Sedlák M, Vinter V, Adamec J, Vohradský J, Voburka Z, Chaloupka J
Department of Cellular and Molecular Microbiology, Czech Academy of Sciences, Prague.
J Bacteriol. 1993 Dec;175(24):8049-52. doi: 10.1128/jb.175.24.8049-8052.1993.
Cells of Bacillus megaterium 27 were challenged by a 30-min heat shock at 45 degrees C during various sporulation stages and then shifted back to a temperature permissive for sporulation (27 degrees C), at which they developed spores. Heat shock applied at 120 min after the end of the exponential phase induced synthesis of heat shock proteins (HSPs) in the sporangia and delayed the inactivation of spores at 85 degrees C. Several HSPs, mainly HSP 70, could be detected in the cytoplasm of these spores. An analogous HSP, the main HSP induced by increased temperature during growth, belongs to the GroEL group according to its N-terminal sequence. The identity of this protein was confirmed by Western blot (immunoblot) analysis with polyclonal antibodies against B. subtilis GroEL. Sporangia treated by heat shock immediately or 240 min after exponential phase also synthesized HSPs, but none of them could be detected in the spores in an appreciable amount. These spores showed only a slightly increased heat resistance.
巨大芽孢杆菌27的细胞在不同芽孢形成阶段于45℃接受30分钟热激处理,然后转移回允许芽孢形成的温度(27℃),在该温度下它们形成芽孢。指数期结束后120分钟施加的热激诱导了芽孢囊内热激蛋白(HSPs)的合成,并延迟了芽孢在85℃下的失活。在这些芽孢的细胞质中可检测到几种热激蛋白,主要是HSP 70。一种类似的热激蛋白,即生长期间温度升高诱导产生的主要热激蛋白,根据其N端序列属于GroEL家族。用抗枯草芽孢杆菌GroEL的多克隆抗体通过蛋白质免疫印迹(免疫印迹)分析证实了该蛋白的身份。指数期后立即或240分钟进行热激处理的芽孢囊也合成了热激蛋白,但在芽孢中均未检测到可观数量的热激蛋白。这些芽孢仅表现出耐热性略有增加。