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Interaction of a Model Peptide on Gram Negative and Gram Positive Bacterial Sliding Clamps

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André, Christophe | Martiel, Isabelle | Wolff, Philippe | Landolfo, Marie | Lorber, Bernard | Silva da Veiga, Cyrielle | Dejaegere, Annick | Dumas, Philippe | Guichard, Gilles | Olieric, Vincent | Wagner, Jérôme | Burnouf, Dominique

Edité par CCSD ; American Chemical Society -

International audience. Bacterial sliding clamps control the access of DNA polymerases to the replication fork and are appealing molecular targets for antibacterial drugs development. To this end, it is critical to decipher the polymerase-clamp binding mode across various bacterial species. We showed previously that synthetic peptides targeting the clamp binding pocket of Gram-bacteria poorly interact with that of Gram+ homologous proteins. Here we analyzed the interaction of a reference peptide with several E. coli and B. subtilis clamp variants. For both Gram-and Gram+ pockets, the peptide binds through an induced-fit process but the complex stability

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Correction: Antibacterial activity of a dual peptide targeting the Escherichia coli sliding clamp and the ribosome

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International audience. Correction for ‘Antibacterial activity of a dual peptide targeting the Escherichia coli sliding clamp and the ribosome’ by Christophe André et al. , RSC Chem. Biol. , 2020, 1 , 137–147, DOI: ...

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