scholarly journals Yersinia pestis TonB: Role in Iron, Heme, and Hemoprotein Utilization

2003 ◽  
Vol 71 (7) ◽  
pp. 4159-4162 ◽  
Author(s):  
Robert D. Perry ◽  
Jessica Shah ◽  
Scott W. Bearden ◽  
Jan M. Thompson ◽  
Jacqueline D. Fetherston

ABSTRACT In Yersinia pestis, the siderophore-dependent yersiniabactin (Ybt) iron transport system and heme transport system (Hmu) have putative TonB-dependent outer membrane receptors. Here we demonstrate that hemin uptake and iron utilization from Ybt are TonB dependent. However, the Yfe iron and manganese transport system does not require TonB.

2008 ◽  
Vol 74 (20) ◽  
pp. 6473-6475 ◽  
Author(s):  
Vanesa Amarelle ◽  
Mark R. O'Brian ◽  
Elena Fabiano

ABSTRACT The bacterium Sinorhizobium meliloti is able to use heme as a nutritional iron source. Here, we show that the iron-regulated shmR gene encodes an outer membrane protein required for growth on heme. Furthermore, an shmR mutant is resistant to the toxic heme analog gallium protoporphyrin. Thus, the receptor protein of the heme transport system has been identified in S. meliloti.


2004 ◽  
Vol 186 (13) ◽  
pp. 4067-4074 ◽  
Author(s):  
Sylvie Létoffé ◽  
Philippe Delepelaire ◽  
Cécile Wandersman

ABSTRACT Many gram-negative bacteria have specific outer membrane receptors for free heme, hemoproteins, and hemophores. Heme is a major iron source and is taken up intact, whereas hemoproteins and hemophores are not transported: the iron-containing molecule has to be stripped off at the cell surface, with only the heme moiety being taken up. The Serratia marcescens hemophore-specific outer membrane receptor HasR can transport either heme itself or heme bound to the hemophore HasA. This second mechanism is much more efficient and requires a higher TonB-ExbB-ExbD (TonB complex) concentration than does free or hemoglobin-bound heme uptake. This requirement for more of the TonB complex is associated with a higher energy requirement. Indeed, the sensitivity of heme-hemophore uptake to the protonophore carbonyl cyanide m-chlorophenyl hydrazone is higher than that of heme uptake from hemoglobin. We show that a higher TonB complex concentration is required for hemophore dissociation from the receptor. This dissociation is concomitant with heme uptake. We propose that increasing the TonB complex concentration drives more energy to the outer membrane receptor and speeds up the release of empty hemophores, which, if they remained on receptors, would inhibit heme transport.


2013 ◽  
Vol 2013 ◽  
pp. 1-15 ◽  
Author(s):  
S. J. Geetha ◽  
Sanket J. Joshi

Under field conditions, inoculated rhizobial strains are at a survival disadvantage as compared to indigenous strains. In order to out-compete native rhizobia it is not only important to develop strong nodulation efficiency but also increase their competence in the soil and rhizosphere. Competitive survival of the inoculated strain may be improved by employing strain selection and by genetic engineering of superior nitrogen fixing strains. Iron sufficiency is an important factor determining the survival and nodulation by rhizobia in soil. Siderophores, a class of ferric specific ligands that are involved in receptor specific iron transport into bacteria, constitute an important part of iron acquisition systems in rhizobia and have been shown to play a role in symbiosis as well as in saprophytic survival. Soils predominantly have iron bound to hydroxamate siderophores, a pool that is largely unavailable to catecholate-utilizing rhizobia. Outer membrane receptors for uptake of ferric hydroxamates include FhuA and FegA which are specific for ferrichrome siderophore. Increase in nodule occupancy and enhanced plant growth of thefegAandfhuAexpressing engineered bioinoculants rhizobial strain have been reported. Engineering rhizobia for developing effective bioinoculants with improved ability to utilize heterologous siderophores could provide them with better iron acquisition ability and consequently, rhizospheric stability.


2013 ◽  
Vol 87 (22) ◽  
pp. 12260-12269 ◽  
Author(s):  
X. Zhao ◽  
Y. Cui ◽  
Y. Yan ◽  
Z. Du ◽  
Y. Tan ◽  
...  

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