La protéine MC1 d'archaeabactérie : reconnaissance de séquences particulières

Abstract : The structural MC1 protein is a small and very abundant protein in Methanisarcina thermophila. To identify DNA sequences that are recognised by this protein we have performed SELEX experiments (Systematic Evolution of Ligands by EXponential enrichment) with a pool of DNA duplexes containing a central randomised N15 region. The alignment of DNAs after 10 rounds of selection reveals a 15 bp consensus sequence. The protein affinity for the consensus sequence is about 50 times higher than for the initial pool. The binding mode of the protein on DNA has been studied by molecular footprintings (DMS, hydroxyl radicals). The protein interacts via the minor groove at two distinct sites located on the same face of the DNA. The more likely is that the protein recognises the DNA sequences via an indirect readout process. The gamma radiation-induced oxidation of certain amino acids (Trp, Met) lead to the loss of recognition of particular sequences and of bent DNA is lost.
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Submitted on : Thursday, July 28, 2005 - 1:46:20 PM
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  • HAL Id : tel-00008337, version 2

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Guillaume de Vuyst. La protéine MC1 d'archaeabactérie : reconnaissance de séquences particulières. Biochimie [q-bio.BM]. Université d'Orléans, 2004. Français. ⟨tel-00008337v2⟩

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