At the very least it is surprising that especially in light of its function as a posttranslational modification (PTM) – which can sweep away en masse all other modifications – histone clipping is not being picked up by the broader scientific community at a time when over 5,000 papers are published on histones every year. Strangely, however, this promise was again not fulfilled. While histone proteolysis nearly disappeared from the publication record during the 90s and early 2000 s, a second wave of papers seemed to be upon us by around 2010, with the publication of the first evidence of the epigenetic potential of histone clipping in mouse and yeast. A brief history of histone proteolysis shows that it has consistently been treated in stepmotherly fashion by the scientific community.Īs the first papers started to suggest that histone truncation might greatly impact transcription, a sudden surge of biochemical studies on nuclear histone‐degrading enzymes occurred during the 70s and 80s (partially reviewed in ). Together this has created a very confusing amalgam of recent reports in which findings with often little biological coherence are continuously being cross‐referenced. While evidence of such epigenetic potential is only now gradually emerging, it is increasingly becoming clear that histones are also being degraded at much higher rates than was initially anticipated. Not surprisingly, many subsequent reports have alluded to the theoretical transcriptional implications of such enzymatic reaction because of the central role that histones play in DNA packaging and epigenetic regulation. Histone proteolysis has a long history of disregard Proteolysis associated with nucleosomes was described about 50 years ago, even before histones received their current nomenclature. In conclusion, we emphasize the significance of reviving the study of histone proteolysis both from a biological and an experimental perspective. Finally, unanticipated histone proteolysis has probably left a mark on many studies of histones in the past. Given the importance of histone modifications in epigenetic regulation we further elaborate on the different ways in which histone proteolysis could play a role in epigenetics. However, the authors often not clearly distinguish or determine whether degradation or clipping was studied. Since the first report decades ago, proteolysis has been found in a broad spectrum of eukaryotic organisms. Our initial observation is that these two different classes are very hard to distinguish both experimentally and biologically, because they can both be mediated by the same enzymes. We propose for the first time to divide histone proteolysis into “histone degradation” and the epigenetically connoted “histone clipping”.
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