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Enzyme shown to help protect genomic stability

n histones, molecules that have attracted increasing attention from scientists as they move beyond sequencing the human genome to trying to better understand how DNA is managed and its activity regulated. Histones are small proteins around which DNA is coiled to create structures called nucleosomes. Compact strings of nucleosomes, then, form into chromatin, the substructure of chromosomes. In many cases, when the DNA is tightly wrapped around the histones, the genes cannot be accessed and their expression is repressed. When the coils of DNA around the histones are loosened or the histone molecules are altered, the genes become available for expression.

It is the complex activity governing this process to which Ubp10 contributes. Enzymatic modifications to histones control DNA activation or silencing through the addition or removal of acetyl, methyl, and ubiquitin molecules in prescribed sequences and patterns. One job of Ubp10, as identified in this study, is to remove ubiquitin from certain histones where ubiquitin is associated with gene activation and to maintain low levels of the ubiquitin molecule at those sites.

Interestingly, Ubp10 appears to work similarly and in concert with another enzyme called Sir2, which removes acetyl molecules from histones. Sir2 has also been associated with promoting genomic stability, and some studies have linked it intriguingly to the aging process. Some studies, for example, have suggested that low-calorie diets that extend life also boost Sir2 activity dramatically.


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Source:The Wistar Institute


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