scholarly journals Identification of an Iron-Regulated, Hemin-Binding Outer Membrane Protein in Sinorhizobium meliloti

2002 ◽  
Vol 68 (12) ◽  
pp. 5877-5881 ◽  
Author(s):  
Federico Battistoni ◽  
Raúl Platero ◽  
Rosario Duran ◽  
Carlos Cerveñansky ◽  
Julio Battistoni ◽  
...  

ABSTRACT Rhizobia are soil bacteria that are able to establish symbiotic associations with leguminous hosts. In iron-limited environments these bacteria can use iron present in heme or heme compounds (hemoglobin, leghemoglobin). Here we report the presence in Sinorhizobium meliloti of an iron-regulated outer membrane protein that is able to bind hemin but not hemoglobin. Protein assignment was done by matrix-assisted laser desorption ionization-time of flight mass spectrometry. Tryptic peptides correlated with the mass measurements obtained accounted for 54% of the translated sequence of a putative heme receptor gene present in the chromosome of S. meliloti 1021. The results which we obtained suggest that this protein (designated ShmR for S inorhizobium heme receptor) is involved in high-affinity heme-mediated iron transport.

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.


Author(s):  
Ángel Rodríguez-Villodres ◽  
Rocío Álvarez-Marín ◽  
María Antonia Pérez-Moreno ◽  
Andrea Miró-Canturri ◽  
Marco Durán Lobato ◽  
...  

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