ATP‐dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli
ATP‐dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli
复制标题
大肠杆菌中的 HslVU 蛋白酶对细胞分裂抑制剂 SulA 进行 ATP 依赖性降解
DOI：
10.1016/s0014-5793(99)00935-7
复制
发表时间：
1999
期刊：
影响因子：
3.5
通讯作者：
C. Chung
中科院分区：
文献类型：
--
作者：
I. Seong;J. Oh;S. J. Yoo;J. Seol;C. Chung
HslVU是一种ATP依赖性蛋白酶，由两种多聚体组分HslU ATP酶和HslV肽酶组成。为了深入了解HslVU在细胞分裂调节中的作用，将重组的HslVU与大肠杆菌细胞分裂抑制剂苏拉或其与麦芽糖结合蛋白（MBP）的融合蛋白一起孵育。HslVU在与ATP孵育后降解了这两种蛋白质，但与其不可水解的类似物ATPγS孵育后不降解，表明苏拉的降解需要ATP水解。使用针对苏拉产生的抗体的脉冲追踪实验揭示，苏拉的稳定性增加了inhsl突变体，并进一步增加了inlon/hsl双突变体，表明苏拉是HslVU以及蛋白酶La（Lon）的体内底物。这些结果表明，除了Lon之外，HslVU通过降解苏拉在调节细胞分裂中起重要作用。
HslVU is an ATP‐dependent protease consisting of two multimeric components, the HslU ATPase and the HslV peptidase. To gain an insight into the role of HslVU in regulation of cell division, the reconstituted enzyme was incubated with SulA, an inhibitor of cell division inEscherichia coli, or its fusion protein with maltose binding protein (MBP). HslVU degraded both proteins upon incubation with ATP but not with its non‐hydrolyzable analog, ATPγS, indicating that the degradation of SulA requires ATP hydrolysis. The pulse‐chase experiment using an antibody raised against MBP‐SulA revealed that the stability of SulA increased inhslmutants and further increased inlon/hsldouble mutants, indicating that SulA is an in vivo substrate of HslVU as well as of protease La (Lon). These results suggest that HslVU in addition to Lon plays an important role in regulation of cell division through degradation of SulA.
DOI：
10.1073/pnas.93.12.5808
发表时间：
1996-06-11
影响因子：
11.1
作者：
Rohrwild, M;Coux, O;Goldberg, AL
通讯作者：
Goldberg, AL