메뉴 건너뛰기




Volumn 7, Issue , 2016, Pages

Dynamic and flexible H3K9me3 bridging via HP1β dimerization establishes a plastic state of condensed chromatin

(20)  Hiragami Hamada, Kyoko a   Soeroes, Szabolcs a,j   Nikolov, Miroslav a   Wilkins, Bryan b   Kreuz, Sarah a   Chen, Carol c   De La Rosa Velázquez, Inti A d   Zenn, Hans Michael e   Kost, Nils a   Pohl, Wiebke a   Chernev, Aleksandar a,f   Schwarzer, Dirk g   Jenuwein, Thomas d   Lorincz, Matthew c   Zimmermann, Bastian e   Walla, Peter Jomo a,h   Neumann, Heinz b   Baubec, Tuncay i   Urlaub, Henning a,f   Fischle, Wolfgang a  


Author keywords

[No Author keywords available]

Indexed keywords

H3K9ME3 PROTEIN; HETEROCHROMATIN PROTEIN 1; HETEROCHROMATIN PROTEIN 1 BETA; HISTONE H3; UNCLASSIFIED DRUG; CHROMATIN; HETEROCHROMATIN; HETEROCHROMATIN-SPECIFIC NONHISTONE CHROMOSOMAL PROTEIN HP-1; HISTONE; LYSINE; NONHISTONE PROTEIN; NUCLEOSOME; PROTEIN BINDING;

EID: 84973369696     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms11310     Document Type: Article
Times cited : (104)

References (64)
  • 1
    • 33845755946 scopus 로고    scopus 로고
    • Heterochromatin revisited
    • Grewal, S. I. & Jia, S. Heterochromatin revisited. Nat. Rev. Genet. 8, 35-46 (2007).
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 35-46
    • Grewal, S.I.1    Jia, S.2
  • 2
    • 1842733449 scopus 로고    scopus 로고
    • HP1 and the dynamics of heterochromatin maintenanceNat
    • Maison, C. & Almouzni, G. HP1 and the dynamics of heterochromatin maintenance. Nat. Rev. Mol. Cell Biol. 5, 296-304 (2004).
    • (2004) Rev. Mol. Cell Biol. , vol.5 , pp. 296-304
    • Maison, C.1    Almouzni, G.2
  • 3
    • 28844495048 scopus 로고    scopus 로고
    • Heterochromatin protein 1: A pervasive controlling influence
    • Hiragami, K. & Festenstein, R. Heterochromatin protein 1: a pervasive controlling influence. Cell Mol. Life Sci. 62, 2711-2726 (2005).
    • (2005) Cell Mol. Life Sci. , vol.62 , pp. 2711-2726
    • Hiragami, K.1    Festenstein, R.2
  • 5
    • 0041624239 scopus 로고    scopus 로고
    • Regulated recruitment of HP1 to a euchromatic gene induces mitotically heritable, epigenetic gene silencing: A mammalian cell culture model of gene variegation
    • Ayyanathan, K. et al. Regulated recruitment of HP1 to a euchromatic gene induces mitotically heritable, epigenetic gene silencing: a mammalian cell culture model of gene variegation. Genes Dev. 17, 1855-1869 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 1855-1869
    • Ayyanathan, K.1
  • 6
    • 18944394968 scopus 로고    scopus 로고
    • In vivo HP1 targeting causes large-scale chromatin condensation and enhanced histone lysine methylation
    • Verschure, P. J. et al. In vivo HP1 targeting causes large-scale chromatin condensation and enhanced histone lysine methylation. Mol. Cell. Biol. 25, 4552-4564 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 4552-4564
    • Verschure, P.J.1
  • 7
    • 0037086355 scopus 로고    scopus 로고
    • Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail
    • Jacobs, S. A. & Khorasanizadeh, S. Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail. Science 295, 2080-2083 (2002).
