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000293458 1001_ $$0P:(DE-HGF)0$$aTallant, Cynthia$$b0
000293458 245__ $$aMolecular Basis of Histone Tail Recognition by Human TIP5 PHD Finger and Bromodomain of the Chromatin Remodeling Complex NoRC
000293458 260__ $$aLondon [u.a.]$$bElsevier Science$$c2015
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000293458 520__ $$aBinding 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.
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000293458 536__ $$0G:(EU-Grant)264257$$aIDPBYNMR - High resolution tools to understand the functional role of protein intrinsic disorder (264257)$$c264257$$fFP7-PEOPLE-2010-ITN$$x2
000293458 536__ $$0G:(DE-HGF)POF3-6G3$$a6G3 - PETRA III (POF3-622)$$cPOF3-622$$fPOF III$$x3
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000293458 7001_ $$0P:(DE-H253)PIP1016688$$aValentini, Erica$$b1
000293458 7001_ $$aFedorov, Oleg$$b2
000293458 7001_ $$aOvervoorde, Lois$$b3
000293458 7001_ $$aFerguson, Fleur M.$$b4
000293458 7001_ $$aFilippakopoulos, Panagis$$b5
000293458 7001_ $$0P:(DE-HGF)0$$aSvergun, Dmitri I.$$b6
000293458 7001_ $$aKnapp, Stefan$$b7
000293458 7001_ $$0P:(DE-HGF)0$$aCiulli, Alessio$$b8$$eCorresponding author
000293458 773__ $$0PERI:(DE-600)2031189-8$$a10.1016/j.str.2014.10.017$$gVol. 23, no. 1, p. 80 - 92$$n1$$p80 - 92$$tStructure$$v23$$x0969-2126$$y2015
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