Identification of a disulfide bonded protein from cytoplasm ofBacillus subtilis

ConclusionIn this study, P23 was found to be a disulfide-bonded cytoplasmic protein, abundant in late exponential phase and stationary phase cells, and was hardly detected in early exponential phase cells, the cells of sporulation process and spores. Therefore, synthesis of P23 was regulated by some specific factors or/and cellular environment. Conclusively, cytoplasm has a mechanism to catalyze the formation of disulfide bonds, which is consistent with Dermanet al. ’s conclusion from mutation experiment[1].

结论 在本研究中，发现P23是一种二硫键连接的胞质蛋白，在指数生长后期和稳定期细胞中含量丰富，而在指数生长前期细胞、芽孢形成过程中的细胞以及芽孢中几乎检测不到。因此，P23的合成受某些特定因子或/和细胞环境的调控。总之，细胞质具有催化二硫键形成的机制，这与德尔曼等人从突变实验中得出的结论一致[1]。