Ascending the nucleosome face: Recognition and function of structured domains in the histone H2A-H2B dimer

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• 作者：John J. Wyrick^a ; ^b ; ^{jwyrick@wsu.edu} ; McKenna N.M. Kyriss^a ; William B. Davis^a
• 关键词：Histone H2A and H2B ; Acidic patch ; Nucleosome recognition ; Sir3 ; Post-translational modification
• 刊名：Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms
• 出版年：2012
• 期刊代码：P11_18749399
• 类别：bio
• 出版时间：August, 2012
• 卷：1819
• 期：8
• 页码：892-901
• 文件大小：1225 K

摘要

Research over the past decade has greatly expanded our understanding of the nucleosome's role as a dynamic hub that is specifically recognized by many regulatory proteins involved in transcription, silencing, replication, repair, and chromosome segregation. While many of these nucleosome interactions are mediated by post-translational modifications in the disordered histone tails, it is becoming increasingly apparent that structured regions of the nucleosome, including the histone fold domains, are also recognized by numerous regulatory proteins. This review will focus on the recognition of structured domains in the histone H2A-H2B dimer, including the acidic patch, the H2A docking domain, the H2B 伪3-伪C helices, and the HAR/HBR domains, and will survey the known biological functions of histone residues within these domains. Novel post-translational modifications and trans-histone regulatory pathways involving structured regions of the H2A-H2B dimer will be highlighted, along with the role of intrinsic disorder in the recognition of structured nucleosome regions.