Fujiwara Y, Den Kamp J A, Steenbakkers J F, Verhoff C, Van Deenen L L
Antonie Van Leeuwenhoek. 1975;41(4):455-64. doi: 10.1007/BF02565089.
Phospholipid metabolism in a temperature-sensitive lysis mutant of Escherichia coli has been investigated. The incorporation of 32P into the phospholipids of this mutant was negligible, not only at the non-permissive temperature, as was demonstrated earlier, but also at 30C. Furthermore, cultivation of the cells at the non-permissive temperature during 90 min, which is the time required to induce lysis, did not alter the amount of phospholipid per cell. In vitro experiments demonstrated that the enzymes involved in phospholipid biosynthesis are fully active at 42C. Lysis therefore is not directly caused by a defect in phospholipid synthesis. Evidence is presented that the low 32P incorporation is the result of a defective glycerol-3-phosphate dehydrogenase which determines the turnover of the immediate lipid percursor, glycerol-3-phosphate.
对大肠杆菌温度敏感裂解突变体中的磷脂代谢进行了研究。不仅如先前所示,在非允许温度下,而且在30℃时,该突变体中32P掺入磷脂的量都可忽略不计。此外,在诱导裂解所需的90分钟内,将细胞在非允许温度下培养,并未改变每个细胞的磷脂量。体外实验表明,参与磷脂生物合成的酶在42℃时完全有活性。因此,裂解并非直接由磷脂合成缺陷引起。有证据表明,32P掺入量低是甘油-3-磷酸脱氢酶缺陷的结果,该酶决定了直接脂质前体甘油-3-磷酸的周转。