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© Michel-Robert Popoff
Clostridium difficile en microscopie à contraste de phase. On distingue des bactéries sporulées, non sporulées et d'autres en cours de lyse (destruction). Bactérie de l'environnement (sol, eau, foin, sable), elle est à l'origine d'infections nosocomiales survenant après un traitement antibiotique : Clostridium difficile prédomine alors que les autres bactéries de la flore intestinale ont été détruites. L'infection peut provoquer deux types de pathologies graves : les colites pseudo-membraneuses dont l'origine est quasiment due à 100 % à C. difficile et la diarrhée post-antibiothérapie due à C. difficile dans 30 % des cas de ces diarrhées.
Publication : Molecular microbiology

Antagonistic effects of dual PTS-catalysed phosphorylation on the Bacillus subtilis transcriptional activator LevR

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Molecular microbiology - 01 Apr 1998

Martin-Verstraete I, Charrier V, Stülke J, Galinier A, Erni B, Rapoport G, Deutscher J

Link to Pubmed [PMID] – 9622354

Mol. Microbiol. 1998 Apr;28(2):293-303

LevR, which controls the expression of the levoperon of Bacillus subtilis, is a regulatory protein containing an N-terminal domain similar to the NifA/NtrC transcriptional activator family and a C-terminal domain similar to the regulatory part of bacterial anti-terminators, such as BgIG and LicT. Here, we demonstrate that the activity of LevR is regulated by two phosphoenolpyruvate (PEP)-dependent phosphorylation reactions catalysed by the phosphotransferase system (PTS), a transport system for sugars, polyols and other sugar derivatives. The two general components of the PTS, enzyme I and HPr, and the two soluble, sugar-specific proteins of the lev-PTS, LevD and LevE, form a signal transduction chain allowing the PEP-dependent phosphorylation of LevR, presumably at His-869. This phosphorylation seems to inhibit LevR activity and probably regulates the induction of the lev operon. Mutants in which His-869 of LevR has been replaced with a non-phosphorylatable alanine residue exhibited constitutive expression from the lev promoter, as do levD or levE mutants. In contrast, PEP-dependent phosphorylation of LevR in the presence of only the general components of the PTS, enzyme I and HPr, regulates LevR activity positively. This phosphorylation most probably occurs at His-585. Mutants in which His-585 has been replaced with an alanine had lost stimulation of LevR activity and PEP-dependent phosphorylation by enzyme I and HPr. This second phosphorylation of LevR at His-585 is presumed to play a role in carbon catabolite repression.

http://www.ncbi.nlm.nih.gov/pubmed/9622354