Andrews Forest H, Shanle Erin K, Strahl Brian D, Kutateladze Tatiana G
a Department of Pharmacology , University of Colorado School of Medicine , Aurora , CO , USA.
b Department of Biochemistry & Biophysics , The University of North Carolina School of Medicine , Chapel Hill , NC , USA.
Transcription. 2016;7(1):14-20. doi: 10.1080/21541264.2015.1125987.
The YEATS domains of AF9 and Taf14 have recently been found to recognize the histone H3K9ac modification. In this commentary, we discuss the mechanistic and biological implications of this interaction. We compare structures of the YEATS-H3K9ac complexes the highlighting a novel mechanism for the acetyllysine recognition through the aromatic cage. We also summarize the latest findings underscoring a critical role of the acetyllysine binding function of AF9 and Taf14 in transcriptional regulation and DNA repair.
最近发现AF9和Taf14的YEATS结构域可识别组蛋白H3K9ac修饰。在本述评中,我们讨论了这种相互作用的机制和生物学意义。我们比较了YEATS-H3K9ac复合物的结构,突出了通过芳香笼识别乙酰赖氨酸的新机制。我们还总结了最新发现,强调了AF9和Taf14的乙酰赖氨酸结合功能在转录调控和DNA修复中的关键作用。