Cavard D
Laboratoire d'Ingénierie et de Dynamique des Systèmes membranaires, C.N.R.S., Marseille, France.
FEMS Microbiol Lett. 1995 Jan 15;125(2-3):173-8. doi: 10.1111/j.1574-6968.1995.tb07354.x.
The total amount of the colicin A lysis protein produced by cells grown in rich medium was analysed by immunoblotting. The intermediate forms of synthesis of this small lipoprotein were present in the cells at any time of induction, confirming that processing and maturation of colicin A lysis protein are slow and incomplete processes. The level of these various forms varied according to the time of induction, the growth conditions, the producing strain and the plasmid carrying the cal gene. It depended mainly on the presence in the producing strain of a degP gene which encodes the DegP protease. According to growth conditions, the DegP protease hydrolysed either a part or the total amount of the acylated precursor form. In some cases, a protease(s) other than DegP seemed to act on either form(s) of the colicin A lysis protein.
通过免疫印迹分析了在丰富培养基中生长的细胞产生的大肠杆菌素A裂解蛋白的总量。在诱导的任何时间,细胞中都存在这种小脂蛋白合成的中间形式,这证实了大肠杆菌素A裂解蛋白的加工和成熟是缓慢且不完全的过程。这些不同形式的水平根据诱导时间、生长条件、产生菌株和携带cal基因的质粒而变化。它主要取决于产生菌株中编码DegP蛋白酶的degP基因的存在。根据生长条件,DegP蛋白酶可水解部分或全部酰化前体形式。在某些情况下,除DegP之外的一种或多种蛋白酶似乎作用于大肠杆菌素A裂解蛋白的一种或多种形式。