Wylie D, Stock A, Wong C Y, Stock J
Department of Molecular Biology, Princeton University, NJ 08544.
Biochem Biophys Res Commun. 1988 Mar 15;151(2):891-6. doi: 10.1016/s0006-291x(88)80365-6.
The CheA protein of the Salmonella typhimurium chemotaxis system is phosphorylated by ATP. Phospho-CheA transfers its phosphoryl group to a second chemotaxis protein, CheY. Unlike phospho-CheA, phospho-CheY is relatively unstable, rapidly decaying to phosphate and CheY. We propose that phosphorylation of CheY may play a role in its function as a tumble regulator to control motor behavior in response to attractant and repellent stimuli.
鼠伤寒沙门氏菌趋化系统中的CheA蛋白由ATP磷酸化。磷酸化的CheA将其磷酰基团转移到另一种趋化蛋白CheY上。与磷酸化的CheA不同，磷酸化的CheY相对不稳定，会迅速分解为磷酸盐和CheY。我们提出，CheY的磷酸化可能在其作为翻滚调节器的功能中发挥作用，以响应吸引剂和排斥剂刺激来控制运动行为。
