Ferré Axelle, De La Mora Javier, Ballado Teresa, Camarena Laura, Dreyfus Georges
Departamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, AP Postal 70-243, 04510 Mexico DF, Mexico.
J Bacteriol. 2004 Aug;186(15):5172-7. doi: 10.1128/JB.186.15.5172-5177.2004.
The six copies of the response regulator CheY from Rhodobacter sphaeroides bind to the switch protein FliM. Phosphorylation by acetyl phosphate (AcP) was detected by tryptophan fluorescence quenching in three of the four CheYs that contain this residue. Autophosphorylation with Ac(32)P was observed in five CheY proteins. We also show that all of the cheY genes are expressed simultaneously; therefore, in vivo all of the CheY proteins could bind to FliM to control the chemotactic response. Consequently, we hypothesize that in this complex chemotactic system, the binding of some CheY proteins to FliM, does not necessarily imply switching of the flagellar motor.
来自球形红杆菌的六个响应调节蛋白CheY拷贝与开关蛋白FliM结合。通过色氨酸荧光猝灭在四个含有该残基的CheY中的三个中检测到乙酰磷酸(AcP)的磷酸化。在五个CheY蛋白中观察到用Ac(32)P进行的自磷酸化。我们还表明所有cheY基因同时表达;因此,在体内所有的CheY蛋白都可以与FliM结合以控制趋化反应。因此,我们推测在这个复杂的趋化系统中,一些CheY蛋白与FliM的结合不一定意味着鞭毛马达的切换。