    • (2002) Science , vol.295 , pp. 2080-2083
    • Jacobs, S.A.1    Khorasanizadeh, S.2
  • 8
    • 0037034911 scopus 로고    scopus 로고
    • Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9
    • Nielsen, P. R. et al. Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9. Nature 416, 103-107 (2002).
    • (2002) Nature , vol.416 , pp. 103-107
    • Nielsen, P.R.1
  • 9
    • 10744228652 scopus 로고    scopus 로고
    • Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin
    • Thiru, A. et al. Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin. EMBO J. 23, 489-499 (2004).
    • (2004) EMBO J. , vol.23 , pp. 489-499
    • Thiru, A.1
  • 10
    • 33644850958 scopus 로고    scopus 로고
    • Heterochromatin protein 1: Don't judge the book by its cover! Curr
    • Hediger, F. & Gasser, S. M. Heterochromatin protein 1: don't judge the book by its cover! Curr. Opin. Genet. Dev. 16, 143-150 (2006).
    • (2006) Opin. Genet. Dev. , vol.16 , pp. 143-150
    • Hediger, F.1    Gasser, S.M.2
  • 11
    • 84871808185 scopus 로고    scopus 로고
    • Hinge and chromoshadow of HP1alpha participate in recognition of K9 methylated histone H3 in nucleosomes
    • Mishima, Y. et al. Hinge and chromoshadow of HP1alpha participate in recognition of K9 methylated histone H3 in nucleosomes. J. Mol. Biol. 425, 54-70 (2013).
    • (2013) J. Mol. Biol. , vol.425 , pp. 54-70
    • Mishima, Y.1
  • 12
    • 84896793351 scopus 로고    scopus 로고
    • Human heterochromatin protein 1alpha promotes nucleosome associations that drive chromatin condensation
    • Azzaz, A. M. et al. Human heterochromatin protein 1alpha promotes nucleosome associations that drive chromatin condensation. J. Biol. Chem. 289, 6850-6861 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 6850-6861
    • Azzaz, A.M.1
  • 13
    • 84926086707 scopus 로고    scopus 로고
    • N-terminal phosphorylation of HP1alpha increases its nucleosome-binding specificity
    • (in the press)
    • Nishibuchi, G. et al. N-terminal phosphorylation of HP1alpha increases its nucleosome-binding specificity. Nucleic Acid Res.. (in the press) 42, 12498-11 (2014).
    • (2014) Nucleic Acid Res. , vol.42 , pp. 12498-12511
    • Nishibuchi, G.1
  • 14
    • 84934911367 scopus 로고    scopus 로고
    • Multivalency governs HP1alpha association dynamics with the silent chromatin state
    • Kilic, S., Bachmann, A. L., Bryan, L. C. & Fierz, B. Multivalency governs HP1alpha association dynamics with the silent chromatin state. Nat. Commun. 6, 7313 (2015).
    • (2015) Nat. Commun. , vol.6 , pp. 7313
    • Kilic, S.1    Bachmann, A.L.2    Bryan, L.C.3    Fierz, B.4
  • 15
    • 58149202451 scopus 로고    scopus 로고
    • HP1-beta is required for development of the cerebral neocortex and neuromuscular junctions
    • Aucott, R. et al. HP1-beta is required for development of the cerebral neocortex and neuromuscular junctions. J. Cell Biol. 183, 597-606 (2008).
    • (2008) J. Cell Biol , vol.183 , pp. 597-606
    • Aucott, R.1
  • 17
    • 84856144675 scopus 로고    scopus 로고
    • Quantitative assessment of protein interaction with methyl-lysine analogues by hybrid computational and experimental approaches
    • Seeliger, D. et al. Quantitative assessment of protein interaction with methyl-lysine analogues by hybrid computational and experimental approaches. ACS Chem. Biol. 7, 150-154 (2012).
    • (2012) ACS Chem. Biol. , vol.7 , pp. 150-154
    • Seeliger, D.1
  • 18
    • 0036089388 scopus 로고    scopus 로고
    • Conformational dynamics of the chromatin fibre in solution: Determinants, mechanisms, and functions
    • Hansen, J. C. Conformational dynamics of the chromatin fibre in solution: determinants, mechanisms, and functions. Annu. Rev. Biophys. Biomol. Struct. 31, 361-392 (2002).
