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Caractérisation d'une protéine de fonction inconnue, YdiB de Bacillus subtilis, membre d'une nouvelle famille d'ATPases exclusivement bactériennes

Johanna Karst 1
1 LPM - Laboratoire des Protéines Membranaires
IBS - UMR 5075 - Institut de biologie structurale
Abstract : We have studied an enzyme of Bacillus subtilis, YdiB, of unknown function. The gene, specifically prokaryote and essential in several species, makes YdiB a good target for the research of new anti-bacterial drugs.
We made a full knock-out of ydiB in B. subtilis, and its growth was strongly reduced. YdiB exhibited a low ATPase activity that was specific to the protein because it was abrogated by a mutation of an invariant residue in the active site. Different techniques revealed that YdiB forms oligomers, and similar results were found with YjeE, the E. coli orthologue. The addition of salt displaced the equilibrium towards the monomer, that is more active than the dimeric/multimeric form of the enzyme. The dimeric form was also detected by in vivo cross-linking experiments. Finally, we tried to find cellular partners of YdiB and preliminary results suggest a possible role in a stress response, or an interaction with the ribosome.
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Submitted on : Thursday, January 10, 2008 - 8:41:34 AM
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Johanna Karst. Caractérisation d'une protéine de fonction inconnue, YdiB de Bacillus subtilis, membre d'une nouvelle famille d'ATPases exclusivement bactériennes. Biochimie [q-bio.BM]. Université Joseph-Fourier - Grenoble I, 2007. Français. ⟨tel-00203404⟩

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