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Molecular basis of histone tail recognition by human TIP5 PHD finger and bromodomain of the chromatin remodeling complex NoRC

DOI: 10.1016/j.str.2014.10.017 DOI Help
PMID: 25533489 PMID Help

Authors: Cynthia Tallant (University of Cambridge; University of Oxford) , Erica Valentini (European Molecular Biology Laboratory) , Oleg Fedorov (University of Oxford) , Lois Overvoorde (University of Cambridge) , Fleur m. Ferguson (University of Cambridge) , Panagis Filippakopoulos (University of Oxford) , Dmitri i. Svergun (European Molecular Biology Laboratory) , Stefan Knapp (University of Oxford) , Alessio Ciulli (University of Cambridge)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Structure , VOL 23 (1) , PAGES 80 - 92

State: Published (Approved)
Published: January 2015
Diamond Proposal Number(s): 8046 , 7141

Open Access Open Access

Abstract: Binding of the chromatin remodeling complex NoRC to RNA complementary to the rDNA promoter mediates transcriptional repression. TIP5, the largest subunit of NoRC, is involved in recruitment to rDNA by interactions with promoter-bound TTF-I, pRNA, and acetylation of H4K16. TIP5 domains that recognize posttranslational modifications on histones are essential for recruitment of NoRC to chromatin, but how these reader modules recognize site-specific histone tails has remained elusive. Here, we report crystal structures of PHD zinc finger and bromodomains from human TIP5 and BAZ2B in free form and bound to H3 and/or H4 histones. PHD finger functions as an independent structural module in recognizing unmodified H3 histone tails, and the bromodomain prefers H3 and H4 acetylation marks followed by a key basic residue, KacXXR. Further low-resolution analyses of PHD-bromodomain modules provide molecular insights into their trans histone tail recognition, required for nucleosome recruitment and transcriptional repression of the NoRC complex.

Subject Areas: Biology and Bio-materials

Instruments: I02-Macromolecular Crystallography , I04-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography

Other Facilities: DESY

Added On: 15/02/2015 20:39


Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)