Clancy M, Madill K A, Wood J M
J Bacteriol. 1981 Jun;146(3):902-6. doi: 10.1128/jb.146.3.902-906.1981.
Chemotaxis to L-proline was examined by the capillary assay, using a set of Escherichia coli strains bearing well-defined defects in the enzymes of proline transport and utilization. Aspartate taxis was measured as a constitutive, control activity whose receptor and transducer requirements are known. Proline chemotaxis showed a pattern of induction more analogous to that of proline dehydrogenase than of that of proline transport, but chemotaxis to proline was eliminated by mutations eliminating either or both of these activities. No response to proline was observed in the absence of a proline concentration gradient or when succinate was provided as an oxidizable carbon source. These data suggest that the chemotactic response to proline results from a direct impact of proline oxidation on the energy metabolism of the cell.
利用一组在脯氨酸运输和利用酶中存在明确缺陷的大肠杆菌菌株,通过毛细管试验检测了对L-脯氨酸的趋化性。将天冬氨酸趋化性作为一种组成型对照活性进行测定,其受体和转导器的要求是已知的。脯氨酸趋化性显示出一种诱导模式,与脯氨酸脱氢酶的诱导模式比与脯氨酸运输的诱导模式更相似,但消除这两种活性中的一种或两种的突变会消除对脯氨酸的趋化性。在没有脯氨酸浓度梯度的情况下或当提供琥珀酸盐作为可氧化碳源时,未观察到对脯氨酸的反应。这些数据表明,对脯氨酸的趋化反应是脯氨酸氧化对细胞能量代谢的直接影响所致。