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 361-392
    • Hansen, J.C.1
  • 20
    • 70350475681 scopus 로고    scopus 로고
    • Monomer-dimer equilibrium in glutathione transferases: A critical re-examination
    • Fabrini, R. et al. Monomer-dimer equilibrium in glutathione transferases: a critical re-examination. Biochemistry 48, 10473-10482 (2009).
    • (2009) Biochemistry , vol.48 , pp. 10473-10482
    • Fabrini, R.1
  • 21
    • 28844477653 scopus 로고    scopus 로고
    • Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation
    • Fischle, W. et al. Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation. Nature 438, 1116-1122 (2005).
    • (2005) Nature , vol.438 , pp. 1116-1122
    • Fischle, W.1
  • 22
    • 0036221883 scopus 로고    scopus 로고
    • Salt-induced conformation and interaction changes of nucleosome core particles
    • Mangenot, S., Leforestier, A., Vachette, P., Durand, D. & Livolant, F. Salt-induced conformation and interaction changes of nucleosome core particles. Biophys. J. 82, 345-356 (2002).
    • (2002) Biophys. J. , vol.82 , pp. 345-356
    • Mangenot, S.1    Leforestier, A.2    Vachette, P.3    Durand, D.4    Livolant, F.5
  • 23
    • 84907588672 scopus 로고    scopus 로고
    • A distinct switch in interactions of the histone H4 tail domain upon salt-dependent folding of nucleosome arrays
    • Pepenella, S., Murphy, K. J. & Hayes, J. J. A distinct switch in interactions of the histone H4 tail domain upon salt-dependent folding of nucleosome arrays. J. Biol. Chem. 289, 27342-27351 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 27342-27351
    • Pepenella, S.1    Murphy, K.J.2    Hayes, J.J.3
  • 24
    • 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, J. C. 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).
    • (2005) J. Biol. Chem. , vol.280 , pp. 33701-33706
    • Gordon, F.1    Luger, K.2    Hansen, J.C.3
  • 25
    • 0037143649 scopus 로고    scopus 로고
    • Addition of a photocrosslinking amino acid to the genetic code of Escherichiacoli
    • Chin, J. W., Martin, A. B., King, D. S., Wang, L. & Schultz, P. G. Addition of a photocrosslinking amino acid to the genetic code of Escherichiacoli. Proc. Natl Acad. Sci. USA 99, 11020-11024 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 11020-11024
    • Chin, J.W.1    Martin, A.B.2    King, D.S.3    Wang, L.4    Schultz, P.G.5
  • 26
    • 0036509836 scopus 로고    scopus 로고
    • Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component
    • Maison, C. et al. Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component. Nat. Genet. 30, 329-334 (2002).
    • (2002) Nat. Genet. , vol.30 , pp. 329-334
    • Maison, C.1
  • 27
    • 0036775704 scopus 로고    scopus 로고
    • Coordinated methyl and RNA binding is required for heterochromatin localization of mammalian HP1alpha
    • Muchardt, C. et al. Coordinated methyl and RNA binding is required for heterochromatin localization of mammalian HP1alpha. EMBO Rep. 3, 975-981 (2002).
    • (2002) EMBO Rep. , vol.3 , pp. 975-981
    • Muchardt, C.1
  • 28
    • 0038613861 scopus 로고    scopus 로고
    • HP1 binding to native chromatin in vitro is determined by the hinge region and not by the chromodomain
    • Meehan, R. R., Kao, C. F. & Pennings, S. HP1 binding to native chromatin in vitro is determined by the hinge region and not by the chromodomain. EMBO J. 22, 3164-3174 (2003).
