11, 312-317. (Pubitemid 29273800)
    • (1999) Current Opinion in Cell Biology , vol.11 , Issue.3 , pp. 312-317
    • Thomas, J.O.1
  • 8
    • 33644865137 scopus 로고    scopus 로고
    • Intrinsic protein disorder, amino acid composition, and histone terminal domains
    • DOI 10.1074/jbc.R500022200
    • Hansen, J.C., Lu, X., Ross, E.D. and Woody, R.W. (2006) Intrinsic protein disorder, amino acid composition, and histone terminal domains. J. Biol. Chem., 281, 1853-1856. (Pubitemid 43845769)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.4 , pp. 1853-1856
    • Hansen, J.C.1    Lu, X.2    Ross, E.D.3    Woody, R.W.4
  • 9
    • 79958068470 scopus 로고    scopus 로고
    • Nucleosome linker DNA contacts and induces specific folding of the intrinsically disordered H1 carboxyl-terminal domain
    • Caterino, T.L., Fang, H. and Hayes, J.J. (2011) Nucleosome linker DNA contacts and induces specific folding of the intrinsically disordered H1 carboxyl-terminal domain. Mol. Cell. Biol., 31, 2341-2348.
    • (2011) Mol. Cell. Biol , vol.31 , pp. 2341-2348
    • Caterino, T.L.1    Fang, H.2    Hayes, J.J.3
  • 10
    • 0022446807 scopus 로고
    • Roles of H1 domains in determining higher order chromatin structure and H1 location
    • Allan, J., Mitchell, T., Harborne, N., Bohm, L. and Crane-Robinson, C. (1986) Roles of H1 domains in determining higher order chromatin structure and H1 location. J. Mol. Biol., 187, 591-601. (Pubitemid 16041060)
    • (1986) Journal of Molecular Biology , vol.187 , Issue.4 , pp. 591-601
    • Allan, J.1    Mitchell, T.2    Harborne, N.3
  • 11
    • 1542305640 scopus 로고    scopus 로고
    • 0 C-terminal Domain
    • DOI 10.1074/jbc.M311348200
    • Lu, X. and Hansen, J.C. (2004) Identification of specific functional subdomains within the linker histone H10 C-terminal domain. J. Biol. Chem., 279, 8701-8707. (Pubitemid 38295925)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.10 , pp. 8701-8707
    • Lu, X.1    Hansen, J.C.2
  • 12
    • 33746041435 scopus 로고    scopus 로고
    • Drosophila ribosomal proteins are associated with linker histone H1 and suppress gene transcription
    • DOI 10.1101/gad.390106
    • Ni, J.-Q., Liu, L.-P., Hess, D., Rietdorf, J. and Sun, F.-L. (2006) Drosophila ribosomal proteins are associated with linker histone H1 and suppress gene transcription. Genes Dev., 20, 1959-1973. (Pubitemid 44079332)
    • (2006) Genes and Development , vol.20 , Issue.14 , pp. 1959-1973
    • Ni, J.-Q.1    Liu, L.-P.2    Hess, D.3    Rietdorf, J.4    Sun, F.-L.5
  • 13
    • 44049092769 scopus 로고    scopus 로고
    • Isolation and characterization of a novel H1.2 complex that acts as a repressor of p53-mediated transcription
    • Kim, K., Choi, J., Heo, K., Kim, H., Levens, D., Kohno, K., Johnson, E.M., Brock, H.W. and An, W. (2008) Isolation and characterization of a novel H1.2 complex that acts as a repressor of p53-mediated transcription. J. Biol. Chem., 283, 9113-9126.
    • (2008) J. Biol. Chem , vol.283 , pp. 9113-9126
    • Kim, K.1    Choi, J.2    Heo, K.3    Kim, H.4    Levens, D.5    Kohno, K.6    Johnson, E.M.7    Brock, H.W.8    An, W.9
  • 14
    • 48049092838 scopus 로고    scopus 로고
    • HaloTag: A novel protein labeling technology for cell imaging and protein analysis
    • Los, G. and Encell, L. (2008) HaloTag: a novel protein labeling technology for cell imaging and protein analysis. ACS Chem. Biol., 3, 373-382.
    • (2008) ACS Chem. Biol , vol.3 , pp. 373-382
    • Los, G.1    Encell, L.2
  • 15
    • 82355184456 scopus 로고    scopus 로고
    • Histone chaperone FACT coordinates nucleosome interaction through multiple synergistic binding events
    • Winkler, D.D., Muthurajan, U.M., Hieb, A.R. and Luger, K. (2011) Histone chaperone FACT coordinates nucleosome interaction through multiple synergistic binding events. J. Biol. Chem., 286, 41883-41892.
