Newcastle Cancer Centre at the Northern Institute for Cancer Research, Newcastle University, Newcastle upon Tyne, England.
Epigenetics. 2020 Jan-Feb;15(1-2):26-31. doi: 10.1080/15592294.2019.1649529. Epub 2019 Aug 1.
Although central to regulating the access to genetic information, most lysine methyltransferases remain poorly characterised relative to other family of enzymes. Herein, I report new substrates for the lysine methyltransferase SETD6. Based on the SETD6-catalysed site on the histone variant H2AZ, I identified similar sequences in the canonical histones H2A, H3, and H4 that are modified by SETD6 , and putative non-histone substrates. I herein expend the repertoire of substrates for methylation by SETD6.
尽管赖氨酸甲基转移酶在调节遗传信息的获取方面至关重要,但与其他酶家族相比,它们的特征仍然很差。在此,我报告了赖氨酸甲基转移酶 SETD6 的新底物。基于 SETD6 催化组蛋白变体 H2AZ 上的位点,我在经典组蛋白 H2A、H3 和 H4 中鉴定出了被 SETD6 修饰的类似序列,以及潜在的非组蛋白底物。在此,我扩展了 SETD6 甲基化的底物谱。