Hazelbauer G L, Engström P, Harayama S
J Bacteriol. 1981 Jan;145(1):43-9. doi: 10.1128/jb.145.1.43-49.1981.
A comparison of the two-dimensional gel patterns of methyl-3H- and 35S-labeled membrane proteins from trg+ and trg null mutant strains of Escherichia coli indicated that the product of trg is probably methyl-accepting chemotaxis protein III. Like the other known methyl-accepting chemotaxis proteins, the trg product is a membrane protein that migrates as more than one species in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, implying that it too is multiple methylated. It appears likely that all chemoreceptors are linked to the tumble regulator through a single class of membrane protein transducers which are methyl-accepting proteins. Three transducers are coded for by genes tsr, tar, and, probably, trg. Another methyl-accepting protein, which is not related to any of these genes, was observed.
对来自大肠杆菌trg+和trg缺失突变株的甲基-3H和35S标记膜蛋白的二维凝胶图谱进行比较表明，trg的产物可能是甲基接受趋化蛋白III。与其他已知的甲基接受趋化蛋白一样，trg产物是一种膜蛋白，在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳中以多种形式迁移，这意味着它也被多次甲基化。所有化学感受器似乎都通过一类单一的作为甲基接受蛋白的膜蛋白转导器与翻滚调节器相连。三个转导器由tsr、tar基因编码，可能还有trg。还观察到另一种与这些基因均无关的甲基接受蛋白。
