Structure and product relationship analysis of acyl homoserine lactone synthases among Ensifer adhaerens reveals distinct chromosome and plasmid origins
Structure and product relationship analysis of acyl homoserine lactone synthases among Ensifer adhaerens reveals distinct chromosome and plasmid origins
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Ensifer adhaerens 中酰基高丝氨酸内酯合酶的结构和产物关系分析揭示了不同的染色体和质粒起源
DOI：
10.1016/j.bbrc.2019.06.131
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发表时间：
2019
影响因子：
3.1
通讯作者：
Yu Zhiliang
中科院分区：
文献类型：
--
作者：
Huang Yili;Xu Xinyi;Song Yao;Yuan Nate;Yu Xionghui;Ji Yuqian;Liu Jiang;Jiang Tingting;Yu Zhiliang
尽管AHL合酶基因的保守DNA序列与酰基高丝氨酸内酯合酶基因（Acyl Homoserine Lactones synthase gene，AHL）同源，但AHL合酶的结构-产物关系仍有待阐明。本研究通过简并引物和体外表达的方法，收集了9株LuxIs嗜胶菌的阿勒基因序列和表达谱信息。染色体编码的LuxI（C-LuxI）不仅在DNA序列上，而且在阿勒谱中与质粒编码的LuxI（P-LuxI）区分开来。C-LuxI仅产生C14-HSL，而P-LuxI主要产生C8-HSL和3-氧代-C8-HSL。序列-产物关系分析更新了我们对T140（EsaI）在3-oxo-HSL生产中的作用的认识。基于这些LuxI的3D结构的计算计算揭示了C-LuxI中的链长与酰胺对阿勒合酶的亲和力之间的线性关系，这在P-LuxI中没有发现。因此，我们提出了线性对接亲和力作为预测长链阿勒生产的阿勒合酶的标准。本研究扩展了我们对阿勒酶的结构-产物关系的理解，并揭示了这种酶的独特的染色体和质粒起源。
Despite the conservative DNA sequences amongLuxI(Acyl Homoserine Lactones synthase gene) homologs, structure-product relationship of AHL synthase remains to be elucidated. In this study, through degenerate primers andin vitroexpression methods, we collected the information of the gene sequences and AHL profiles from nine LuxIs amongEnsifer adhaerensstrains. The chromosome-encoded LuxI (C-LuxI) distinguished themselves from the plasmid-encoded ones (P-LuxI) not only in the DNA sequences, but also in AHL profiles. The C-LuxIs produced only C14-HSL, while the P-LuxIs produced predominantly C8-HSL and 3-oxo-C8-HSL. Sequence-product relationship analysis updated our recognition of the role of T140 (EsaI) in the 3-oxo-HSL production. Computational calculation based on 3D structures of these LuxIs revealed the linear relationship between the chain length and the affinity of amides to AHL synthase in C-LuxI, which was not found in the P-LuxI. We hereby proposed the linear docking affinity as a criterion for the prediction of long-chain AHL production by an AHL synthase. This study extends our understanding on the structure-product relationship of AHL synthases and revealed the distinct chromosome and plasmid origin of this enzyme amongE. adhaerens.