Dataset Information

A Pseudomonas aeruginosa biliverdin IX-dependent transcriptional regulator (BdrB) integrates extracellular heme metabolism with Type IV pili-dependent motilities

ABSTRACT: Pseudomonas aeruginosa displays remarkable adaptability in chronic infections by exploiting heme as its primary iron source at the expense of siderophore uptake. Previous studies have identified a pivotal role for the heme metabolites BVIX β/δ in the regulation of Type IV pili-dependent motility and biofilm formation. Thus, the heme metabolites integrate the switch in iron source with lifestyle adaptations required for chronic infection. The mechanism by which the BVIX metabolites directly or indirectly regulate such lifestyle adaptations remains elusive. In this study, through a combination of thermal proteome profiling (TPP) followed by quantitative mass spectrometry (MS), we identified a BVIX-binding protein PA5271 encoded in a three-gene operon (pa5269-pa-5270-pa5271). PA5271 is annotated as a helix-turn-helix DNA-binding protein and purifies as a dimer that binds BVIX but not BVIX or BVIX. Deletion of the gene renamed bdrB (biliverdin-dependent regulator responsive to BVIX) displayed a marked reduction in Type IV pili (TFP) associated motilities including twitching.

INSTRUMENT(S):

ORGANISM(S): Pseudomonas Sp. Ar40

SUBMITTER: Mehari Weldemariam

LAB HEAD: Maureen A. Kane

PROVIDER: PXD062383 | Pride | 2026-06-08

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	WH_PAO1_TPP_Ctrl_47C_1ug_3-5ul_1_redo_12-15-2016.mgf	Mgf
	WH_PAO1_TPP_Ctrl_47C_1ug_3-5ul_2_12-12-2016.mgf	Mgf
	WH_PAO1_TPP_Ctrl_47C_1ug_3-5ul_3_12-12-2016.mgf	Mgf
	WH_PAO1_TPP_Ctrl_50C_1ug_3-5ul_1_12-12-2016.-1326212816.mznld	Other
	WH_PAO1_TPP_Ctrl_50C_1ug_3-5ul_1_redo_12-15-2016.mgf	Mgf

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Publications

pmultiqc: An Open-Source, Lightweight, and Metadata-Oriented QC Reporting Library for MS Proteomics.

Yue Qi-Xuan QX Dai Chengxin C Kamatchinathan Selvakumar S Bandla Chakradhar C Webel Henry H Larrea Asier A Bittremieux Wout W Uszkoreit Julian J Müller Tom David TD Xiao Jinqiu J Cox Juergen J Yu Fengchao F Ewels Philip P Demichev Vadim V Kohlbacher Oliver O Sachsenberg Timo T Bielow Chris C Bai Mingze M Perez-Riverol Yasset Y

Molecular & cellular proteomics : MCP 20260217 6

The increasing scale and complexity of proteomics data demand robust, scalable, and interpretable quality control (QC) frameworks to ensure data reliability and reproducibility. Here, we present pmultiqc, an open-source Python package that standardizes and generates web-based QC reports across multiple proteomics data analysis platforms. Built on top of the widely adopted MultiQC framework, pmultiqc offers specialized modules tailored to mass spectrometry workflows, with full initial support for ...[more]

PMID: 41713790

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Project description:The response regulator HrrA belonging to the HrrSA two-component system (previously named CgtSR11) is known to be repressed by the global iron-dependent regulator DtxR in Corynebacterium glutamicum. Sequence analysis indicated an involvement of the HrrSA system in heme-dependent gene expression. Growth experiments revealed that the non-pathogenic soil bacterium C. glutamicum is able to use hemin or hemoglobin as sole iron source. In DNA microarray analyses a putative operon encoding the hemin-binding protein HtaA and the putative hemin ABC transporter HmuTUV showed a strong upregulation in heme-grown cells. Deletion of the hmu operon clearly affects heme utilization, but does not completely abolish growth on heme or hemoglobin. As a central part of this study, we investigated the regulon of the response regulator HrrA via comparative transcriptome analysis of a hrrA deletion mutant and C. glutamicum wild type in combination with DNA-protein interaction studies with purified HrrA protein. Our data provide evidence for a heme-dependent transcriptional activation of heme oxygenase (hmuO), an enzyme involved in the utilization of heme as iron source. Besides hmuO, HrrA was shown to activate the expression of heme-containing components of the respiratory chain, namely ctaD and the ctaE-qcrCAB operon encoding subunits I and III of cytochrome aa3 oxidase and three subunits of the cytochrome bc1 complex. Furthermore, HrrA represses almost all genes involved in heme biosynthesis, including glutamyl-tRNA reductase (hemA), uroporphyrinogen decarboxylase (hemE), and ferrochelatase (hemH). Thus, our data clearly emphasize a central role of the HrrSA system in the control of heme homeostasis in C. glutamicum. Three biological replicates of each experiment were performed. Experiment 1: Transcriptome comparison of wild type grown und FeSO4 or heme as iron source; Exp. 2: WT vs. hrrA deletion mutant grown on FeSO4; Exp. 3: WT vs. hrrA mutant grown on heme. For analysis via DNA microarraysose RNA was isolated from exponentially growing cells cultivated in CgXII medium containing glucose as carbon source and either 2.5 uM FeSO4 or 2.5 uM heme as iron source.