Last year marked the 10-year anniversary of the 'histone code' hypothesis, which formally proposed that combinatorial post-translational modifications (PTMs) on histone proteins govern the diverse activities associated with eukary-otic DNA [1,2]. In the intervening decade, significant advancements have been made in our understanding of chromatin biology. For example, more than 60 sites of modification on histones have been identified (which include acetylation, phosphorylation, ubiquitination, methylation and others), as have a variety of specialized effector domains that recognize these histone PTMs [3,4]. The collective results of many studies show that histone PTMs contribute to a wide range of biological processes, including gene transcription, DNA replication and DNA repair. These advances, however, would not have been possible without the creation of PTM-specific histone antibodies [5,6]. Histone antibodies have become the predominant tool for chromatin research, and are ubiquitously used to understand how histone PTMs regulate chromatin structure and function.
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