The P. aeruginosa heme binding protein PhuS is a heme oxygenase titratable regulator of heme uptake.

The P. aeruginosa heme binding protein PhuS is a heme oxygenase titratable regulator of heme uptake.
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铜绿假单胞菌血红素结合蛋白PHUS是血红素氧化酶的滴定器的血红素摄取调节剂。

DOI:
10.1021/cb400165b
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发表时间:
2013-08-16
影响因子:
4
通讯作者:
Wilks, Angela
Wilks, Angela
中科院分区:
生物学2区
文献类型:
--
作者:
O'Neill, Maura J.;Wilks, Angela

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The Pseudomonas aeruginosa heme utilization (Phu) system encodes several proteins involved in the acquisition of heme as an iron source. Once internalized heme is degraded by the iron-regulated heme oxygenase, HemO to biliverdin (BV) IXδ and β. In vitro studies have shown holo-PhuS transfers heme to the iron-regulated HemO. This protein-protein interaction is specific for HemO as PhuS does not interact with the α-regioselective heme oxygenase, BphO. Bacterial genetics and isotopic labeling (13C-heme) studies confirmed extracellular heme is converted to 13C-BVIX δ and β through the catalytic action of HemO. In an effort to further understand the role of PhuS similar studies were performed on the P. aeruginosa PAO1 ΔphuS and ΔphuS/ΔhemO strains. In contrast to wild type strain the absence of PhuS results in extracellular heme uptake and degradation via the catalytic action of HemO and BphO. At low heme concentrations loss of PhuS leads to inefficient extracellular heme uptake supported by the fact the mRNA levels of PhuR, HemO and BphO remain elevated when compared to the wild type PAO1. On increasing extracellular heme concentrations the elevated levels of PhuR, HemO and BphO allow “leaky uptake” and degradation of heme via HemO and BphO. Similarly, in the ΔphuS/ΔhemO strain the higher heme concentrations combined with elevated levels of PhuR and BphO leads to non-specific heme uptake and degradation by BphO. Thus we propose heme flux into the cell is driven by the catalytic action of HemO with PhuS acting as a “control-valve” to regulate extracellular heme flux.
DOI: 10.1128/jb.183.21.6394-6403.2001
发表时间: 2001-11-01
影响因子: 3.2
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