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Updated: Jun 10, 2026
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Chromatin Immunoprecipitation (ChIP) of Histone Modifications from Saccharomyces cerevisiae
Published on: December 29, 2017
Reading chromatin: insights from yeast into YEATS domain structure and function
Julia M Schulze1, Alice Y Wang, Michael S Kobor
1Department of Medical Genetics, University of British Columbia, Centre for Molecular Medicine and Therapeutics, Child and Family Research Institute, Vancouver, BC, CA.
Epigenetics
|July 27, 2010
Summary
The YEATS domain in yeast protein Yaf9 has a structure suggesting it binds acetyl-lysine. This finding advances understanding of chromatin-modifying complexes and potential interactions.
Area of Science:
- Molecular Biology
- Epigenetics
- Structural Biology
Background:
- Chromatin-modifying complexes utilize signature domains to interact with histone modifications.
- The YEATS domain is an evolutionarily conserved module found in various chromatin and transcription complexes.
- Yaf9, a yeast protein, contains a YEATS domain and is part of key complexes like SWR1-C and NuA4.
Purpose of the Study:
- To investigate the structural characteristics of the YEATS domain from the yeast protein Yaf9.
- To explore the potential function of the Yaf9 YEATS domain in protein interactions.
Main Methods:
- Three-dimensional structure determination of the Yaf9 YEATS domain.
- Structural analysis to identify functional regions.
Main Results:
- The solved structure of the Yaf9 YEATS domain revealed three distinct structural regions.
- One region features a shallow groove, potentially acting as an acetyl-lysine binding pocket.
Conclusions:
- The Yaf9 YEATS domain's structure suggests a role in binding acetyl-lysine modifications.
- This structural insight raises questions about the Yaf9 YEATS domain's protein interaction partners and functional mechanisms.
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