Dailey F E, Berg H C
Department of Cellular and Developmental Biology, Harvard University, Cambridge, Massachusetts 02138.
J Bacteriol. 1993 May;175(10):3236-9. doi: 10.1128/jb.175.10.3236-3239.1993.
Strains of Escherichia coli lacking all cytoplasmic chemotaxis proteins except CheY swim smoothly under most conditions. However, they tumble when exposed to acetate. Acetate coenzyme A synthetase (EC 6.2.1.1) was thought to be essential for this response. New evidence suggests that the tumbling is mediated instead by acetate kinase (EC 2.7.2.1), which might phosphorylate CheY via acetyl phosphate. In strains that were wild type for chemotaxis, neither acetate coenzyme A synthetase, acetate kinase, nor phosphotransacetylase (EC 2.3.1.8) (and thus acetyl phosphate) was required for responses to aspartate, serine, or sugars sensed by the phosphotransferase system. Thus, acetate-induced tumbling does not appear to play an essential role in chemotaxis in wild-type cells.
除CheY外缺乏所有细胞质趋化蛋白的大肠杆菌菌株在大多数情况下游动顺畅。然而,当暴露于乙酸盐时它们会翻滚。乙酸辅酶A合成酶(EC 6.2.1.1)被认为对这种反应至关重要。新证据表明,翻滚反应相反是由乙酸激酶(EC 2.7.2.1)介导的,乙酸激酶可能通过乙酰磷酸使CheY磷酸化。在趋化性为野生型的菌株中,对天冬氨酸、丝氨酸或磷酸转移酶系统感知的糖类的反应,既不需要乙酸辅酶A合成酶、乙酸激酶,也不需要磷酸转乙酰酶(EC 2.3.1.8)(以及因此的乙酰磷酸)。因此,乙酸诱导的翻滚似乎在野生型细胞的趋化性中不发挥重要作用。