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Chapter 5 : Bacterial Heme and Hemoprotein Receptors

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Bacterial Heme and Hemoprotein Receptors, Page 1 of 2

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Abstract:

This chapter focuses on describing the general features of heme acquisition systems by using the most extensively studied heme transport systems. General heme receptors have been identified in numerous bacteria. These receptors recognize either free heme or heme bound to host-carrier proteins. Three examples of general heme receptors, which can recognize numerous heme-containing substrates, are HmuR of , HemR of Yersinia enterocolitica, and HmuR of Porphyromonas gingivalis. HpuAB is unusual among heme receptors because it consists of two outer membrane-associated proteins. Current understanding of these proteins is based on the elucidated function of nonheme permeases and ATPases. The newly identified heme utilization systems of these three bacteria have laid the foundation for our understanding of heme-iron utilization in gram-positive bacteria. Structural information about receptors and other system components will undoubtedly follow, allowing one to investigate structure-function relationships and further understand the mechanism of heme transport. Results ranging from heme transport being essential to virulence to being dispensable for virulence have been reported for different model systems of bacterial infection.

Citation: Perkins-Balding D, Rasmussen A, Stojiljkovic I. 2004. Bacterial Heme and Hemoprotein Receptors, p 66-85. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch5

Key Concept Ranking

Outer Membrane Proteins
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Electron Transport System
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Figures

Image of FIGURE 1
FIGURE 1

Structure of heme. A ball-and-stick model of iron-protoporphyrin IX, with propionic side chains located at the bottom. Four nitrogen atoms coordinate the central iron atom. Possible axial ligands of iron are not shown. Double bonds are indicated by gray shading.

Citation: Perkins-Balding D, Rasmussen A, Stojiljkovic I. 2004. Bacterial Heme and Hemoprotein Receptors, p 66-85. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch5
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Image of FIGURE 3
FIGURE 3

Evolutionary relationships of bacterial heme and hemoprotein receptors. An unrooted phylogenetic tree of heme and hemoprotein receptors from Table 1 , excluding HbpA (), Pap31 (), HbpA (), HxuA (), lipoprotein e (), and the gram-positive receptors, is shown. The evolutionary distance is represented schematically by branch length. ClustalX and Treeview software were used to align data, perform bootstrapping analysis, and construct the tree.

Citation: Perkins-Balding D, Rasmussen A, Stojiljkovic I. 2004. Bacterial Heme and Hemoprotein Receptors, p 66-85. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch5
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Image of FIGURE 2
FIGURE 2

Heme assimilation systems of selected gram-negative and gram-positive bacteria. The Hem system of the gram-negative bacterium (left) and the Hmu system of the gram-positive bacterium (right) are drawn schematically. The heme transport locus in , encodes HemP, a protein of unknown function (not shown), HemR, the outer membrane hemoprotein receptor, HemS, a cytoplasmic heme-sequestering protein, HemT, a heme PBP, HemU, a membrane permease, and HemV, an ATPase. HemO, a heme oxygenase found in , is included because some gram-negative bacteria use heme oxygenases in the catabolism of heme to ferric iron, biliverdin, and CO, although a homologue has not been identified in . The Hmu system of consists of HmuT, a membrane-associated heme-binding protein, HmuU, a membrane permease, and HmuV, an ATPase. HmuO of converts heme in the cytoplasm to biliverdin, CO, and ferric iron. Abbreviations: Hm, heme; Hb, hemoglobin; OM, outer membrane; PP, periplasm; CM, cellular membrane; CO, carbon monoxide.

Citation: Perkins-Balding D, Rasmussen A, Stojiljkovic I. 2004. Bacterial Heme and Hemoprotein Receptors, p 66-85. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch5
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References

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Tables

Generic image for table
TABLE 1

Characterized bacterial heme uptake systems

Citation: Perkins-Balding D, Rasmussen A, Stojiljkovic I. 2004. Bacterial Heme and Hemoprotein Receptors, p 66-85. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch5
Generic image for table
TABLE 2

Bacteria that are able to bind or utilize heme or hemoproteins but have uncharacterized heme assimilation systems

Citation: Perkins-Balding D, Rasmussen A, Stojiljkovic I. 2004. Bacterial Heme and Hemoprotein Receptors, p 66-85. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch5

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