GAS41 Recognizes Diacetylated Histone H3 through a Bivalent Binding Mode
| Autor: | EunGi Kim, Brian M. Linhares, Tomasz Cierpicki, Hao Li, Hyo Je Cho, Hongzhi Miao, Jolanta Grembecka, Juliano Ndoj |
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| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular 0301 basic medicine Stereochemistry Biochemistry Article Bivalent (genetics) Histones 03 medical and health sciences Histone H3 0302 clinical medicine Transcription (biology) Humans Protein Interaction Domains and Motifs Protein Dimerization Histone binding Binding Sites biology Chemistry Acetylation General Medicine HEK293 Cells 030104 developmental biology Histone biology.protein Molecular Medicine Protein Multimerization 030217 neurology & neurosurgery Protein Binding Transcription Factors |
| Zdroj: | ACS Chemical Biology. 13:2739-2746 |
| ISSN: | 1554-8937 1554-8929 |
| DOI: | 10.1021/acschembio.8b00674 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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