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首页> 外文期刊>Microbiology >Genetic analysis of Bacillus anthracis Sap S-layer protein crystallization domain
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Genetic analysis of Bacillus anthracis Sap S-layer protein crystallization domain

机译：杆菌炭疽病S层蛋白结晶结构域的遗传分析

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Bacillus anthracis, the aetiological agent of anthrax, synthesizes two surface-layer (S-layer) proteins. S-layers are two-dimensional crystalline arrays that completely cover bacteria. In rich medium, the B. anthracis S-layer consists of Sap during the exponential growth phase. Sap is a modular protein composed of an SLH (S-layer homology)-anchoring domain followed by a putative crystallization domain (Sapc). A projection map of the two-dimensional Sap array has been established on deflated bacteria. In this work, the authors used two approaches to investigate whether Sapc is the crystallization domain. The purified Sapc polypeptide (604?aa) was sufficient to form a crystalline structure, as illustrated by electron microscopy. Consistent with this result, the entire Sapc domain promoted auto-interaction in a bacterial two-hybrid screen developed for the present study. The screen was derived from a system that takes advantage of the Bordetella pertussis cyclase subdomain structure to enable one to identify peptides that interact. A screening strategy was then employed to study Sapc subdomains that mediate interaction. A random library, derived from the Sapc domain, was constructed and screened. The selected polypeptides interacting with the complete Sapc were all larger (155?aa and above) than the mean size of the randomly cloned peptides (approx. 60 residues). This result suggests that, in contrast with observations for other interactions studied with this two-hybrid system, large fragments were required to ensure efficient interaction. It was noteworthy that only one polypeptide, which spanned aa 148–358, was able to interact with less than the complete Sapc, in fact, with itself.
机译：芽孢杆菌，炭疽病的Aetiological代理，合成两个表面层（S层）蛋白。 S层是完全覆盖细菌的二维晶体阵列。在富培养基中，B.炭疽S层由在指数增长阶段的SAP组成。 SAP是由SLH（S层同源性） - 分析结构域组成的模块化蛋白质，然后是推定的结晶结构域（SAPC）。二维SAP阵列的投影映射已经在放气细菌上建立。在这项工作中，作者使用了两种方法来研究SAPC是否是结晶结构域。纯化的SAPC多肽（604〜A）足以形成结晶结构，如电子显微镜所示。与此结果一致，整个SAPC结构域在为本研究开发的细菌双杂交屏中促进了自身相互作用。屏幕衍生自利用Bordetella Pertussis Cyclase亚域结构的系统，以使其能够识别相互作用的肽。然后使用筛选策略来研究调节相互作用的SAPC子域。构建和筛选来自SAPC域的随机库。与完整的SAPC相互作用的所选多肽均较大（155〜A和以上），而不是随机克隆肽的平均尺寸（约60个残基）。该结果表明，与用该双混合系统研究的其他相互作用的观察结果相比，需要大的碎片来确保有效的相互作用。值得注意的是，只有一种跨越AA 148-358的多肽，能够与完整的SAPC相互作用，其本身就是这样。

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