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Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
Published on: November 30, 2018
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GAS41 Recognizes Diacetylated Histone H3 through a Bivalent Binding Mode
Hyo Je Cho1, Hao Li1,2, Brian M Linhares1
1Department of Pathology , University of Michigan , Ann Arbor , Michigan 48109 , United States.
ACS Chemical Biology
|August 4, 2018
Summary
Growth arrest specific 41 (GAS41), a YEATS family protein, recognizes acetylated histones. Full-length GAS41 binds diacetylated histones with higher affinity, suggesting a unique histone reader role.
Area of Science:
- Biochemistry
- Molecular Biology
- Epigenetics
Background:
- GAS41 is a chromatin-associated protein in the YEATS family.
- It recognizes acetyl-lysine on histones and possesses a coiled-coil domain for dimerization.
Purpose of the Study:
- To characterize the binding specificity of the GAS41 YEATS domain.
- To investigate the binding mode of full-length, dimeric GAS41 to acetylated histones.
Main Methods:
- Peptide binding assays to determine GAS41 YEATS domain specificity.
- Crystal structure determination of GAS41 YEATS domain complexed with diacetylated histone peptides.
Main Results:
- GAS41 YEATS domain preferentially binds to acetylated H3K18 and H3K27 peptides.
- Full-length dimeric GAS41 exhibits enhanced affinity for diacetylated H3 peptides via bivalent binding.
- Crystal structure reveals the molecular basis for diacetylated histone recognition.
Conclusions:
- GAS41 functions as a reader of diacetylated histones.
- The dimeric nature of GAS41 contributes to its unique binding properties and affinity for specific histone marks.
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