Belitsky B R, Sonenshein A L
Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.
J Bacteriol. 1998 Dec;180(23):6298-305. doi: 10.1128/JB.180.23.6298-6305.1998.
The complete Bacillus subtilis genome contains two genes with the potential to encode glutamate dehydrogenase (GlutDH) enzymes. Mutations in these genes were constructed and characterized. The rocG gene proved to encode a major GlutDH whose synthesis was induced in media containing arginine or ornithine or, to a lesser degree, proline and was repressed by glucose. A rocG null mutant was impaired in utilization of arginine, ornithine, and proline as nitrogen or carbon sources. The gudB gene was expressed under all growth conditions tested but codes for a GlutDH that seemed to be intrinsically inactive. Spontaneous mutations in gudB that removed a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family.
完整的枯草芽孢杆菌基因组包含两个有可能编码谷氨酸脱氢酶(GlutDH)的基因。构建并表征了这些基因中的突变。rocG基因被证明编码一种主要的GlutDH,其合成在含有精氨酸或鸟氨酸的培养基中被诱导,在较小程度上也可被脯氨酸诱导,并受到葡萄糖的抑制。rocG基因缺失突变体在利用精氨酸、鸟氨酸和脯氨酸作为氮源或碳源方面存在缺陷。gudB基因在所有测试的生长条件下均有表达,但编码的GlutDH似乎本身无活性。gudB基因中的自发突变去除了野生型gudB序列内的一个9碱基对直接重复序列,激活了GudB蛋白,并使谷氨酸家族氨基酸的利用效率更高。