非传统翻译是 UFMylation 及其他的关键。
Nontraditional translation is the key to UFMylation and beyond.
机构信息
Zhejiang Provincial Key Laboratory for Drug Evaluation and Clinical Research, First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China.
Life Sciences Institute, Zhejiang University, Hangzhou, Zhejiang, China.
出版信息
J Biol Chem. 2022 Oct;298(10):102431. doi: 10.1016/j.jbc.2022.102431. Epub 2022 Aug 28.
The Ubiquitin-fold modifier 1 (Ufm1) is a ubiquitin-like protein that can also be conjugated to protein substrates and subsequently alter their fates. Both UFMylation and de-UFMylation are mediated by Ufm1-specific proteases (UFSPs). In humans, it is widely believed that UFSP2 is the only active Ufm1 protease involved in Ufm1 maturation and de-UFMylation, whereas UFSP1 is thought to be inactive. Here, Liang et al. provide strong evidence showing that human UFSP1 is also an active Ufm1 protease. These results solve an age-old mystery in the human Ufm1 conjugation system and could have a greater impact not only on Ufm1 biology but also on the translation of genes employing nontraditional start codons.
泛素样修饰蛋白 1（Ufm1）是一种类泛素蛋白，也可以与蛋白质底物结合，从而改变它们的命运。Ufm1 的连接和去连接都是由 Ufm1 特异性蛋白酶（UFSPs）介导的。在人类中，普遍认为 UFSP2 是唯一一种参与 Ufm1 成熟和去 Ufm1 连接的活性 Ufm1 蛋白酶，而 UFSP1 则被认为是无活性的。在这里，Liang 等人提供了强有力的证据，表明人类 UFSP1 也是一种活性的 Ufm1 蛋白酶。这些结果解决了人类 Ufm1 连接系统中长期存在的一个谜团，不仅对 Ufm1 生物学，而且对采用非传统起始密码子的基因翻译都可能产生更大的影响。
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