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OxyR-regulated catalase CatB promotes the virulence in rice via detoxifying hydrogen peroxide in Xanthomonas oryzae pv. oryzae. | LitMetric

OxyR-regulated catalase CatB promotes the virulence in rice via detoxifying hydrogen peroxide in Xanthomonas oryzae pv. oryzae.

BMC Microbiol

State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, 100193, China.

Published: November 2016

AI Article Synopsis

Article Abstract

Background: To facilitate infection, Xanthomonas oryzae pv. oryzae (Xoo), the bacterial blight pathogen of rice, needs to degrade hydrogen peroxide (HO) generated by the host defense response via a mechanism that is mediated by the transcriptional regulator OxyR. The catalase (CAT) gene catB has previously been shown to belong to the OxyR regulon in Xoo. However, its expression patterns and function in HO detoxification and bacterial pathogenicity on rice remain to be elucidated.

Results: The catB gene encodes a putative catalase and is highly conserved in the sequenced strains of Xanthomonas spp. β-galactosidase analysis and electrophoretic mobility shift assays (EMSA) showed that OxyR positively regulated the transcription of catB by directly binding to its promoter region. The quantitative real-time PCR (qRT-PCR) assays revealed that the expression levels of catB and oxyR were significantly induced by HO. Deletion of catB or oxyR drastically impaired bacterial viability in the presence of extracellular HO and reduced CAT activity, demonstrating that CatB and OxyR contribute to HO detoxification in Xoo. In addition, ΔcatB and ΔoxyR displayed shorter bacterial blight lesions and reduced bacterial growth in rice compared to the wild-type stain, indicating that CatB and OxyR play essential roles in the virulence of Xoo.

Conclusions: Transcription of catB is enhanced by OxyR in response to exogenous HO. CatB functions as an active catalase that is required for the full virulence of Xoo in rice.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5101826PMC
http://dx.doi.org/10.1186/s12866-016-0887-0DOI Listing

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