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@ARTICLE{Danilenko:874827,
      author       = {Danilenko, Nataliya and Lercher, Lukas and Kirkpatrick,
                      John and Gabel, Frank and Codutti, Luca and Carlomagno,
                      Teresa},
      title        = {{H}istone chaperone exploits intrinsic disorder to switch
                      acetylation specificity},
      journal      = {Nature Communications},
      volume       = {10},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2020-01660},
      pages        = {3435},
      year         = {2019},
      abstract     = {Histones, the principal protein components of chromatin,
                      contain long disordered sequences, which are extensively
                      post-translationally modified. Although histone chaperones
                      are known to control both the activity and specificity of
                      histone-modifying enzymes, the mechanisms promoting
                      modification of highly disordered substrates, such as
                      lysine-acetylation within the N-terminal tail of histone H3,
                      are not understood. Here, to understand how histone
                      chaperones Asf1 and Vps75 together promote H3
                      K9-acetylation, we establish the solution structural model
                      of the acetyltransferase Rtt109 in complex with Asf1 and
                      Vps75 and the histone dimer H3:H4. We show that Vps75
                      promotes K9-acetylation by engaging the H3 N-terminal tail
                      in fuzzy electrostatic interactions with its disordered
                      C-terminal domain, thereby confining the H3 tail to a wide
                      central cavity faced by the Rtt109 active site. These fuzzy
                      interactions between disordered domains achieve localization
                      of lysine residues in the H3 tail to the catalytic site with
                      minimal loss of entropy, and may represent a common
                      mechanism of enzymatic reactions involving highly disordered
                      substrates},
      cin          = {JCNS-FRM-II / JCNS-2 / MLZ / JCNS-1},
      ddc          = {500},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-2-20110106 / I:(DE-588b)4597118-3 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6G15 - FRM II / MLZ (POF3-6G15)},
      pid          = {G:(DE-HGF)POF3-6G4 / G:(DE-HGF)POF3-6G15},
      experiment   = {EXP:(DE-MLZ)KWS1-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31387991},
      UT           = {WOS:000478866600001},
      doi          = {10.1038/s41467-019-11410-7},
      url          = {https://juser.fz-juelich.de/record/874827},
}