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© Pierre Gounon
Entrée de Listeria dans une cellule épithéliale (Grossissement X 10000). Image colorisée.
Publication : Molecular microbiology

An ideR mutant of Mycobacterium smegmatis has derepressed siderophore production and an altered oxidative-stress response

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Molecular microbiology - 01 Nov 1996

Dussurget O, Rodriguez M, Smith I

Link to Pubmed [PMID] – 8939436

Mol. Microbiol. 1996 Nov;22(3):535-44

The mycobacterial ideR protein is a homologue of the diphtheria-toxin repressor DtxR. We have previously demonstrated that Mycobacterium tuberculosis ideR, like DtxR, represses transcription of Corynebacterium diphtheriae iron-regulated promoters in vivo and binds to C. diphtheriae operators in a metal-dependent manner in vitro. We show here that ideR mutants of M. smegmatis, constructed by allelic replacement, were defective in their ability to repress siderophore biosynthesis in the presence of iron. They were also more sensitive to hydrogen peroxide and had decreased levels of catalase/peroxidase (KatG) and manganese superoxide dismutase (Mn-SOD). This indicates that ideR is a negative regulator of siderophore production and is required for the response to superoxide- and hydrogen peroxide stress. We propose that ideR is the mycobacterial counterpart of the Escherichia coli Fur protein, i.e. It is a pleiotropic regulator that couples iron metabolism to the oxidative-stress response.

http://www.ncbi.nlm.nih.gov/pubmed/8939436