RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences
RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences
复制标题
DOI：
10.1038/sj.emboj.7600449
复制
发表时间：
2004-11-10
期刊：
影响因子：
11.4
通讯作者：
Ito, K
中科院分区：
文献类型：
--
作者：
Akiyama, Y;Kanehara, K;Ito, K
大肠杆菌RseP（以前称为YaeL）被认为是一种“调节性膜内蛋白水解”（RIP）蛋白酶，其在跨膜区段内或靠近跨膜区段的位置处将第二切割引入抗σ（E）蛋白RseA中。然而，其酶活性和底物裂解位置均未确定。在这里，我们表明，RseP依赖的切割确实发生在预测的跨膜序列的膜蛋白在体内。此外，RseP催化相同的特异性蛋白水解在体外反应系统中使用纯化的组分。我们在体内和体外的结果表明，RseP可以切割一些模式的膜蛋白，是无关的RseA的跨膜序列，只要跨膜区含有低螺旋倾向的残基。这些结果表明，RseP具有潜在的能力，以削减广泛的膜蛋白序列。有趣的是，它仍然被招募到sigma（E）压力反应级联中，作为RIP的特定参与者。
Escherichia coli RseP (formerly YaeL) is believed to function as a 'regulated intramembrane proteolysis' (RIP) protease that introduces the second cleavage into anti-sigma(E) protein RseA at a position within or close to the transmembrane segment. However, neither its enzymatic activity nor the substrate cleavage position has been established. Here, we show that RseP-dependent cleavage indeed occurs within predicted transmembrane sequences of membrane proteins in vivo. Moreover, RseP catalyzed the same specificity proteolysis in an in vitro reaction system using purified components. Our in vivo and in vitro results show that RseP can cleave transmembrane sequences of some model membrane proteins that are unrelated to RseA, provided that the transmembrane region contains residues of low helical propensity. These results show that RseP has potential ability to cut a broad range of membrane protein sequences. Intriguingly, it is nevertheless recruited to the sigma(E) stress-response cascade as a specific player of RIP.