A dynamically localized protease complex and a polar specificity factor control a cell cycle master regulator
A dynamically localized protease complex and a polar specificity factor control a cell cycle master regulator
复制标题
DOI：
10.1016/j.cell.2005.12.033
复制
发表时间：
2006-02-10
期刊：
影响因子：
64.5
通讯作者：
McAdams, HH
中科院分区：
文献类型：
--
作者：
McGrath, PT;Iniesta, AA;McAdams, HH
调节蛋白质水解对于原核生物和真核生物的细胞周期进程都是必不可少的。我们在这里表明，ClpXP蛋白酶，负责多种细菌蛋白质的降解，是动态定位到特定的细胞位置在柄杆菌，它降解共定位的蛋白质。必须从柄杆菌属细胞中清除以允许染色体复制起始的CtrA细胞周期主调节因子在其降解的细胞极处与ClpXP蛋白酶相互作用。我们已经确定了一种新的，保守的蛋白质，RcdA，在细胞中与CtrA和ClpX形成复合物。CtrA极性定位和ClpXP降解需要RcdA。RcdA的定位模式与ClpX定位一致并依赖于ClpX定位。因此，动态定位的ClpXP蛋白水解复合物与细胞质因子一起为细菌细胞周期期间的蛋白质降解提供时间和空间特异性。
Regulated proteolysis is essential for cell cycle progression in both prokaryotes and eukaryotes. We show here that the ClpXP protease, responsible for the degradation of multiple bacterial proteins, is dynamically localized to specific cellular positions in Caulobacter where it degrades colocalized proteins. The CtrA cell cycle master regulator, that must be cleared from the Caulobacter cell to allow the initiation of chromosome replication, interacts with the ClpXP protease at the cell pole where it is degraded. We have identified a novel, conserved protein, RcdA, that forms a complex with CtrA and ClpX in the cell. RcdA is required for CtrA polar localization and degradation by ClpXP. The localization pattern of RcdA is coincident with and dependent upon ClpX localization. Thus, a dynamically localized ClpXP proteolysis complex in concert with a cytoplasmic factor provides temporal and spatial specificity to protein degradation during a bacterial cell cycle.