Silber K R, Sauer R T
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Mol Gen Genet. 1994 Jan;242(2):237-40. doi: 10.1007/BF00391018.
The Escherichia coli protease Prc (Tsp) exhibits specificity in vitro for proteins with nonpolar carboxyl termini. To determine whether Prc is responsible for the selective degradation in vivo of proteins with nonpolar carboxyl termini, we constructed a prc (tsp) deletion strain. Deletion of the prc gene did not prevent the rapid intracellular degradation of a variant of the amino-terminal domain of lambda repressor with a nonpolar carboxyl terminus, even though this protein is a substrate for Prc in vitro. Our results indicate that at least one additional carboxy-terminal-specific proteolytic system must exist in E. coli.
大肠杆菌蛋白酶Prc(Tsp)在体外对具有非极性羧基末端的蛋白质表现出特异性。为了确定Prc是否负责体内具有非极性羧基末端蛋白质的选择性降解,我们构建了一个prc(tsp)缺失菌株。prc基因的缺失并未阻止λ阻遏物氨基末端结构域变体(具有非极性羧基末端)在细胞内的快速降解,尽管该蛋白质在体外是Prc的底物。我们的结果表明,大肠杆菌中必定存在至少一种额外的羧基末端特异性蛋白水解系统。