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

Christophe André (1) , Isabelle Martiel (2) , Philippe Wolff (3) , Marie Landolfo (3) , Bernard Lorber (3) , Cyrielle Silva da Veiga (3) , Annick Dejaegere (4) , Philippe Dumas (5) , Gilles Guichard (6) , Vincent Olieric (2) , Jérôme Wagner (7) , Dominique Burnouf (3)

1 IBMM - Institut des Biomolécules Max Mousseron [Pôle Chimie Balard]
2 SLS-PSI - The Swiss Light Source (SLS)
3 ARN - Architecture et Réactivité de l'ARN
4 IGBMC - Institut de génétique et biologie moléculaire et cellulaire
5 CINaM - Centre Interdisciplinaire de Nanoscience de Marseille
6 ICT - Immunologie et chimie thérapeutiques
7 BSC - Biotechnologie et signalisation cellulaire

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

Mots clés: sliding clamp; ITC; kinITC

Domaines: Biophysique; Biochimie [q-bio.BM]; Bactériologie; Matériaux

Christophe André, Isabelle Martiel, Philippe Wolff, Marie Landolfo, Bernard Lorber, et al.. Interaction of a Model Peptide on Gram Negative and Gram Positive Bacterial Sliding Clamps. ACS Infectious Diseases, 2019, 5 (6), pp.1022-1034. ⟨10.1021/acsinfecdis.9b00089⟩. ⟨hal-02379658⟩