Structure, function and microbial ecology of diverse MarR bacterial regulators of auxin catabolism
Source: NCBI BioProject (ID PRJNA868387)
Source: NCBI BioProject (ID PRJNA868387)
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Project name: Structure, function and microbial ecology of diverse MarR bacterial regulators of auxin catabolism
Description: Chemical signaling in the plant microbiome can have drastic effects on microbial community structure, and on host growth and development. Previously, we demonstrated that the auxin metabolic signal interference performed by the bacterial genus Variovorax via a novel auxin degradation locus was essential for maintaining stereotypic root development in an ecologically-relevant bacterial synthetic community. Here, we dissect the Variovorax auxin degradation locus to define the genes necessary and sufficient for indole-3-acetic acid (IAA) degradation and signal interference. We determine the crystal structures and binding properties of the operon’s MarR-family repressor with IAA and other auxins. We identify auxin-degradation operons across the bacterial tree of life and define two distinct types based on gene content and metabolic products: iac-like and iad-like. We solve the structures of MarRs from representatives of each auxin degradation operon type, establishing that each have distinct IAA binding pockets. Comparison of representative IAA degrading strains from diverse bacterial genera show that while all degrade IAA, only strains containing iad-like auxin degrading operons interfere with auxin signaling in a complex synthetic community context. This suggests that iad-like operon containing strains, including Variovorax species, play a key ecological role in modulating auxins in the plant microbiome.Overall design: We performed RNA-Seq on triplicate cultures of CL14 wild type, IAA degradation deficient strain CL14 ΔiadDE, and MarR mutants CL14 ΔMarR_73 and CL14 ΔMarR_50. Standardized gene expression of the IAA degradation locus in these strains with and without IAA supplementation
Data type: Transcriptome or Gene expression
Sample scope: Multiisolate
Relevance: Other
Organization: The University of North Carolina at Chapel Hill
Literatures
- PMID: 36266335
Last updated: 2022-08-10