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首页> 外文期刊>Applied Microbiology >The Lactococcin G Immunity Protein Recognizes Specific Regions in Both Peptides Constituting the Two-Peptide Bacteriocin Lactococcin G
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The Lactococcin G Immunity Protein Recognizes Specific Regions in Both Peptides Constituting the Two-Peptide Bacteriocin Lactococcin G

机译：Lactococcin G免疫蛋白可识别构成两肽细菌素的两种肽中的特定区域

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摘要

Lactococcin G and enterocin 1071 are two homologous two-peptide bacteriocins. Expression vectors containing the gene encoding the putative lactococcin G immunity protein ( lagC ) or the gene encoding the enterocin 1071 immunity protein ( entI ) were constructed and introduced into strains sensitive to one or both of the bacteriocins. Strains that were sensitive to lactococcin G became immune to lactococcin G when expressing the putative lactococcin G immunity protein, indicating that the lagC gene in fact encodes a protein involved in lactococcin G immunity. To determine which peptide or parts of the peptide(s) of each bacteriocin that are recognized by the cognate immunity protein, combinations of wild-type peptides and hybrid peptides from the two bacteriocins were assayed against strains expressing either of the two immunity proteins. The lactococcin G immunity protein rendered the enterococcus strain but not the lactococcus strains resistant to enterocin 1071, indicating that the functionality of the immunity protein depends on a cellular component. Moreover, regions important for recognition by the immunity protein were identified in both peptides (Lcn-α and Lcn-β) constituting lactococcin G. These regions include the N-terminal end of Lcn-α (residues 1 to 13) and the C-terminal part of Lcn-β (residues 14 to 24). According to a previously proposed structural model of lactococcin G, these regions will be positioned adjacent to each other in the transmembrane helix-helix structure, and the model thus accommodates the present results.
机译：乳球菌G和肠球菌1071是两种同源的二肽细菌素。构建了包含编码推定的乳球菌G蛋白免疫蛋白（lagC）的基因或编码肠球蛋白1071免疫蛋白（entI）的基因的表达载体，并将其导入对一种或两种细菌素敏感的菌株中。当表达推定的乳球菌G免疫蛋白时，对乳球菌G敏感的菌株对乳球菌G产生免疫，这表明lagC基因实际上编码了一种与乳球菌G免疫有关的蛋白。为了确定同源免疫蛋白识别每种细菌素的哪些肽或肽的一部分，针对表达两种免疫蛋白中任一种的菌株测定了来自两种细菌素的野生型肽和杂合肽的组合。乳球菌G免疫蛋白产生了肠球菌菌株，但没有产生对肠球菌1071耐药的乳球菌菌株，表明该免疫蛋白的功能取决于细胞成分。此外，在构成乳球菌G的两种肽（Lcn-α和Lcn-β）中都鉴定了对免疫蛋白识别重要的区域。这些区域包括Lcn-α的N末端（残基1至13）和C- Lcn-β的末端部分（残基14至24）。根据先前提出的乳球菌G的结构模型，这些区域将在跨膜螺旋-螺旋结构中彼此相邻放置，因此该模型适应了当前结果。

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