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@ARTICLE{Tallant:293458,
      author       = {Tallant, Cynthia and Valentini, Erica and Fedorov, Oleg and
                      Overvoorde, Lois and Ferguson, Fleur M. and
                      Filippakopoulos, Panagis and Svergun, Dmitri I. and Knapp,
                      Stefan and Ciulli, Alessio},
      title        = {{M}olecular {B}asis of {H}istone {T}ail {R}ecognition by
                      {H}uman {TIP}5 {PHD} {F}inger and {B}romodomain of the
                      {C}hromatin {R}emodeling {C}omplex {N}o{RC}},
      journal      = {Structure},
      volume       = {23},
      number       = {1},
      issn         = {0969-2126},
      address      = {London [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {PUBDB-2016-00547},
      pages        = {80 - 92},
      year         = {2015},
      abstract     = {Binding of the chromatin remodeling complex NoRCto RNA
                      complementary to the rDNA promoter medi-ates transcriptional
                      repression. TIP5, the largest sub-unit of NoRC, is involved
                      in recruitment to rDNA byinteractions with promoter-bound
                      TTF-I, pRNA, andacetylation of H4K16. TIP5 domains that
                      recognizeposttranslational modifications on histones
                      areessential for recruitment of NoRC to chromatin, buthow
                      these reader modules recognize site-specifichistone tails
                      has remained elusive. Here, we reportcrystal structures of
                      PHD zinc finger and bromodo-mains from human TIP5 and BAZ2B
                      in free form andbound to H3 and/or H4 histones. PHD finger
                      functionsas an independent structural module in
                      recognizingunmodified H3 histone tails, and the
                      bromodomainprefers H3 and H4 acetylation marks followed by
                      akey basic residue, KacXXR. Further low-resolutionanalyses
                      of PHD-bromodomain modules providemolecular insights into
                      their trans histone tail recogni-tion, required for
                      nucleosome recruitment and tran-scriptional repression of
                      the NoRC complex.},
      cin          = {EMBL / EMBL-User},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-20120731 / I:(DE-H253)EMBL-User-20120814},
      pnm          = {899 - ohne Topic (POF3-899) / BIOSTRUCT-X - Transnational
                      access and enhancement of integrated Biological Structure
                      determination at synchrotron X-ray radiation facilities
                      (283570) / IDPBYNMR - High resolution tools to understand
                      the functional role of protein intrinsic disorder (264257) /
                      6G3 - PETRA III (POF3-622)},
      pid          = {G:(DE-HGF)POF3-899 / G:(EU-Grant)283570 /
                      G:(EU-Grant)264257 / G:(DE-HGF)POF3-6G3},
      experiment   = {EXP:(DE-H253)DORISIII(machine)-20150101 /
                      EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000347469500013},
      pubmed       = {pmid:25533489},
      doi          = {10.1016/j.str.2014.10.017},
      url          = {https://bib-pubdb1.desy.de/record/293458},
}