scholarly journals The P. aeruginosa Heme Binding Protein PhuS Is a Heme Oxygenase Titratable Regulator of Heme Uptake

2013 ◽  
Vol 8 (8) ◽  
pp. 1794-1802 ◽  
Author(s):  
Maura J. O’Neill ◽  
Angela Wilks
Keyword(s):  
Heme Oxygenase ◽  
Binding Protein ◽  
Heme Binding ◽  
Heme Uptake ◽  
Heme Binding Protein

scholarly journals The Cytoplasmic Heme-binding Protein (PhuS) from the Heme Uptake System ofPseudomonas aeruginosaIs an Intracellular Heme-trafficking Protein to the δ-Regioselective Heme Oxygenase

2006 ◽  
Vol 281 (19) ◽  
pp. 13652-13662 ◽  
Author(s):  
Ila B. Lansky ◽  
Gudrun S. Lukat-Rodgers ◽  
Darci Block ◽  
Kenton R. Rodgers ◽  
Melanie Ratliff ◽  
...  
Keyword(s):  
Heme Oxygenase ◽  
Binding Protein ◽  
Uptake System ◽  
Heme Binding ◽  
Heme Uptake ◽  
Heme Trafficking ◽  
Heme Binding Protein

Expression of the mRNA of Heme-Binding Protein 23 Is Coordinated with That of Heme Oxygenase-1 by Heme and Heavy Metals in Primary Rat Hepatocytes and Hepatoma Cells

Biochemistry ◽  
1995 ◽  
Vol 34 (41) ◽  
pp. 13407-13411 ◽  
Author(s):  
Stephan Immenschuh ◽  
Shin-ichiro Iwahara ◽  
Hiroyuki Satoh ◽  
Christina Nell ◽  
Norbert Katz ◽  
...  
Keyword(s):  
Heavy Metals ◽  
Heme Oxygenase ◽  
Binding Protein ◽  
Rat Hepatocytes ◽  
Hepatoma Cells ◽  
Heme Oxygenase 1 ◽  
Heme Binding ◽  
Primary Rat Hepatocytes ◽  
Heme Binding Protein

Characterization of the Periplasmic Heme-Binding Protein ShuT from the Heme Uptake System ofShigella dysenteriae†

Biochemistry ◽  
2005 ◽  
Vol 44 (39) ◽  
pp. 13179-13191 ◽  
Author(s):  
Suntara Eakanunkul ◽  
Gudrun S. Lukat-Rodgers ◽  
Suganya Sumithran ◽  
Arundhati Ghosh ◽  
Kenton R. Rodgers ◽  
...  
Keyword(s):  
Binding Protein ◽  
Uptake System ◽  
Heme Binding ◽  
Heme Uptake ◽  
Heme Binding Protein

scholarly journals Ligand-induced allostery in the interaction of the Pseudomonas aeruginosa heme binding protein with heme oxygenase

2017 ◽  
Vol 114 (13) ◽  
pp. 3421-3426 ◽  
Author(s):  
Daniel J. Deredge ◽  
Weiliang Huang ◽  
Colleen Hui ◽  
Hirotoshi Matsumura ◽  
Zhi Yue ◽  
...  
Keyword(s):  
Heme Oxygenase ◽  
Binding Protein ◽  
Underlying Mechanism ◽  
Site Directed Mutagenesis ◽  
Heme Binding ◽  
Conformational Rearrangement ◽  
Terminal Domain ◽  
Heme Transfer ◽  
Hdx Ms ◽  
Heme Binding Protein

A heme-dependent conformational rearrangement of the C-terminal domain of heme binding protein (PhuS) is required for interaction with the iron-regulated heme oxygenase (HemO). Herein, we further investigate the underlying mechanism of this conformational rearrangement and its implications for heme transfer via site-directed mutagenesis, resonance Raman (RR), hydrogen–deuterium exchange MS (HDX-MS) methods, and molecular dynamics (MD). HDX-MS revealed that the apo-PhuS C-terminal α6/α7/α8-helices are largely unstructured, whereas the apo-PhuS H212R variant showed an increase in structure within these regions. The increased rate of heme association with apo-PhuS H212R compared with the WT and lack of a detectable five-coordinate high-spin (5cHS) heme intermediate are consistent with a more folded and less dynamic C-terminal domain. HDX-MS and MD of holo-PhuS indicate an overall reduction in molecular flexibility throughout the protein, with significant structural rearrangement and protection of the heme binding pocket. We observed slow cooperative unfolding/folding events within the C-terminal helices of holo-PhuS and the N-terminal α1/α2-helices that are dampened or eliminated in the holo-PhuS H212R variant. Chemical cross-linking and MALDI-TOF MS mapped these same regions to the PhuS:HemO protein–protein interface. We previously proposed that the protein–protein interaction induces conformational rearrangement, promoting a ligand switch from His-209 to His-212 and triggering heme release to HemO. The reduced conformational freedom of holo-PhuS H212R combined with the increase in entropy and decrease in heme transfer on interaction with HemO further support this model. This study provides significant insight into the role of protein dynamics in heme binding and release in bacterial heme transport proteins.

Heme dependent transcriptional regulation of the Pseudomonas aeruginosa tandem sRNA prrF1,F2 locus by the cytoplasmic heme binding protein PhuS

2020 ◽  
Author(s):  
Tyree Wilson ◽  
Susana Mouriño ◽  
Angela Wilks
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Fluorescence Anisotropy ◽  
Binding Protein ◽  
Transcriptional Regulator ◽  
Opportunistic Pathogen ◽  
Dual Function ◽  
Heme Binding ◽  
Heme Uptake ◽  
Qpcr Analysis ◽  
Heme Binding Protein

Pseudomonas aeruginosa is an opportunistic pathogen requiring iron for its survival and virulence. P. aeruginosa can acquire iron from heme via the heme assimilation system (Has) and Pseudomonas heme uptake (Phu) systems. The Has and Phu systems have non-redundant roles in heme sensing and transport, respectively. However, despite their respective roles heme taken up by either the Has or Phu system is regulated at the metabolic level by the cytoplasmic heme binding protein PhuS, which controls heme flux through the iron-regulated heme oxygenase HemO. Herein, through a combination of CHIP-PCR, EMSA and fluorescence anisotropy we show PhuS binds upstream of the tandem iron-responsive sRNAs prrF1,F2. Furthermore, qPCR analysis of the PAO1 WT and ΔphuS allelic strain shows loss of PhuS abrogates the heme dependent regulation of PrrH. Taken together our data shows PhuS, in addition to its role in regulating extracellular heme metabolism also functions as a transcriptional regulator of the heme-dependent sRNA, PrrH. This dual function of PhuS is central to integrating extracellular heme utilization into the PrrF/PrrH sRNA regulatory network critical for P. aeruginosa adaptation and virulence within the host.

scholarly journals Differential Cellular and Subcellular Localization of Heme-Binding Protein 23/Peroxiredoxin I and Heme Oxygenase-1 in Rat Liver

2003 ◽  
Vol 51 (12) ◽  
pp. 1621-1631 ◽  
Author(s):  
Stephan Immenschuh ◽  
Eveline Baumgart-Vogt ◽  
Melly Tan ◽  
Shin-Ichiro Iwahara ◽  
Giuliano Ramadori ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Heme Oxygenase ◽  
Rat Liver ◽  
Binding Protein ◽  
Heme Oxygenase 1 ◽  
Heme Binding ◽  
Heme Binding Protein ◽  
Peroxiredoxin I
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