| Literature DB >> 30071723 |
Hyo Je Cho1, Hao Li1,2, Brian M Linhares1, EunGi Kim1, Juliano Ndoj1, Hongzhi Miao1, Jolanta Grembecka1,2, Tomasz Cierpicki1,2.
Abstract
GAS41 is a chromatin-associated protein that belongs to the YEATS family and is involved in the recognition of acetyl-lysine in histone proteins. A unique feature of GAS41 is the presence of a C-terminal coiled-coil domain, which is responsible for protein dimerization. Here, we characterized the specificity of the GAS41 YEATS domain and found that it preferentially binds to acetylated H3K18 and H3K27 peptides. Interestingly, we found that full-length, dimeric GAS41 binds to diacetylated H3 peptides with an enhanced affinity when compared to those for monoacetylated peptides, through a bivalent binding mode. We determined the crystal structure of the GAS41 YEATS domain with H3K23acK27ac to visualize the molecular basis of diacetylated histone binding. Our results suggest a unique binding mode in which full-length GAS41 is a reader of diacetylated histones.Entities:
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Year: 2018 PMID： 30071723 PMCID： PMC6611172 DOI： 10.1021/acschembio.8b00674
Source DB: PubMed Journal: ACS Chem Biol ISSN： 1554-8929 Impact factor: 5.100