蛋白质精氨酸甲基转移酶PRMT7催化活性的研究进展
| 作者: |
1张培准,
2何化成,
2高勤雨
1 北京交通大学中国产业安全研究中心，北京 100044 2 中国科学院遗传与发育生物学研究所，北京 100101 |
| 通讯: |
张培准
Email: zhunzp2006@163.com |
| DOI: | 10.3978/j.issn.2095-6959.2014.05.037 |
摘要
蛋白质精氨酸甲基转移酶（protein arginine methyltransferase，PRMTs）广泛存在于真核生物细胞 中，主要通过翻译后修饰底物蛋白参与生命过程的调控。PRMT7是PRMTs家族的重要成员，目前 已发现其参与调控基因表达、剪接体组装、DNA损伤修复、细胞迁移与分化、细胞药物敏感性和 个体发育等多个过程。对于PRMT7的催化活性，目前一直有较大争议。有些研究人员认为目前仅 能确认PRMT7可以单甲基化修饰蛋白质底物；另一些研究人员则认为PRMT7既可以单甲基化修饰 蛋白质底物，也可以双甲基化修饰蛋白质底物。
关键词：
蛋白质精氨酸甲基转移酶
单甲基化
对称性双甲基化
Progression of catalytic activity of protein arginine methyltransferase 7
CorrespondingAuthor: ZHANG Peizhun Email: zhunzp2006@163.com
DOI: 10.3978/j.issn.2095-6959.2014.05.037
Abstract
Protein arginine methyltransferase (PRMTs) family is familiar in eukaryotic cells, which regulates biological process by modifying substrate proteins after translation. PRMT7 is an important member of PRMTs family, and it has been implicated in roles of transcriptional regulation, RNA splicing, DNA damage repair, metastasis, cell differentiation, cellular sensitivity to drugs and individual development. The type of methylation reaction catalyzed by PRMT7 has been under debate up recently. Some biologists reported that PRMT7 could only mono-methylate substrate proteins; but some other biologists believed that PRMT7 could mono-methylate and di-methylate substrate proteins.