Kalinowski J, Cremer J, Bachmann B, Eggeling L, Sahm H, Pühler A
Lehrstuhl für Genetik, Fakultät für Biologie, Universität Bielefeld, Germany.
Mol Microbiol. 1991 May;5(5):1197-204. doi: 10.1111/j.1365-2958.1991.tb01893.x.
The lysC/asd gene cluster of Corynebacterium glutamicum ATCC 13032 was cloned and sequenced. The lysC locus coding for aspartokinase consists of two in-frame overlapping genes, lysC alpha encoding a protein of 421 amino acids (Mr 44,300) and lysC beta encoding a protein of 172 amino acids (Mr 18,600). The C. glutamicum aspartokinase was purified and found to contain two proteins of Mr 47,000 and Mr 18,000. A C. glutamicum mutant expressing a feedback-resistant aspartokinase was shown to be changed in a single base pair of the lysC beta gene, leading to an amino acid exchange in the beta-subunit of the aspartokinase. In addition, the identified mutation was found to be responsible for the enhanced expression of the asd gene located downstream of lysC.
对谷氨酸棒杆菌ATCC 13032的lysC/asd基因簇进行了克隆和测序。编码天冬氨酸激酶的lysC基因座由两个读框内重叠基因组成，lysCα编码一个421个氨基酸的蛋白质（Mr 44,300），lysCβ编码一个172个氨基酸的蛋白质（Mr 18,600）。纯化了谷氨酸棒杆菌天冬氨酸激酶，发现其含有Mr 47,000和Mr 18,000的两种蛋白质。一个表达抗反馈天冬氨酸激酶的谷氨酸棒杆菌突变体被证明在lysCβ基因的单个碱基对处发生了变化，导致天冬氨酸激酶β亚基中的一个氨基酸交换。此外，发现所鉴定的突变导致了位于lysC下游的asd基因表达增强。
