Squires C K, Ingraham J L
J Bacteriol. 1969 Feb;97(2):488-94. doi: 10.1128/jb.97.2.488-494.1969.
As part of a study on the effect of low temperature on cellular regulatory processes, a class of lactose-negative mutants of Escherichia coli K-12 was isolated which could use lactose as a sole carbon and energy source at 37 C, but which could not use this sugar at 20 C. The lactose operon of the mutants functioned normally at 20 C. Galactose exhibited a strong inhibitory effect on growth, especially at 20 C. Growth of the mutants on glycerol was stopped at 20 C and slowed considerably at 37 C if galactose was added to the medium. Making the mutants galactose-positive eliminated the cold sensitivity of lactose utilization. One mutant was shown to be galactose-1-phosphate uridyl transferase-negative, galactose-kinase heat-sensitive, and uridine diphosphate-galactose-4-epimerase-positive. It is postulated that the mutant is able to phosphorylate galactose at 20 C (if only at a very low rate), but lacking transferase it is poisoned by the accumulation of galactose-1-phosphate. At 37 C, galactokinase is nonfunctional and the mutant grows on the glucose moiety of lactose.
作为一项关于低温对细胞调节过程影响的研究的一部分,分离出了一类大肠杆菌K - 12乳糖阴性突变体,它们在37℃时能够将乳糖作为唯一的碳源和能源,但在20℃时不能利用这种糖。这些突变体的乳糖操纵子在20℃时功能正常。半乳糖对生长表现出强烈的抑制作用,尤其是在20℃时。如果向培养基中添加半乳糖,这些突变体在甘油上的生长在20℃时停止,在37℃时也显著减缓。使突变体变为半乳糖阳性消除了乳糖利用的冷敏感性。一个突变体被证明是半乳糖-1-磷酸尿苷酰转移酶阴性、半乳糖激酶热敏感且尿苷二磷酸半乳糖-4-表异构酶阳性。据推测,该突变体在20℃时能够(即使速率非常低)将半乳糖磷酸化,但由于缺乏转移酶,它会因半乳糖-1-磷酸的积累而中毒。在37℃时,半乳糖激酶无功能,该突变体利用乳糖中的葡萄糖部分生长。