Molecular Basis of Histone Tail Recognition by Human TIP5 PHD Finger and Bromodomain of the Chromatin Remodeling Complex NoRC

Tallant, Cynthia; Svergun, Dmitri I.; Filippakopoulos, Panagis; Ferguson, Fleur M.; Fedorov, Oleg; Valentini, Erica; Knapp, Stefan; Overvoorde, Lois; Ciulli, Alessio

doi:10.1016/j.str.2014.10.017

Journal Article

PUBDB-2016-00547

Molecular Basis of Histone Tail Recognition by Human TIP5 PHD Finger and Bromodomain of the Chromatin Remodeling Complex NoRC

Tallant, C. ; Valentini, E.Extern* ; Fedorov, O. ; Overvoorde, L. ; Ferguson, F. ; Filippakopoulos, P. ; Svergun, D.EMBL* ; Knapp, S. ; Ciulli, A. (Corresponding author)

2015
Elsevier Science London [u.a.]

Structure 23(1), 80 - 92 (2015) [10.1016/j.str.2014.10.017]

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Please use a persistent id in citations: doi:10.1016/j.str.2014.10.017

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.

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