    • (2003) EMBO J , vol.22 , pp. 3164-3174
    • Meehan, R.R.1    Kao, C.F.2    Pennings, S.3
  • 29
    • 78650734995 scopus 로고    scopus 로고
    • Chromodomain-mediated oligomerization of HP1 suggests a nucleosome-bridging mechanism for heterochromatin assembly
    • Canzio, D. et al. Chromodomain-mediated oligomerization of HP1 suggests a nucleosome-bridging mechanism for heterochromatin assembly. Mol. Cell 41, 67-81 (2011).
    • (2011) Mol. Cell , vol.41 , pp. 67-81
    • Canzio, D.1
  • 30
    • 84866924932 scopus 로고    scopus 로고
    • Methylation of lysine 9 in histone H3 directs alternative modes of highly dynamic interaction of heterochromatin protein hHP1beta with the nucleosome
    • Munari, F. et al. Methylation of lysine 9 in histone H3 directs alternative modes of highly dynamic interaction of heterochromatin protein hHP1beta with the nucleosome. J. Biol. Chem. 287, 33756-33765 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 33756-33765
    • Munari, F.1
  • 31
    • 79959869345 scopus 로고    scopus 로고
    • Recognition of multivalent histone states associated with heterochromatin by UHRF1 protein
    • Nady, N. et al. Recognition of multivalent histone states associated with heterochromatin by UHRF1 protein. J. Biol. Chem. 286, 24300-24311 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 24300-24311
    • Nady, N.1
  • 32
    • 77950862656 scopus 로고    scopus 로고
    • Proviral silencing in embryonic stem cells requires the histone methyltransferase ESET
    • Matsui, T. et al. Proviral silencing in embryonic stem cells requires the histone methyltransferase ESET. Nature 464, 927-931 (2010).
    • (2010) Nature , vol.464 , pp. 927-931
    • Matsui, T.1
  • 33
    • 84904537943 scopus 로고    scopus 로고
    • Suv39h-dependent H3K9me3 marks intact retrotransposons and silences LINE elements in mouse embryonic stem cells
    • Bulut-Karslioglu, A. et al. Suv39h-dependent H3K9me3 marks intact retrotransposons and silences LINE elements in mouse embryonic stem cells. Mol. Cell 55, 277-290 (2014).
    • (2014) Mol. Cell , vol.55 , pp. 277-290
    • Bulut-Karslioglu, A.1
  • 34
    • 79957844585 scopus 로고    scopus 로고
    • DNA methylation and SETDB1/H3K9me3 regulate predominantly distinct sets of genes, retroelements, and chimeric transcripts in mESCs
    • Karimi, M. M. et al. DNA methylation and SETDB1/H3K9me3 regulate predominantly distinct sets of genes, retroelements, and chimeric transcripts in mESCs. Cell Stem Cell 8, 676-687 (2011).
    • (2011) Cell Stem Cell , vol.8 , pp. 676-687
    • Karimi, M.M.1
  • 35
    • 84953635706 scopus 로고    scopus 로고
    • An ultra-low-input native ChIP-seq protocol for genome-wide profiling of rare cell populations
    • Brind'Amour, J. et al. An ultra-low-input native ChIP-seq protocol for genome-wide profiling of rare cell populations. Nat. Commun. 6, 6033 (2015).
    • (2015) Nat. Commun. , vol.6 , pp. 6033
    • Brind'Amour, J.1
  • 36
    • 84899831694 scopus 로고    scopus 로고
    • Regulation of DNA methylation turnover at LTR retrotransposons and imprinted loci by the histone methyltransferase Setdb1
    • Leung, D. et al. Regulation of DNA methylation turnover at LTR retrotransposons and imprinted loci by the histone methyltransferase Setdb1. Proc. Natl Acad. Sci. USA 111, 6690-6695 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 6690-6695
    • Leung, D.1
  • 37
    • 12144289862 scopus 로고    scopus 로고
    • From silencing to gene expression: Real-time analysis in single cells
    • Janicki, S. M. et al. From silencing to gene expression: real-time analysis in single cells. Cell 116, 683-698 (2004).
