DeMoss J A
J Bacteriol. 1978 Feb;133(2):626-30. doi: 10.1128/jb.133.2.626-630.1978.
Five temperature-sensitive chlC mutants were isolated from Escherichia coli by the technique of localized mutagenesis. All of the mutants produced severely reduced levels of both nitrate reductase and formate dehydrogenase when grown at 43 degrees C. In three of the mutants, the nitrate reductase activity produced at the permissive temperature was shown to be thermolabile compared with the activity produced by the parent wild-type strain, both in membrane preparations and in preparations released from the membrane by deoxycholate. In each case, formate dehydrogenase activity was similar to the wild-type activity in its stability to heat. It is concluded that the chlC gene codes for at least one of the polypeptide chains of nitrate reductase and that the chlC mutations affect indirectly the formation of formate dehydrogenase.
通过局部诱变技术从大肠杆菌中分离出五个温度敏感型chlC突变体。当在43摄氏度下生长时,所有突变体产生的硝酸还原酶和甲酸脱氢酶水平均大幅降低。在其中三个突变体中,与亲本野生型菌株产生的活性相比,在允许温度下产生的硝酸还原酶活性在膜制剂和经脱氧胆酸盐从膜中释放的制剂中均表现出热不稳定。在每种情况下,甲酸脱氢酶活性在其热稳定性方面与野生型活性相似。结论是chlC基因编码硝酸还原酶的至少一条多肽链,并且chlC突变间接影响甲酸脱氢酶的形成。