A novel 3-oxoacyl-ACP reductase (FabG3) is involved in the xanthomonadin biosynthesis of Xanthomonas campestris pv. campestris
A novel 3-oxoacyl-ACP reductase (FabG3) is involved in the xanthomonadin biosynthesis of Xanthomonas campestris pv. campestris
复制标题
一种新型 3-氧代酰基-ACP 还原酶 (FabG3) 参与 Xanthomonas Campestris pv. 的黄单胞菌素生物合成。
DOI:
10.1111/mpp.12871
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发表时间:
2019
影响因子:
4.9
通讯作者:
Wang Haihong
中科院分区:
文献类型:
--
作者:
Yu Yonghong;Ma Jianrong;Guo Qiaoqiao;Ma Jincheng;Wang Haihong
Xanthomonas campestrispv.campestris(Xcc), the causal agent of black rot in crucifers, produces a membrane‐bound yellow pigment called xanthomonadin to protect against photobiological and peroxidative damage, and uses a quorum‐sensing mechanism mediated by the diffusible signal factor (DSF) family signals to regulate virulence factors production. TheXccgene XCC4003, annotated asXcc fabG3, is located in thepigcluster, which may be responsible for xanthomonadin synthesis. We report thatfabG3expression restored the growth of theEscherichia coli fabGtemperature‐sensitive mutant CL104 under non‐permissive conditions.In vitroassays demonstrated that FabG3 catalyses the reduction of 3‐oxoacyl‐acyl carrier protein (ACP) intermediates in fatty acid synthetic reactions, although FabG3 had a lower activity than FabG1. Moreover, thefabG3deletion did not affect growth or fatty acid composition. These results indicate thatXcc fabG3encodes a 3‐oxoacyl‐ACP reductase, but is not essential for growth or fatty acid synthesis. However, theXcc fabG3knock‐out mutant abolished xanthomonadin production, which could be only restored by wild‐typefabG3, but not by other 3‐oxoacyl‐ACP reductase‐encoding genes, indicating thatXccFabG3 is specifically involved in xanthomonadin biosynthesis. Additionally, our study also shows that theXcc fabG3‐disrupted mutant affectsXccvirulence in host plants.