Hebert A M, Kropinski A M, Jarrell K F
Department of Microbiology and Immunology, Queen's University, Kingston, Ontario, Canada.
J Bacteriol. 1991 May;173(10):3224-7. doi: 10.1128/jb.173.10.3224-3227.1991.
The general properties of the heat shock response of the archaebacterium Methanococcus voltae were characterized. The induction of 11 heat shock proteins, with apparent molecular weights ranging from 18,000 to 90,000, occurred optimally at 40 to 50 degrees C. Some of the heat shock proteins were preferentially enriched in either the soluble (cytoplasm) or particulate (membrane) fraction. Alternative stresses (ethanol, hydrogen peroxide, NaCl) stimulated the synthesis of subsets of the heat shock proteins as well as unique proteins. Western blot (immunoblot) analysis, in which antisera to Escherichia coli heat shock proteins (DnaK and GroEL) were used, did not detect any immunologically cross-reactive proteins. In addition, Southern blot analysis did not reveal any homology between M. voltae and four highly conserved heat shock genes, mopB and dnaK from E. coli and hsp70 genes from Drosophila species and Saccharomyces cerevisiae.
对嗜热栖热甲烷球菌热休克反应的一般特性进行了表征。诱导出了11种热休克蛋白,其表观分子量范围为18,000至90,000,在40至50摄氏度时诱导效果最佳。一些热休克蛋白优先富集于可溶性(细胞质)或颗粒性(膜)组分中。其他应激因素(乙醇、过氧化氢、氯化钠)刺激了热休克蛋白亚群以及独特蛋白质的合成。使用针对大肠杆菌热休克蛋白(DnaK和GroEL)的抗血清进行的蛋白质免疫印迹(免疫印迹)分析未检测到任何免疫交叉反应蛋白。此外,Southern印迹分析未揭示嗜热栖热甲烷球菌与四个高度保守的热休克基因(大肠杆菌的mopB和dnaK以及果蝇属和酿酒酵母的hsp70基因)之间存在任何同源性。