Bacterial SOS checkpoint protein SulA inhibits polymerization of purified FtsZ cell division protein
Bacterial SOS checkpoint protein SulA inhibits polymerization of purified FtsZ cell division protein
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DOI：
10.1128/jb.180.15.3946-3953.1998
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发表时间：
1998-08-01
影响因子：
3.2
通讯作者：
Bramhill, D
中科院分区：
文献类型：
--
作者：
Trusca, D;Scott, S;Bramhill, D
当苏拉蛋白作为SOS检查点控制系统的一部分响应于DNA损伤而被诱导时，大肠杆菌的细胞分裂被抑制。苏拉蛋白与微管蛋白样FtsZ分裂蛋白相互作用。我们研究了纯化的苏拉对FtsZ的影响，苏拉蛋白抑制FtsZ的聚合和GTdR活性，而点突变的苏拉蛋白对这两种FtsZ活性几乎没有影响。苏拉不抑制纯化的FtsZ 2突变蛋白的聚合，该突变蛋白最初被分离为对苏拉不敏感。这些研究定义了FtsZ的聚合测定，其响应于真实的细胞调节剂。这里提出的观察结果支持这样的观点，即聚合的FtsZ是其细胞的作用和直接的，可逆的抑制FtsZ聚合苏拉可能占分裂抑制的核心。
Cell division of Escherichia coli is inhibited when the SulA protein is induced in response to DNA damage as part of the SOS checkpoint control system. The SulA protein interacts with the tubulin-like FtsZ division protein. We investigated the effects of purified SulA upon FtsZ, SulA protein inhibits the polymerization ana the GTPase activity of FtsZ, while point mutant SulA proteins show little effect on either of these FtsZ activities. SulA did not inhibit the polymerization of purified FtsZ2 mutant protein, which was originally isolated as insensitive to SulA. These studies define polymerization assays for FtsZ which respond to an authentic cellular regulator. The observations presented here support the notion that polymerization of FtsZ is central to its cellular role and that direct, reversible inhibition of FtsZ polymerization by SulA may account for division inhibition.