The Taf14 YEATS domain is a reader of histone crotonylation
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منابع مشابه
The Taf14 YEATS domain is a reader of histone crotonylation
The discovery of new histone modifications is unfolding at startling rates; however, the identification of effectors capable of interpreting these modifications has lagged behind. Here we report the YEATS domain as an effective reader of histone lysine crotonylation, an epigenetic signature associated with active transcription. We show that the Taf14 YEATS domain engages crotonyllysine via a un...
متن کاملYEATS domain: Linking histone crotonylation to gene regulation
Recent research reveals that the YEATS domains preferentially recognize crotonylated lysines on histones. Here, we discuss the molecular mechanisms that enable this recognition and the biological significances of this interaction. The dynamics of histone crotonylation and its potential roles in the regulation of gene expression will also be discussed.
متن کاملSolution structure of the Taf14 YEATS domain and its roles in cell growth of Saccharomyces cerevisiae.
Chromatin modifications play important roles in cellular biological process. A novel conserved domain family, YEATS, has been discovered in a variety of eukaryotic species ranging from yeasts to humans. Taf14, which is involved in a few protein complexes of chromatin remodelling and gene transcription, and is essential for keeping chromosome stability, regular cell growth and transcriptional re...
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Decades of research has explored the epigenetic control of gene expression and the impact of histone post-translational modifications (PTMs), such as acetylation, on chromatin remodeling. Indeed, the writers, readers, and erasers of lysine acetylation are increasingly well understood. Recent studies have added crotonylation, butyrylation, and propionylation to the types of acylations by which h...
متن کاملIdentification of 67 Histone Marks and Histone Lysine Crotonylation as a New Type of Histone Modification
We report the identification of 67 previously undescribed histone modifications, increasing the current number of known histone marks by about 70%. We further investigated one of the marks, lysine crotonylation (Kcr), confirming that it represents an evolutionarily-conserved histone posttranslational modification. The unique structure and genomic localization of histone Kcr suggest that it is m...
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ژورنال
عنوان ژورنال: Nature Chemical Biology
سال: 2016
ISSN: 1552-4450,1552-4469
DOI: 10.1038/nchembio.2065