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首页> 外文期刊>Journal of bacteriology >Cloning of a new low-molecular-weight spore-specific protein gene from Bacillus megaterium.
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Cloning of a new low-molecular-weight spore-specific protein gene from Bacillus megaterium.

机译：克隆来自Megillus的新的低分子量孢子特异性蛋白基因。

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摘要

Three EcoRI fragments of Bacillus megaterium DNA hybridized only under nonrestrictive conditions on Southern blots to a probe containing the previously cloned gene for protein C, a small, acid-soluble spore protein (SASP) from B. megaterium. All three fragments were cloned in Escherichia coli cells in plasmid pBR325, and after being transferred to an E. coli expression vector, one of the fragments (C-3) directed the synthesis of a new small, acid-soluble spore protein (termed C-3) immunologically related to protein C. As previously observed with the protein C gene, protein C-3 gene expression in E. coli required an external promoter and suppression of termination of transcription. Protein C-3 was purified from induced E. coli cells, and its immunological properties, electrophoretic mobility, amino acid composition, and amino-terminal sequence were determined. These data indicated that protein C-3 was related, but not identical, to either protein C or the closely related protein A--two of the major small, acid-soluble spore proteins of B. megaterium. Detailed examination of acid extracts of B. megaterium spores showed that they contained a minor protein which comigrated with C-3 on acrylamide gel electrophoresis at low pH and reacted immunologically like C-3.
机译：芽孢杆菌的三个EcoRI片段仅在南部排列的非传记条件下杂交，探针含有来自B. Megircium的蛋白C的先前克隆基因的蛋白C，酸可溶性孢子蛋白（SASP）。在质粒PBR325中的大肠杆菌细胞中克隆了所有三个片段，并且在转移到大肠杆菌表达载体之后，其中一种片段（C-3）指导了新的小酸溶孢子蛋白的合成（称为C. -3）与蛋白质c免疫相关。如前用蛋白C基因观察到，在大肠杆菌中蛋白C-3基因表达需要外部启动子和抑制转录终止。从诱导的大肠杆菌细胞纯化蛋白C-3，测定其免疫学特性，电泳迁移率，氨基酸组合物和氨基末端序列。这些数据表明，蛋白C-3与蛋白C或密切相关的蛋白A - B. MegiStium的主要小型酸溶孢子蛋白中有关但不相同。详细检测B. Megirium孢子的酸性提取物，显示它们含有在低pH下用C-3在丙烯酰胺凝胶电泳上进行的次要蛋白质，并使C-3免疫。

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