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| Home > Publications database > Molecular Basis of Histone Tail Recognition by Human TIP5 PHD Finger and Bromodomain of the Chromatin Remodeling Complex NoRC > print |
| Home > Publications database > Molecular Basis of Histone Tail Recognition by Human TIP5 PHD Finger and Bromodomain of the Chromatin Remodeling Complex NoRC > print |
| 001 | 293458 | ||
| 005 | 20250730113916.0 | ||
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| 100 | 1 | _ | |a Tallant, Cynthia |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Molecular Basis of Histone Tail Recognition by Human TIP5 PHD Finger and Bromodomain of the Chromatin Remodeling Complex NoRC |
| 260 | _ | _ | |a London [u.a.] |c 2015 |b Elsevier Science |
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| 520 | _ | _ | |a 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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| 700 | 1 | _ | |a Valentini, Erica |0 P:(DE-H253)PIP1016688 |b 1 |
| 700 | 1 | _ | |a Fedorov, Oleg |b 2 |
| 700 | 1 | _ | |a Overvoorde, Lois |b 3 |
| 700 | 1 | _ | |a Ferguson, Fleur M. |b 4 |
| 700 | 1 | _ | |a Filippakopoulos, Panagis |b 5 |
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| 700 | 1 | _ | |a Ciulli, Alessio |0 P:(DE-HGF)0 |b 8 |e Corresponding author |
| 773 | _ | _ | |a 10.1016/j.str.2014.10.017 |g Vol. 23, no. 1, p. 80 - 92 |0 PERI:(DE-600)2031189-8 |n 1 |p 80 - 92 |t Structure |v 23 |y 2015 |x 0969-2126 |
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