大肠杆菌plsA突变体中磷脂合成的特异性抑制
Specific inhibition of phospholipid synthesis in plsA mutants of Escherichia coli.
作者信息
Ray T K, Cronan J E, Godson G N
出版信息
J Bacteriol. 1976 Jan;125(1):136-41. doi: 10.1128/jb.125.1.136-141.1976.
Abstract
plsA mutants of Escherichia coli are temperature-sensitive strains which possess two enzymes of abnormal thermolability, sn-glycerol 3-phosphate acyltransferase and adenylate kinase. Phospholipid synthesis is inhibited after shift of plsA mutants to temperatures at the lower end of the nonpermissive temperature range. This inhibition is not due to inactivation of the adenylate kinase activity since nucleic acid (and hence adenosine 5'-triphosphate) synthesis is inhibited only slightly. These results show that in vivo inactivation of the sn-glycerol 3-phosphate acyltransferase can be observed under conditions which allow normal adenylate kinase function.
摘要
大肠杆菌的plsA突变体是温度敏感型菌株，它们拥有两种热稳定性异常的酶，即sn-甘油3-磷酸酰基转移酶和腺苷酸激酶。将plsA突变体转移到非允许温度范围下限的温度后，磷脂合成受到抑制。这种抑制并非由于腺苷酸激酶活性的失活，因为核酸（进而三磷酸腺苷）合成仅受到轻微抑制。这些结果表明，在允许腺苷酸激酶正常发挥功能的条件下，可以观察到sn-甘油3-磷酸酰基转移酶在体内的失活。
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