Childrens Hospital Boston, Harvard Medical School, 3 Blackfan Circle, Boston, MA 02115, USA.
Department of Biochemistry and Microbiology, Marshall University, One John Marshall Dr., Huntington, WV 25755, USA.
Biochem Biophys Res Commun. 2014 Jul 18;450(1):802-7. doi: 10.1016/j.bbrc.2014.06.050. Epub 2014 Jun 19.
Post-translational modifications (PTMs) of histones such as phosphorylation, acetylation, and ubiquitination, collectively referred to as the "histone-code", have been known to regulate gene expression and chromatin condensation for over a decade. They are also implicated in processes such as DNA repair and apoptosis. However, the study of the phosphorylation of histones has been mainly focused on chromosome condensation and mitosis. Therefore, the phosphorylation of histones in apoptosis is not fully understood. It was recently demonstrated by Tang et al. that histones are released from nucleosome during apoptosis, an observation that is in agreement with our findings. In addition to the release of histones, the dephosphorylation of histone H3 at Thr-3 and Ser-10 was observed during apoptosis in some cancer cells. Our data suggest that the modification and release of histones could serve markers of apoptosis in human cancer cells. We also suggest that the released histones, especially H3, could be translocated to mitochondria during apoptosis.
组蛋白的翻译后修饰（PTMs），如磷酸化、乙酰化和泛素化等，统称为“组蛋白密码”，它们已被证实可以调节基因表达和染色质凝聚超过十年。它们还涉及到 DNA 修复和细胞凋亡等过程。然而，组蛋白磷酸化的研究主要集中在染色体凝聚和有丝分裂上。因此，细胞凋亡中组蛋白的磷酸化还不完全清楚。最近，Tang 等人证明了细胞凋亡过程中组蛋白从核小体中释放出来，这一观察结果与我们的发现一致。除了组蛋白的释放之外，在一些癌细胞的细胞凋亡过程中还观察到组蛋白 H3 的 Thr-3 和 Ser-10 的去磷酸化。我们的数据表明，组蛋白的修饰和释放可以作为人癌细胞凋亡的标志物。我们还提出，释放的组蛋白，特别是 H3，可能在细胞凋亡过程中转移到线粒体。
