Krebes K A, Dirksen L B, Krause D C
Department of Microbiology, University of Georgia, Athens 30602, USA.
J Bacteriol. 1995 Aug;177(15):4571-4. doi: 10.1128/jb.177.15.4571-4574.1995.
A cell-free system was used to characterize the phosphorylation of Mycoplasma pneumoniae proteins HMW1 and HMW2, which are involved in the adherence of this organism to human tracheal epithelium during infection. The pH and cation requirements for phosphorylation of HMW1 and HMW2 were determined, and the effects of glycolytic intermediates, cyclic AMP, and eukaryotic kinase-phosphatase inhibitors and stimulators on this process were examined. Phosphoamino acid analysis identified serine as the major phosphate acceptor for both HMW1 and HMW2 in this system.
利用无细胞系统对肺炎支原体蛋白HMW1和HMW2的磷酸化进行了表征,这两种蛋白在感染过程中参与该生物体与人气管上皮的黏附。确定了HMW1和HMW2磷酸化的pH和阳离子需求,并研究了糖酵解中间产物、环磷酸腺苷以及真核激酶 - 磷酸酶抑制剂和刺激剂对该过程的影响。磷酸氨基酸分析确定丝氨酸是该系统中HMW1和HMW2的主要磷酸受体。