Bussey L B, Switzer R L
Department of Biochemistry, University of Illinois, Urbana 61801.
J Bacteriol. 1993 Oct;175(19):6348-53. doi: 10.1128/jb.175.19.6348-6353.1993.
A search for genes involved in the inactivation and degradation of enzymes in sporulating Bacillus subtilis led to identification of the B. subtilis degA gene, whose product stimulates degradation of B. subtilis glutamine phosphoribosylpyrophosphate amidotransferase in Escherichia coli cells. degA encodes a 36.7-kDa protein that has sequence similarity to several E. coli and B. subtilis regulatory proteins of the LacI class. B. subtilis degA::cat insertional inactivation mutants had no detectable defect in the inactivation or degradation of phosphoribosylpyrophosphate amidotransferase in glucose- or lysine-starved B. subtilis cells, however. We suggest that degA encodes either a novel protease or, more likely, a gene that stimulates production of such a protease.
对参与枯草芽孢杆菌芽孢形成过程中酶的失活和降解的基因进行搜索,导致了枯草芽孢杆菌degA基因的鉴定,其产物能刺激大肠杆菌细胞中枯草芽孢杆菌谷氨酰胺磷酸核糖焦磷酸酰胺转移酶的降解。degA编码一种36.7 kDa的蛋白质,该蛋白质与几种大肠杆菌和枯草芽孢杆菌LacI类调节蛋白具有序列相似性。然而,枯草芽孢杆菌degA::cat插入失活突变体在葡萄糖或赖氨酸饥饿的枯草芽孢杆菌细胞中,磷酸核糖焦磷酸酰胺转移酶的失活或降解方面没有可检测到的缺陷。我们认为degA要么编码一种新型蛋白酶,或者更有可能编码一个刺激这种蛋白酶产生的基因。