大肠杆菌lon突变体中细胞分裂抑制剂SulA的蛋白水解作用及活性调节
Proteolysis and modulation of the activity of the cell division inhibitor SulA in Escherichia coli lon mutants.
作者信息
Canceill D, Dervyn E, Huisman O
机构信息
Département de Biotechnologie, Institut Pasteur, Paris, France.
出版信息
J Bacteriol. 1990 Dec;172(12):7297-300. doi: 10.1128/jb.172.12.7297-7300.1990.
Abstract
Intracellular accumulation of the inducible cell division inhibitor SulA is modulated by proteases that ensure its degradation, namely, the Lon protease and another ATP-dependent protease(s). Lon- cells are UV sensitive because SulA is stable. We asked whether these ATP-dependent proteases are more active when lon cells are grown at high temperature or in synthetic medium since these conditions decrease the UV sensitivity of lon cells. We found that these growth conditions have no direct effect on Lon-independent degradation of SulA. They may, instead, decrease the SulA-FtsZ interaction.
摘要
诱导型细胞分裂抑制剂SulA的细胞内积累受到确保其降解的蛋白酶的调节，即Lon蛋白酶和另一种ATP依赖性蛋白酶。Lon基因缺失的细胞对紫外线敏感，因为SulA是稳定的。我们想知道，当lon基因缺失的细胞在高温或合成培养基中生长时，这些ATP依赖性蛋白酶是否更具活性，因为这些条件会降低lon基因缺失细胞的紫外线敏感性。我们发现，这些生长条件对SulA的不依赖Lon的降解没有直接影响。相反，它们可能会减少SulA与FtsZ的相互作用。
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