Childs J D, Smith D A
J Bacteriol. 1969 Oct;100(1):377-82. doi: 10.1128/jb.100.1.377-382.1969.
Eight metH mutants in Salmonella typhimurium with closely linked sites of mutation which could grow only on methionine were isolated from a metE mutant deficient in N(5)-methyltetrahydropteroyltriglutamate-homocysteine transmethylase; their deficiency in cobalamin-dependent N(5)-methyltetrahydrofolate-homocysteine transmethylase was supported by the results of enzyme studies of one of them. Cotransduction of metH and metA (homoserine O-transsuccinylase) mutants was obtained, thus revealing linkage between a second pair of the six known methionine structural genes. One metH mutant clearly differed from the rest in that it reverted at a higher frequency, was temperature sensitive, complemented all other metH mutants, and was located farthest from the metA gene.
从缺乏N(5)-甲基四氢蝶酰三谷氨酸-同型半胱氨酸转甲基酶的metE突变体中分离出8个鼠伤寒沙门氏菌的metH突变体,这些突变体的突变位点紧密连锁,且只能在甲硫氨酸上生长;对其中一个突变体的酶学研究结果证实了它们缺乏钴胺素依赖性N(5)-甲基四氢叶酸-同型半胱氨酸转甲基酶。获得了metH和metA(高丝氨酸O-转琥珀酰酶)突变体的共转导,从而揭示了六对已知甲硫氨酸结构基因中的第二对之间的连锁关系。一个metH突变体与其他突变体明显不同,它回复突变频率更高,对温度敏感,能互补所有其他metH突变体,且位于离metA基因最远的位置。