Ohta T, Honda K, Saito K, Hayashi H, Tano H, Hamamoto T, Kagawa Y
Institute of Basic Medical Sciences, University of Tsukuba, Japan.
Biochem Biophys Res Commun. 1993 Mar 15;191(2):550-7. doi: 10.1006/bbrc.1993.1253.
The translation of a heat shock protein (HSP), TGroEL, of thermophilic bacterium PS3 increased within 10 minutes when the culture temperature was raised from 60 degrees C to 70 degrees C. In contrast to hyperthermophilic HSPs such as Pyrodictium ATPase, TGroEL is homologous to GroEL of E. coli (Tamada et al. (1991) Biochem. Biophys. Res. Commun. 197, 565-571). The promoter of the thermophilic heat shock gene (tgrE) was sequenced to analyze the heat shock response. The sequences of the promoter were CCTACTTGCA (-35 region) and GTTCATTAATA (-10 region), which are more heat labile than those of the sigma 32 recognition sites of GroEL. The expression of this homologous tgrE in E. coli may be lethal to the cells. The ATPase alpha subunit of this thermophile is also homologous to TGroEL.
嗜热细菌PS3的一种热休克蛋白(HSP)TGroEL,当培养温度从60℃升高到70℃时,其翻译在10分钟内增加。与超嗜热HSP如嗜热栖热菌ATP酶不同,TGroEL与大肠杆菌的GroEL同源(玉田等人(1991年)《生物化学与生物物理研究通讯》197,565 - 571)。对嗜热热休克基因(tgrE)的启动子进行测序以分析热休克反应。启动子序列为CCTACTTGCA(-35区)和GTTCATTAATA(-10区),它们比GroEL的σ32识别位点的序列对热更不稳定。这种同源tgrE在大肠杆菌中的表达可能对细胞是致命的。这种嗜热菌的ATP酶α亚基也与TGroEL同源。