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Abstract ▼ AI-Helper

The CheY, a signaling protein involved in bacterial chemotaxis, was purified by Affi-gel blue affinity chromatography and Sephacryl S-200 gel filtration chromatography. Purified CheY was acetylated in vitro by acetyl-CoA synthetase (ACS; isolated from yeast) using $[2-^{14}C]-acetate$. Co...

The CheY, a signaling protein involved in bacterial chemotaxis, was purified by Affi-gel blue affinity chromatography and Sephacryl S-200 gel filtration chromatography. Purified CheY was acetylated in vitro by acetyl-CoA synthetase (ACS; isolated from yeast) using $[2-^{14}C]-acetate$. Coenzyme A reduced the level of acetylated CheY, suggesting that other metabolic intermediates of acetate but not acetyl-CoA serves as an acetyl donor. To investigate the modification of CheY protein by acetylation, we developed a urea gel electrophoresis system similar to acid-urea gel electrophoresis that has been used for the analysis of histone modification. The resolution of urea gel was found better than that of native gel, in which CheY protein was clearly separated from other cellular proteins. In addition to CheY acetylation, CheY phosphorylation by CheA was detected on urea gel as multiply modified forms separated from the unmodified one. Analysis of the modified CheY bands revealed that CheY has more than one site for acetylation and for phosphorylation.