%0 Journal Article
%A Tallant, Cynthia
%A Valentini, Erica
%A Fedorov, Oleg
%A Overvoorde, Lois
%A Ferguson, Fleur M.
%A Filippakopoulos, Panagis
%A Svergun, Dmitri I.
%A Knapp, Stefan
%A Ciulli, Alessio
%T Molecular Basis of Histone Tail Recognition by Human TIP5 PHD Finger and Bromodomain of the Chromatin Remodeling Complex NoRC
%J Structure
%V 23
%N 1
%@ 0969-2126
%C London [u.a.]
%I Elsevier Science
%M PUBDB-2016-00547
%P 80 - 92
%D 2015
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000347469500013
%$ pmid:25533489
%R 10.1016/j.str.2014.10.017
%U https://bib-pubdb1.desy.de/record/293458