Role of a novel zinc-binding motif in the structure-function of deubiquitinating enzymes

泛素途径破坏许多控制细胞功能和生长的蛋白质，通过将泛素连接到它们并标记它们降解。去泛素化酶（DUBs）通过控制泛素的数量来调节蛋白质的破坏。DUBs和泛素途径也可以在生物技术应用中进行操纵。然而，对DUBs的结构/功能知之甚少。我们已经在DUBs中发现了一个新的锌结合基序，我们将探索这如何影响它们的结构以及与其他蛋白质的相互作用。这将大大提高我们对DUBs在生物技术和控制细胞功能方面的作用的认识。

The ubiquitin pathway destroys many proteins that control cell function and growth, by attaching ubiquitin to them and marking them for degradation. Deubiquitinating enzymes (DUBs) regulate protein destruction by controlling the amount of ubiquitin attached. DUBs and the ubiquitin pathway can also be manipulated in biotechnology applications. However, very little is known about the structure/function of DUBs. We have identified a new zinc-binding motif in DUBs, and we will explore how this contributes to their structure, and interactions with other proteins. This will significantly enhance our knowledge of how DUBs function in both biotechnology and in controlling cell function.