    • (2011) J. Biol. Chem , vol.286 , pp. 41883-41892
    • Winkler, D.D.1    Muthurajan, U.M.2    Hieb, A.R.3    Luger, K.4
  • 17
    • 84865310327 scopus 로고    scopus 로고
    • Quantifying chromatin-associated interactions: The HI-FI system
    • Winkler, D., Luger, K. and Hieb, A. (2012) Quantifying chromatin-associated interactions: the HI-FI system. Methods Enzymol., 512, 243-274.
    • (2012) Methods Enzymol , vol.512 , pp. 243-274
    • Winkler, D.1    Luger, K.2    Hieb, A.3
  • 18
    • 0036674269 scopus 로고    scopus 로고
    • Large-scale proteomic analysis of the human spliceosome
    • DOI 10.1101/gr.473902
    • Rappsilber, J., Ryder, U., Lamond, A.I. and Mann, M. (2002) Large-scale proteomic analysis of the human spliceosome. Genome Res., 12, 1231-1245. (Pubitemid 41264425)
    • (2002) Genome Research , vol.12 , Issue.8 , pp. 1231-1245
    • Rappsilber, J.1    Ryder, U.2    Lamond, A.I.3    Mann, M.4
  • 19
    • 0037068447 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of the human spliceosome
    • DOI 10.1038/nature01031
    • Zhou, Z., Licklider, L.J., Gygi, S.P. and Reed, R. (2002) Comprehensive proteomic analysis of the human spliceosome. Nature, 419, 182-185. (Pubitemid 35025448)
    • (2002) Nature , vol.419 , Issue.6903 , pp. 182-185
    • Zhou, Z.1    Licklider, L.J.2    Gygi, S.P.3    Reed, R.4
  • 22
    • 84858419821 scopus 로고    scopus 로고
    • Fluorescence strategies for high-throughput quantification of protein interactions
    • Hieb, A., D'Arcy, S. and Kramer, M. (2012) Fluorescence strategies for high-throughput quantification of protein interactions. Nucleic Acids Res., 40, e33.
    • (2012) Nucleic Acids Res , vol.40
    • Hieb, A.1    D'Arcy, S.2    Kramer, M.3
  • 23
    • 84863255704 scopus 로고    scopus 로고
    • Evolution of SR protein and hnRNP splicing regulatory factors Wiley Interdiscip
    • Busch, A. and Hertel, K.J. (2012) Evolution of SR protein and hnRNP splicing regulatory factors. Wiley Interdiscip. Rev. RNA, 3, 1-12.
    • (2012) Rev. RNA , vol.3 , pp. 1-12
    • Busch, A.1    Hertel, K.J.2
  • 24
    • 79955844395 scopus 로고    scopus 로고
    • The histone chaperone FACT: Structural insights and mechanisms for nucleosome reorganization
    • Winkler, D.D. and Luger, K. (2011) The histone chaperone FACT: structural insights and mechanisms for nucleosome reorganization. J. Biol. Chem., 286, 18369-18374.
    • (2011) J. Biol. Chem , vol.286 , pp. 18369-18374
    • Winkler, D.D.1    Luger, K.2
  • 25
    • 58149289691 scopus 로고    scopus 로고
    • Histone H1 and its isoforms: Contribution to chromatin structure and function
    • Happel, N. and Doenecke, D. (2009) Histone H1 and its isoforms: contribution to chromatin structure and function. Gene, 431, 1-12.
    • (2009) Gene , vol.431 , pp. 1-12
    • Happel, N.1    Doenecke, D.2
  • 26
    • 79955041234 scopus 로고    scopus 로고
    • Structure of the H1 C-terminal domain and function in chromatin condensation
    • Caterino, T.L. and Hayes, J.J. (2011) Structure of the H1 C-terminal domain and function in chromatin condensation. Biochem. Cell Biol., 89, 35-44.
    • (2011) Biochem. Cell Biol , vol.89 , pp. 35-44
    • Caterino, T.L.1    Hayes, J.J.2
  • 27
    • 79954417213 scopus 로고    scopus 로고
    • The nucleolus: Structure/function relationship in RNA metabolism Wiley Interdiscip
    • Hernandez-Verdun, D., Roussel, P., Thiry, M., Sirri, V. and Lafontaine, D.L.J. (2010) The nucleolus: structure/function relationship in RNA metabolism. Wiley Interdiscip. Rev. RNA, 1, 415-431.
