Roles of a solo LuxR in the biological control agent Lysobacter enzymogenes strain OH11.

Roles of a solo LuxR in the biological control agent Lysobacter enzymogenes strain OH11.
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Solo LuxR 在生物防治剂产酶溶杆菌菌株 OH11 中的作用

DOI:
10.1094/phyto-07-13-0188-r
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发表时间:
2014-03
期刊:
影响因子:
3.2
通讯作者:
Liu F
Liu F
中科院分区:
农林科学2区
文献类型:
--
作者:
Qian G;Xu F;Venturi V;Du L;Liu F

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产酶溶杆菌(Lysobacter enzymogenes)是一种广泛存在的植物伴生细菌,是一种环境友好的植物病害生物防治新品种。这种细菌产生多种抗真菌因子,如溶解酶和具有新颖结构和作用模式的抗真菌活性的次级代谢产物(热稳定抗真菌因子,HSAF)。抗真菌因子生物合成的调控机制在很大程度上是未知的。酶基因单独的LuxR蛋白已被证明是广泛存在的,在植物相关细菌中发挥重要作用。本研究克隆并研究了一个单独的LuxR蛋白LesR。产酶菌株OH 11。过表达,但没有删除lesR显着损害HSAF的生物合成水平和抗菌活性,但没有显示出明显的影响生产的主要裂解酶。过表达lesR还能显著加速细胞聚集并诱导L.这两种表型都是由L.酶基因C-末端螺旋-转角-螺旋结构域被证明是几个lesR控制的功能的关键。总的来说,我们的研究提供了第一个例子的作用和机制的一个单独的LuxR蛋白在植物相关的L。酶基因
Lysobacter enzymogenes is a ubiquitous plant-associated and environmentally friendly bacterium emerging as a novel biological control agent of plant disease. This bacterium produces diverse antifungal factors, such as lytic enzymes and a secondary metabolite (heat-stable antifungal factor, HSAF) having antifungal activity with novel structure and mode of action. The regulatory mechanism for biosynthesis of antifungal factors is largely unknown in L. enzymogenes. The solo LuxR proteins have been shown to be widespread, playing important roles in plant-associated bacteria. Here, we cloned and studied a solo LuxR protein, LesR from L. enzymogenes strain OH11. Overexpression, but not deletion of lesR significantly impaired HSAF biosynthesis levels and antimicrobial activities but did not show visible effect on production of major lytic enzymes. Overexpression of lesR also led to remarkably accelerated cell aggregation and induced production of a melanin-like pigment in L. enzymogenes; these two phenotyes are mediated by diffusible factor cell-cell signaling system of L. enzymogenes. The C-terminus helix-turn-helix domain was shown to be critical for several lesR-controlled functions. Overall, our study provides the first example of the roles and mechanisms of a solo LuxR protein in a plant-associated L. enzymogenes.