    • (2004) Cell , vol.116 , pp. 683-698
    • Janicki, S.M.1
  • 38
    • 80054051524 scopus 로고    scopus 로고
    • A BEN-domain-containing protein associates with heterochromatin and represses transcription
    • Sathyan, K. M., Shen, Z., Tripathi, V., Prasanth, K. V. & Prasanth, S. G. A BEN-domain-containing protein associates with heterochromatin and represses transcription. J. Cell Sci. 124, 3149-3163 (2011).
    • (2011) J. Cell Sci. , vol.124 , pp. 3149-3163
    • Sathyan, K.M.1    Shen, Z.2    Tripathi, V.3    Prasanth, K.V.4    Prasanth, S.G.5
  • 39
    • 1842505448 scopus 로고    scopus 로고
    • In vivo dynamics of Swi6 in yeast: Evidence for a stochastic model of heterochromatin
    • Cheutin, T., Gorski, S. A., May, K. M., Singh, P. B. & Misteli, T. In vivo dynamics of Swi6 in yeast: evidence for a stochastic model of heterochromatin. Mol. Cell Biol. 24, 3157-3167 (2004).
    • (2004) Mol. Cell Biol. , vol.24 , pp. 3157-3167
    • Cheutin, T.1    Gorski, S.A.2    May, K.M.3    Singh, P.B.4    Misteli, T.5
  • 40
    • 0348150714 scopus 로고    scopus 로고
    • Maintenance of stable heterochromatin domains by dynamic HP1 binding
    • Cheutin, T. et al. Maintenance of stable heterochromatin domains by dynamic HP1 binding. Science 299, 721-725 (2003).
    • (2003) Science , vol.299 , pp. 721-725
    • Cheutin, T.1
  • 41
    • 0346525136 scopus 로고    scopus 로고
    • Modulation of heterochromatin protein 1 dynamics in primary Mammalian cells
    • Festenstein, R. et al. Modulation of heterochromatin protein 1 dynamics in primary Mammalian cells. Science 299, 719-721 (2003).
    • (2003) Science , vol.299 , pp. 719-721
    • Festenstein, R.1
  • 42
    • 72149127696 scopus 로고    scopus 로고
    • Heterochromatin protein 1 is extensively decorated with histone code-like post-translational modifications
    • LeRoy, G. et al. Heterochromatin protein 1 is extensively decorated with histone code-like post-translational modifications. Mol. Cell. Proteomics 8, 2432-2442 (2009).
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2432-2442
    • LeRoy, G.1
  • 43
    • 84876285368 scopus 로고    scopus 로고
    • A conformational switch in HP1 releases auto-inhibition to drive heterochromatin assembly
    • Canzio, D. et al. A conformational switch in HP1 releases auto-inhibition to drive heterochromatin assembly. Nature 496, 377-381 (2013).
    • (2013) Nature , vol.496 , pp. 377-381
    • Canzio, D.1
  • 44
    • 84921670393 scopus 로고    scopus 로고
    • Affinity, stoichiometry and cooperativity of heterochromatin protein 1 (HP1) binding to nucleosomal arrays
    • Teif, V. B., Kepper, N., Yserentant, K., Wedemann, G. & Rippe, K. Affinity, stoichiometry and cooperativity of heterochromatin protein 1 (HP1) binding to nucleosomal arrays. J. Phys. Condens. Matter 27, 064110 (2014).
    • (2014) J. Phys. Condens. Matter , vol.27 , pp. 064110
    • Teif, V.B.1    Kepper, N.2    Yserentant, K.3    Wedemann, G.4    Rippe, K.5
  • 45
    • 84901470319 scopus 로고    scopus 로고
    • Mechanisms of functional promiscuity by HP1 proteins
    • Canzio, D., Larson, A. & Narlikar, G. J. Mechanisms of functional promiscuity by HP1 proteins. Trends Cell Biol. 24, 377-386 (2014).
    • (2014) Trends Cell Biol. , vol.24 , pp. 377-386
    • Canzio, D.1    Larson, A.2    Narlikar, G.J.3
  • 46
    • 84875149194 scopus 로고    scopus 로고
    • Regulation of nucleosome dynamics by histone modifications
    • Zentner, G. E. & Henikoff, S. Regulation of nucleosome dynamics by histone modifications. Nat. Struct. Mol. Biol. 20, 259-266 (2013).
