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 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

scholarly journals Molecular Characterization of a Newly Identified Heme-binding Protein Induced during Differentiation of urine Erythroleukemia Cells

1998 ◽  
Vol 273 (47) ◽  
pp. 31388-31394 ◽  
Author(s):  
Shigeru Taketani ◽  
Yasushi Adachi ◽  
Hirao Kohno ◽  
Susumu Ikehara ◽  
Rikio Tokunaga ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Binding Protein ◽  
Heme Binding ◽  
Erythroleukemia Cells ◽  
Heme Binding Protein

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 Characterization of Heme Ligation Properties of Rv0203, a Secreted Heme Binding Protein Involved inMycobacterium tuberculosisHeme Uptake

Biochemistry ◽  
2012 ◽  
Vol 51 (7) ◽  
pp. 1518-1531 ◽  
Author(s):  
Cedric P. Owens ◽  
Jing Du ◽  
John H. Dawson ◽  
Celia W. Goulding
Keyword(s):  
Binding Protein ◽  
Heme Binding ◽  
Heme Ligation ◽  
Heme Binding Protein

Purification and Characterization of an Extracellular Heme-Binding Protein, HasA, Involved in Heme Iron Acquisition†

Biochemistry ◽  
1997 ◽  
Vol 36 (23) ◽  
pp. 7050-7057 ◽  
Author(s):  
Nadia Izadi ◽  
Yann Henry ◽  
Jean Haladjian ◽  
Michel E. Goldberg ◽  
Cécile Wandersman ◽  
...  
Keyword(s):  
Binding Protein ◽  
Iron Acquisition ◽  
Heme Iron ◽  
Heme Binding ◽  
Purification And Characterization ◽  
Heme Binding Protein
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