Burgess-Cassler A, Ordal G W
J Biol Chem. 1982 Nov 10;257(21):12835-8.
A chemotaxis-related methyltransferase enzyme from Bacillus subtilis has been shown to methylate membrane-bound proteins in Escherichia coli in vitro. The methylated proteins are in the same molecular weight range as authentic E. coli methyl-accepting chemotaxis proteins. It was also shown that wild type E. coli cytoplasmic extract could methylate membrane proteins from B. subtilis in its methyl-accepting chemotaxis protein region. Cytoplasmic extracts from methyltransferase mutants of either species could methylate neither set of methyl-accepting proteins in vitro. The B. subtilis enzyme was incapable of methylating any of a group of soluble eucaryotic proteins. These data suggest functional homology between B subtilis methyltransferase II and E. coli cheR protein (chemotaxis methyltransferase) despite the evolutionary divergence between these two species.
来自枯草芽孢杆菌的一种与趋化性相关的甲基转移酶已被证明在体外可使大肠杆菌中的膜结合蛋白甲基化。甲基化的蛋白与真正的大肠杆菌甲基接受趋化蛋白分子量范围相同。还表明野生型大肠杆菌细胞质提取物可在其甲基接受趋化蛋白区域使枯草芽孢杆菌的膜蛋白甲基化。任一物种的甲基转移酶突变体的细胞质提取物在体外均不能使任何一组甲基接受蛋白甲基化。枯草芽孢杆菌的酶不能使一组可溶性真核蛋白中的任何一种甲基化。这些数据表明尽管这两个物种在进化上存在差异，但枯草芽孢杆菌甲基转移酶II与大肠杆菌cheR蛋白（趋化性甲基转移酶）之间存在功能同源性。