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 259-266
    • Zentner, G.E.1    Henikoff, S.2
  • 47
    • 55249118199 scopus 로고    scopus 로고
    • The heterochromatin protein 1 (HP1) family: Put away a bias toward HP1
    • Kwon, S. H. & Workman, J. L. The heterochromatin protein 1 (HP1) family: put away a bias toward HP1. Mol. Cells 26, 217-227 (2008).
    • (2008) Mol. Cells , vol.26 , pp. 217-227
    • Kwon, S.H.1    Workman, J.L.2
  • 48
    • 79952704960 scopus 로고    scopus 로고
    • The changing faces of HP1: From heterochromatin formation and gene silencing to euchromatic gene expression: HP1 acts as a positive regulator of transcription
    • Kwon, S. H. & Workman, J. L. The changing faces of HP1: From heterochromatin formation and gene silencing to euchromatic gene expression: HP1 acts as a positive regulator of transcription. Bioessays 33, 280-289 (2011).
    • (2011) Bioessays , vol.33 , pp. 280-289
    • Kwon, S.H.1    Workman, J.L.2
  • 49
    • 84897042327 scopus 로고    scopus 로고
    • Nucleolus and nuclear periphery: Velcro for heterochromatin
    • Padeken, J. & Heun, P. Nucleolus and nuclear periphery: velcro for heterochromatin. Curr. Opin. Cell Biol. 28, 54-60 (2014).
    • (2014) Curr. Opin. Cell Biol. , vol.28 , pp. 54-60
    • Padeken, J.1    Heun, P.2
  • 51
    • 84862732690 scopus 로고    scopus 로고
    • New insights into nucleosome and chromatin structure: An ordered state or a disordered affair?
    • Luger, K., Dechassa, M. L. & Tremethick, D. J. New insights into nucleosome and chromatin structure: an ordered state or a disordered affair? Nat. Rev. Mol. Cell Biol. 13, 436-447 (2012).
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 436-447
    • Luger, K.1    Dechassa, M.L.2    Tremethick, D.J.3
  • 52
    • 84899837221 scopus 로고    scopus 로고
    • Chromatin without the 30-nm fiber: Constrained disorder instead of hierarchical folding
    • Razin, S. V. & Gavrilov, A. A. Chromatin without the 30-nm fiber: constrained disorder instead of hierarchical folding. Epigenetics 9, 653-657 (2014).
    • (2014) Epigenetics , vol.9 , pp. 653-657
    • Razin, S.V.1    Gavrilov, A.A.2
  • 54
    • 33645325418 scopus 로고    scopus 로고
    • Efficient incorporation of unnatural amino acids into proteins in Escherichia coli
    • Ryu, Y. & Schultz, P. G. Efficient incorporation of unnatural amino acids into proteins in Escherichia coli. Nat. Methods 3, 263-265 (2006).
    • (2006) Nat. Methods , vol.3 , pp. 263-265
    • Ryu, Y.1    Schultz, P.G.2
  • 55
    • 33646242052 scopus 로고    scopus 로고
    • EM measurements define the dimensions of the "30-nm" chromatin fiber: Evidence for a compact, interdigitated structure
    • Robinson, P. J., Fairall, L., Huynh, V. A. & Rhodes, D. EM measurements define the dimensions of the "30-nm" chromatin fiber: evidence for a compact, interdigitated structure. Proc. Natl Acad. Sci. USA 103, 6506-6511 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 6506-6511
    • Robinson, P.J.1    Fairall, L.2    Huynh, V.A.3    Rhodes, D.4
  • 56
    • 0033289822 scopus 로고    scopus 로고
    • Expression and purification of recombinant histones and nucleosome reconstitution
    • Luger, K., Rechsteiner, T. J. & Richmond, T. J. Expression and purification of recombinant histones and nucleosome reconstitution. Methods Mol. Biol. 119, 1-16 (1999).
