The degradation of RcsA by ClpYQ(HslUV) protease in Escherichia coli

Chun Yang Chang, Hui Ting Hu, Chih Hsuan Tsai, Whei Fen Wu

研究成果: Article同行評審

17 引文 斯高帕斯(Scopus)


In Escherichia coli, RcsA, a positive activator for transcription of cps (capsular polysaccharide synthesis) genes, is degraded by the Lon protease. In lon mutant, the accumulation of RcsA leads to overexpression of capsular polysaccharide. In a previous study, overproduction of ClpYQ(HslUV) protease represses the expression of cpsBlacZ, but there has been no direct observation demonstrating that ClpYQ degrades RcsA. By means of a MBP-RcsA fusion protein, we showed that RcsA activated cpsBlacZ expression and could be rapidly degraded by Lon protease in SG22622 (lon+). Subsequently, the comparative half-life experiments performed in the bacterial strains SG22623 (lon) and AC3112 (lon clpY clpQ) indicated that the RcsA turnover rate in AC3112 was relatively slow and RcsA was stable at 30 °C or 41 °C. In addition, ClpY could interact with RscA in an in vitro pull-down assay, and the more rapid degradation of RcsA was observed in the presence of ClpYQ protease at 41 °C. Thus, we conclude that RcsA is indeed proteolized by ClpYQ protease.

頁(從 - 到)42-50
期刊Microbiological Research
出版狀態Published - 2016 3月 1

All Science Journal Classification (ASJC) codes

  • 微生物學


深入研究「The degradation of RcsA by ClpYQ(HslUV) protease in Escherichia coli」主題。共同形成了獨特的指紋。