A tandem GGDEF-EAL domain protein-regulated c-di-GMP signal contributes to spoilage-related activities of Shewanella baltica OS155

A tandem GGDEF-EAL domain protein-regulated c-di-GMP signal contributes to spoilage-related activities of Shewanella baltica OS155
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串联 GGDEF-EAL 结构域蛋白调节的 c-di-GMP 信号有助于 Shewanella baltica OS155 的腐败相关活性

DOI:
10.1007/s00253-020-10357-w
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发表时间:
2020-01
影响因子:
5
通讯作者:
Wang Yanbo
Wang Yanbo
中科院分区:
工程技术2区
文献类型:
--
作者:
Wang Feifei;Wang Yongzheng;Cen Congnan;Fu Linglin;Wang Yanbo

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环二鸟苷酸(c-di-GMP)是一种第二信使,参与调节细菌的各种生理过程。然而,其在腐败菌中的功能尚未得到解决。在这里,我们研究了一个串联GGDEF-EAL结构域蛋白,Sbal_3235,在腐败细菌希瓦氏菌baltica OS 155的功能。sbal_3235的缺失显着降低了c-di-GMP水平,生物膜的形成,和胞外多糖,三甲胺(TMA),腐胺的生产; sbal_3235缺失也下调了torS和speF基因的表达,并影响膜脂肪酸组成。在保守的GGDEF和EAL基序的定点突变废除二鸟苷酸环化酶(DGC)和磷酸二酯酶(PDE)的活性,分别。这些数据表明,Sbal_3235是具有双功能DGC和PDE活性的c-di-GMP库的重要贡献者,其参与S的生物膜形成和腐败活性。baltica OS 155.我们的研究结果扩展了c-di-GMP的生化作用,并揭示了其与腐败活动的联系,为食品质量和安全控制提供了新的目标。
Cyclic diguanylate (c-di-GMP) is a second messenger involved in the regulation of various physiological processes in bacteria. However, its function in spoilage bacteria has not yet been addressed. Here, we studied the function of a tandem GGDEF-EAL domain protein, Sbal_3235, in the spoilage bacterium Shewanella baltica OS155. The deletion of sbal_3235 significantly reduced the c-di-GMP level, biofilm formation, and exopolysaccharide, trimethylamine (TMA), and putrescine production; sbal_3235 deletion also downregulated the expression of the torS and speF genes and affected membrane fatty acid composition. Site-directed mutagenesis in conserved GGDEF and EAL motifs abolished diguanylate cyclase (DGC) and phosphodiesterase (PDE) activity, respectively. These data indicate that Sbal_3235 is an essential contributor to the c-di-GMP pool with bifunctional DGC and PDE activity, which is involved in the biofilm formation and spoilage activity of S. baltica OS155. Our findings expand the biochemical role of c-di-GMP and uncover its link to spoilage activities, providing novel targets for food quality and safety controlling.
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