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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 : The Journal of biological chemistry

A Novel H-NS-like protein from an antarctic psychrophilic bacterium reveals a crucial role for the N-terminal domain in thermal stability

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The Journal of biological chemistry - 13 Mar 2003

Tendeng C, Krin E, Soutourina OA, Marin A, Danchin A, Bertin PN

Link to Pubmed [PMID] – 12637536

J. Biol. Chem. 2003 May;278(21):18754-60

We describe here new members of the H-NS protein family identified in a psychrotrophic Acinetobacter spp. bacterium collected in Siberia and in a psychrophilic Psychrobacter spp. bacterium collected in Antarctica. Both are phylogenetically closely related to the HvrA and SPB Rhodobacter transcriptional regulators. Their amino acid sequence shares 40% identity, and their predicted secondary structure displays a structural and functional organization in two modules similar to that of H-NS in Escherichia coli. Remarkably, the Acinetobacter protein fully restores to the wild-type H-NS-dependent phenotypes, whereas the Psychrobacter protein is no longer able to reverse the effects of H-NS deficiency in an E. coli mutant strain above 30 degrees C. Moreover, in vitro experiments demonstrate that the ability of the Psychrobacter H-NS protein to bind curved DNA and to form dimers is altered at 37 degrees C. The construction of hybrid proteins containing the N- or the C-terminal part of E. coli H-NS fused to the C- or N-terminal part of the Psychrobacter protein demonstrates the role of the N-terminal domain in this process. Finally, circular dichroism analysis of purified H-NS proteins suggests that, as compared with the E. coli and Acinetobacter proteins, the alpha-helical domain displays weaker intermolecular interactions in the Psychrobacter protein, which may account for the low thermal stability observed at 37 degrees C.

http://www.ncbi.nlm.nih.gov/pubmed/12637536