MacGregor C H, Schnaitman C A
J Bacteriol. 1971 Oct;108(1):564-70. doi: 10.1128/jb.108.1.564-570.1971.
Chlorate-resistant mutants corresponding to each known genetic locus (chlA, chlB, chlC, chlD, chlE) were isolated from Escherichia coli K-12. All these mutants showed decreased amounts of membrane-bound nitrate reductase, cytochrome b, and formic dehydrogenase, but all had normal succinic dehydrogenase activity. Proteins from the cytoplasmic membranes of these mutants were compared to those of the wild type-on polyacrylamide gels. The addition of nitrate to wild-type anaerobic cultures caused increased formation of three membrane proteins. These same proteins, along with one other, were missing in varying patterns in mutants altered at the different genetic loci. One of the missing proteins was found to be the enzyme nitrate reductase, although this protein was present in some mutants lacking nitrate reductase activity. None of the others has been identified.
从大肠杆菌K-12中分离出与每个已知基因位点(chlA、chlB、chlC、chlD、chlE)相对应的抗氯酸盐突变体。所有这些突变体的膜结合硝酸还原酶、细胞色素b和甲酸脱氢酶含量均降低,但琥珀酸脱氢酶活性均正常。在聚丙烯酰胺凝胶上,将这些突变体细胞质膜中的蛋白质与野生型的进行了比较。向野生型厌氧培养物中添加硝酸盐会导致三种膜蛋白的形成增加。在不同基因位点发生改变的突变体中,这些相同的蛋白质以及另一种蛋白质以不同模式缺失。发现其中一种缺失的蛋白质是硝酸还原酶,尽管该蛋白质在一些缺乏硝酸还原酶活性的突变体中也存在。其他蛋白质均未被鉴定出来。