YEATS Domain—A Histone Acylation Reader in Health and Disease. Issue 13 (30th June 2017)

• Record Type: Journal Article
• Authors: Zhao, Dan; Li, Yuanyuan; Xiong, Xiaozhe; Chen, Zhonglei; Li, Haitao
• Is Part Of: Journal of molecular biology. Volume 429:Issue 13(2017)
• Page Start: 1994
• Page End: 2002
• Publication Date: 2017-06-30
• Subjects: PTMs post-translational modifications -- YEATS Yaf9, ENL, AF9, Taf14, Sas5 -- DPF double plant homeodomain finger -- acyl-CoA acyl-coenzyme A -- Kac lysine acetylation -- Kcr lysine crotonylation -- Khib lysine 2-hydroxyisobutyrylation -- Kpr lysine propionylation -- Kbu lysine butyrylation -- GAS41 glioma amplified sequence 41 -- MLL mixed lineage leukemia -- SEC super elongation complex; histone acylation -- YEATS domain -- lysine crotonylation -- aromatic-π stacking -- epigenetic regulation; Molecular biology -- Periodicals; Biology -- Periodicals; Biochemistry -- Periodicals; Bacteriology -- Periodicals; Molecular Biology -- Periodicals; Biochemistry -- Periodicals; Biologie moléculaire -- Périodiques; Biologie -- Périodiques; Biochimie -- Périodiques; Moleculaire biologie; Biochemistry; Biology; Molecular biology; Periodicals; 572.805
• DOI: 10.1016/j.jmb.2017.03.010
• Languages: English
• ISSNs: 0022-2836

Abstract

Abstract: Histone post-translational modifications (PTMs) carry an epigenetic layer of message to regulate diverse cellular processes at the chromatin level. Many of these PTMs are selectively recognized by dedicated effector proteins for normal cell growth and development, while dysregulation of these recognition events is often implicated in human diseases, notably cancer. Thus, it is fundamentally important to elucidate the regulatory mechanism(s) underlying the readout of PTMs on histones. The Y af9, E NL, A F9, T af14, S as5 (YEATS) domain is an emerging reader module that selectively recognizes histone lysine acylation with a preference for crotonylation over acetylation. In the review, we discuss the recognition of histone acylations by the YEATS domain and the biological significance of this readout from multiple perspectives. Graphical Abstract: Highlights: YEATS reads a repertoire of histone acylations with a preference for crotonylation. YEATS couples histone acylation readout to active transcription. An aromatic-π interaction contributes to crotonylation preference by YEATS. Dysfunction of YEATS domain is linked to multiple human diseases.