    • (2010) Rev. RNA , vol.1 , pp. 415-431
    • Hernandez-Verdun, D.1    Roussel, P.2    Thiry, M.3    Sirri, V.4    Lafontaine, D.L.J.5
  • 29
    • 0027221770 scopus 로고
    • A light microscope study of linker histone distribution in rat metaphase chromosomes and interphase nuclei
    • DOI 10.1006/excr.1993.1115
    • Breneman, J., Yau, P., Teplitz, R. and Bradbury, E. (1993) A light microscope study of linker histone distribution in rat metaphase chromosomes and interphase nuclei. Exp. Cell Res., 206, 16-26. (Pubitemid 23194674)
    • (1993) Experimental Cell Research , vol.206 , Issue.1 , pp. 16-26
    • Breneman, J.W.1    Yau, P.2    Teplitz, R.L.3    Bradbury, E.M.4
  • 31
    • 33748431061 scopus 로고    scopus 로고
    • SnoRNP Biogenesis Meets Pre-mRNA Splicing
    • DOI 10.1016/j.molcel.2006.08.023, PII S1097276506006058
    • Kiss, T. (2006) SnoRNP biogenesis meets pre-mRNA splicing. Mol. Cell, 23, 775-776. (Pubitemid 44344525)
    • (2006) Molecular Cell , vol.23 , Issue.6 , pp. 775-776
    • Kiss, T.1
  • 34
    • 0034649663 scopus 로고    scopus 로고
    • Dynamic binding of histone H1 to chromatin in living cells
    • DOI 10.1038/35048610
    • Misteli, T., Gunjan, A., Hock, R., Bustin, M. and Brown, D.T. (2000) Dynamic binding of histone H1 to chromatin in living cells. Nature, 408, 877-881. (Pubitemid 32016100)
    • (2000) Nature , vol.408 , Issue.6814 , pp. 877-881
    • Misteli, T.1    Gunjan, A.2    Hock, R.3    Bustin, M.4    Brown, D.T.5
  • 35
    • 0034649621 scopus 로고    scopus 로고
    • Rapid exchange of histone H1.1 on chromatin in living human cells
    • DOI 10.1038/35048603
    • Lever, M.A., Th'ng, J.P., Sun, X. and Hendzel, M.J. (2000) Rapid exchange of histone H1.1 on chromatin in living human cells. Nature, 408, 873-876. (Pubitemid 32016099)
    • (2000) Nature , vol.408 , Issue.6814 , pp. 873-876
    • Lever, M.A.1    Th'ng, J.P.H.2    Sun, X.3    Hendzel, M.J.4
  • 36
    • 21044438900 scopus 로고    scopus 로고
    • Multiple roles of arginine/serine-rich splicing factors in RNA processing
    • DOI 10.1042/BST0330443
    • Sanford, J.R., Ellis, J. and Cáceres, J.F. (2005) Multiple roles of arginine/serine-rich splicing factors in RNA processing. Biochem. Soc. Trans., 33, 443-446. (Pubitemid 40873861)
    • (2005) Biochemical Society Transactions , vol.33 , Issue.3 , pp. 443-446
    • Sanford, J.R.1    Ellis, J.2    Caceres, J.F.3
  • 37
    • 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. and Parseghian, M. (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.3
  • 39
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: Polymorphism and structural disorder in protein-protein interactions
    • Tompa, P. and Fuxreiter, M. (2008) Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends Biochem. Sci., 33, 2-8.
    • (2008) Trends Biochem. Sci , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 40
    • 19644400009 scopus 로고    scopus 로고
    • The histone H1 C-terminal domain binds to the apoptotic nuclease, DNA fragmentation factor (DFF40/CAD) and stimulates DNA cleavage
    • DOI 10.1021/bi050100n
    • Widlak, P., Kalinowska, M., Parseghian, M.H., Lu, X., Hansen, J.C. and Garrard, W.T. (2005) The histone H1 C-terminal domain binds to the apoptotic nuclease, DNA fragmentation factor (DFF40/CAD) and stimulates DNA cleavage. Biochemistry, 44, 7871-7878. (Pubitemid 40740770)
    • (2005) Biochemistry , vol.44 , Issue.21 , pp. 7871-7878
    • Widlak, P.1    Kalinowska, M.2    Parseghian, M.H.3    Lu, X.4    Hansen, J.C.5    Garrard, W.T.6
  • 41
    • 29144529317 scopus 로고    scopus 로고
    • Binding of barrier to autointegration factor (BAF) to histone H3 and selected linker histones including H1.1
    • DOI 10.1074/jbc.M509917200
    • Montes de Oca, R., Lee, K.K. and Wilson, K.L. (2005) Binding of barrier to autointegration factor (BAF) to histone H3 and selected linker histones including H1.1. J. Biol. Chem., 280, 42252-42262. (Pubitemid 43023196)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.51 , pp. 42252-42262
    • Montes De Oca, R.1    Lee, K.K.2    Wilson, K.L.3
  • 42
    • 15944379232 scopus 로고    scopus 로고
    • The many faces of the helix-turn-helix domain: Transcription regulation and beyond
    • DOI 10.1016/j.femsre.2004.12.008, Bacterial Genomics
    • Aravind, L., Anantharaman, V., Balaji, S., Babu, M.M. and Iyer, L.M. (2005) The many faces of the helix-turn-helix domain: transcription regulation and beyond. FEMS Microbiol. Rev., 29, 231-262. (Pubitemid 40439243)
    • (2005) FEMS Microbiology Reviews , vol.29 , Issue.2 , pp. 231-262
    • Aravind, L.1    Anantharaman, V.2    Balaji, S.3    Babu, M.M.4    Iyer, L.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.