Boy E, Reinisch F, Richaud C, Patte J C
Biochimie. 1976;58(1-2):213-8. doi: 10.1016/s0300-9084(76)80372-0.
A mutant of lysyl-tRNA synthetase has been isolated in Escherichia coli K12. With this strain the Kmapp for lysine is 25 fold higher than with the parental strain. The percentage of charged tRNAlys in vivo is only 7 per cent (as against 65 per cent with HFR H). Under these conditions no derepression of synthesis is observed for three lysine biosynthetic enzymes (AK III, ASA-dehydrogenase, DAP-decarboxylase) ; a partial derepression is obtained in the case of the dhdp-reductase. Thus lysyl-tRNA does not act as the only corepressor molecule in the lysine regulon.
在大肠杆菌K12中分离出了一种赖氨酰 - tRNA合成酶突变体。用该菌株时,赖氨酸的表观米氏常数(Kmapp)比亲代菌株高25倍。体内带电荷的tRNAlys的百分比仅为7%(而高频重组H菌株为65%)。在这些条件下,未观察到三种赖氨酸生物合成酶(AK III、ASA - 脱氢酶、DAP - 脱羧酶)的合成去阻遏;对于dhdp - 还原酶,仅获得部分去阻遏。因此,赖氨酰 - tRNA并非赖氨酸调节子中唯一的共阻遏分子。