Wolfinbarger L
Biochim Biophys Acta. 1976 Jul 15;436(4):774-88. doi: 10.1016/0005-2736(76)90405-3.
Characterization of a double mutant, his-6: hgu-4, which is unable to utilize L-histidyl-glycine as a source of histidine has revealed a new locus on linkage group V. The hgu-4 genotype results in a generalized reduced transport activity for amino acids, with a concomitant increased resistance to amino acid analogs. Transport rates and analog resistance for amino acids by this mutant are compared to the previously reported transport deficient mutants fpr-1, nap and un-3. Transport of L-aspartate as a function of temperature is examined in a variety of transport deficient strains in an attempt to explain the mode of action of mutation which pleiotropically affect several genetically and biochemically distinct amino acid transport systems.
对无法利用L-组氨酰甘氨酸作为组氨酸来源的双突变体his-6:hgu-4进行的表征揭示了连锁群V上的一个新位点。hgu-4基因型导致氨基酸的一般转运活性降低，同时对氨基酸类似物的抗性增加。将该突变体对氨基酸的转运速率和类似物抗性与先前报道的转运缺陷突变体fpr-1、nap和un-3进行比较。在多种转运缺陷菌株中检测L-天冬氨酸的转运随温度的变化，以试图解释多效性影响几个遗传和生化上不同的氨基酸转运系统的突变作用模式。
