Abstract 3024 A heme-dependent conformational switch in the Pseudomonas aeruginosa PhuS protein drives its function from transcriptional regulator to heme chaperone

Pseudomonas aeruginosa an opportunistic pathogen requires iron for survival and virulence. Within the host heme is the preferred source of iron, particularly in chronic infection where P. aeruginosa switches to utilize heme at the expense of iron-siderophores. Heme enters the cell through two non-redundant heme uptake systems, the heme assimilation system (Has) and the Pseudomonas heme uptake (Phu) system. Once in the cytoplasm, heme is bound by PhuS, which selectively transfers heme to heme oxygenase (HemO) for metabolism and release of iron and the biliverdin (BVIX)beta and BVIXdelta metabolites.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109678
Primary Topic
Bacterial Genetics and Biotechnology
Type
article
Field-Weighted Citation Impact
0.00

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Abstract 3024 A heme-dependent conformational switch in the Pseudomonas aeruginosa PhuS protein drives its function from transcriptional regulator to heme chaperone

Nicholas Montes, Samuel A. Krug, Daniel Deredge, Angela Wilks et al.
1 links
Journal of Biological Chemistry
Bacterial Genetics and Biotechnology
article

Abstract 3024 A heme-dependent conformational switch in the Pseudomonas aeruginosa PhuS protein drives its function from transcriptional regulator to heme chaperone

Nicholas Montes, Samuel A. Krug, Daniel Deredge, Angela Wilks, Riki Egoshi, Maureen A. Kane
article en

Abstract

Pseudomonas aeruginosa an opportunistic pathogen requires iron for survival and virulence. Within the host heme is the preferred source of iron, particularly in chronic infection where P. aeruginosa switches to utilize heme at the expense of iron-siderophores. Heme enters the cell through two non-redundant heme uptake systems, the heme assimilation system (Has) and the Pseudomonas heme uptake (Phu) system. Once in the cytoplasm, heme is bound by PhuS, which selectively transfers heme to heme oxygenase (HemO) for metabolism and release of iron and the biliverdin (BVIX)beta and BVIXdelta metabolites.

Journal of Biological ChemistryVol. 301(5)
The University of Texas Medical Branch at Galveston (US)
National Institutes of Health, Chemistry, Engineering and Medicine for Human Health, Stanford University
Zero hunger
Openalex Percentile: Top 84%
Bacterial Genetics and Biotechnology
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Abstract 3024 A heme-dependent conformational switch in the Pseudomonas aeruginosa PhuS protein drives its function from transcriptional regulator to heme chaperone — Nicholas Montes, Samuel A. Krug, et al. · Journal of Biological Chemistry (2025) | TGRS Research Map | TGRS