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© Institut Pasteur
Spirochète : bactérie hélicoïdale, flexible et ondulante de longueur variable, non colorable par la coloration de Gram, très mobile (endoflagelles). Trois familles : Spirochaetaceae, Leptospiraceae, et Brachyspiraceae. Principaux genres pathogènes pour l'homme : Borrelia (Borrelia burgdorferi cause de la maladie de Lyme), Treponema (Treponema pallidum cause de la syphillis), Leptospira (Leptospira interrogans serovar icterohaemorrhagiae cause de la maladie de Weil). Image colorisée.
Publication : Molecular microbiology

HemR is an OmpR/PhoB-like response regulator from Leptospira, which simultaneously effects transcriptional activation and repression of key haem metabolism genes

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Molecular microbiology - 15 Sep 2014

Morero NR, Botti H, Nitta KR, Carrión F, Obal G, Picardeau M, Buschiazzo A

Link to Pubmed [PMID] – 25145397

Mol. Microbiol. 2014 Oct;94(2):340-52

Several Leptospira species cause leptospirosis, the most extended zoonosis worldwide. In bacteria, two-component systems constitute key signalling pathways, some of which are involved in pathogenesis. The physiological roles of two-component systems in Leptospira are largely unknown, despite identifying several dozens within their genomes. Biochemical confirmation of an operative phosphorelaying two-component system has been obtained so far only for the Hklep/Rrlep pair. It is known that hklep/rrlep knockout strains of Leptospira biflexa result in haem auxotrophy, although their de novo biosynthesis machinery remains fully functional. Haem is essential for Leptospira, but information about Hklep/Rrlep effector function(s) and target(s) is still lacking. We are now reporting a thorough molecular characterization of this system, which we rename HemK/HemR. The DNA HemR-binding motif was determined, and found within the genomes of saprophyte and pathogenic Leptospira. In this way, putative HemR-regulated genes were pinpointed, including haem catabolism-related (hmuO – haem oxygenase) and biosynthesis-related (the hemA/C/D/B/L/E/N/G operon). Specific HemR binding to these two promoters was quantified, and a dual function was observed in vivo, inversely repressing the hmuO, while activating the hemA operon transcription. The crystal structure of HemR receiver domain was determined, leading to a mechanistic model for its dual regulatory role.

http://www.ncbi.nlm.nih.gov/pubmed/25145397