    • (1999) Methods Mol. Biol. , vol.119 , pp. 1-16
    • Luger, K.1    Rechsteiner, T.J.2    Richmond, T.J.3
  • 57
    • 50349087461 scopus 로고    scopus 로고
    • Specificity of the chromodomain y chromosome family of chromodomains for lysine-methylated ARK(S/T) motifs
    • Fischle, W., Franz, H., Jacobs, S. A., Allis, C. D. & Khorasanizadeh, S. Specificity of the chromodomain Y chromosome family of chromodomains for lysine-methylated ARK(S/T) motifs. J. Biol. Chem. 283, 19626-19635 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 19626-19635
    • Fischle, W.1    Franz, H.2    Jacobs, S.A.3    Allis, C.D.4    Khorasanizadeh, S.5
  • 58
    • 84857966803 scopus 로고    scopus 로고
    • Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography
    • Leitner, A. et al. Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography. Mol. Cell Proteomics 11, 014126 (2012).
    • (2012) Mol. Cell Proteomics , vol.11 , pp. 014126
    • Leitner, A.1
  • 59
    • 84891714984 scopus 로고    scopus 로고
    • Lysine-specific chemical cross-linking of protein complexes and identification of cross-linking sites using LC-MS/MS and the xQuest/xProphet software pipeline
    • Leitner, A., Walzthoeni, T. & Aebersold, R. Lysine-specific chemical cross-linking of protein complexes and identification of cross-linking sites using LC-MS/MS and the xQuest/xProphet software pipeline. Nat. Protoc. 9, 120-137 (2014).
    • (2014) Nat. Protoc. , vol.9 , pp. 120-137
    • Leitner, A.1    Walzthoeni, T.2    Aebersold, R.3
  • 60
    • 84893249767 scopus 로고    scopus 로고
    • Insights into the activation of the helicase Prp43 by biochemical studies and structural mass spectrometry
    • Christian, H., Hofele, R. V., Urlaub, H. & Ficner, R. Insights into the activation of the helicase Prp43 by biochemical studies and structural mass spectrometry. Nucleic Acids Res. 42, 1162-1179 (2014).
    • (2014) Nucleic Acids Res. , vol.42 , pp. 1162-1179
    • Christian, H.1    Hofele, R.V.2    Urlaub, H.3    Ficner, R.4
  • 61
    • 84866117936 scopus 로고    scopus 로고
    • Identification of cross-linked peptides from complex samples
    • Yang, B. et al. Identification of cross-linked peptides from complex samples. Nat. Methods 9, 904-906 (2012).
    • (2012) Nat. Methods , vol.9 , pp. 904-906
    • Yang, B.1
  • 62
    • 84866095385 scopus 로고    scopus 로고
    • Structural probing of a protein phosphatase 2A network by chemical cross-linking and mass spectrometry
    • Herzog, F. et al. Structural probing of a protein phosphatase 2A network by chemical cross-linking and mass spectrometry. Science 337, 1348-1352 (2012).
    • (2012) Science , vol.337 , pp. 1348-1352
    • Herzog, F.1
  • 63
    • 33644873467 scopus 로고    scopus 로고
    • Two-step cross-linking method for identification of NF-kappaB gene network by chromatin immunoprecipitation
    • Nowak, D. E., Tian, B. & Brasier, A. R. Two-step cross-linking method for identification of NF-kappaB gene network by chromatin immunoprecipitation. Biotechniques 39, 715-725 (2005).
    • (2005) Biotechniques , vol.39 , pp. 715-725
    • Nowak, D.E.1    Tian, B.2    Brasier, A.R.3
  • 64
    • 79953177468 scopus 로고    scopus 로고
    • Aligning short sequencing reads with Bowtie
    • Chapter 11, Unit 11.7
    • Langmead, B. Aligning short sequencing reads with Bowtie. Curr. Protoc. Bioinformatics Chapter 11, Unit 11.7 (2010).
    • (2010) Curr. Protoc. Bioinformatics
    • Langmead, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.