Journal
STRUCTURE
Volume 23, Issue 1, Pages 80-92Publisher
CELL PRESS
DOI: 10.1016/j.str.2014.10.017
Keywords
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Funding
- UK Biotechnology and Biological Sciences Research Council [BB/G023123/1, BB/J001201/1]
- Federation of European Biochemical Societies short-term fellowship [04-11-12-10]
- European Commission [283570]
- AbbVie
- Bayer
- Boehringer Ingelheim
- Canada Foundation for Innovation
- Canadian Institutes for Health Research
- Genome Canada
- GlaxoSmithKline
- Janssen
- Lilly Canada
- Novartis Research Foundation
- Ontario Ministry of Economic Development and Innovation
- Pfizer
- Takeda
- Wellcome Trust [092809/Z/10/Z]
- European Commission FP7 Marie Curie grant IDPbyNMR [264257]
- Welcome Trust Career Development Fellowship [095751/Z/11/Z]
- Biotechnology and Biological Sciences Research Council [BB/G023123/1, BB/J001201/2, BB/J001201/1, 980607, BB/G023123/2] Funding Source: researchfish
- BBSRC [BB/G023123/2, BB/J001201/1, BB/G023123/1, BB/J001201/2] Funding Source: UKRI
- Wellcome Trust [095751/Z/11/Z] Funding Source: Wellcome Trust
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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.
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