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

dc.rights.licenseopenen_US
dc.contributor.authorANDRÉ, Christophe
dc.contributor.authorMARTIEL, Isabelle
dc.contributor.authorWOLFF, Philippe
dc.contributor.authorLANDOLFO, Marie
dc.contributor.authorLORBER, Bernard
dc.contributor.authorSILVA DA VEIGA, Cyrielle
dc.contributor.authorDEJAEGERE, Annick
dc.contributor.authorDUMAS, Philippe
dc.contributor.authorGUICHARD, Gilles
dc.contributor.authorOLIÉRIC, Vincent
dc.contributor.authorWAGNER, Jérôme
dc.contributor.authorBURNOUF, Dominique Y.
dc.date.accessioned2019
dc.date.available2019
dc.date.issued2019
dc.identifier.issn2373-8227en_US
dc.identifier.other10.1021/acsinfecdis.9b00089en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/3839
dc.description.abstractEnBacterial sliding clamps control the access of DNA polymerases to the replication fork and are appealing targets for antibacterial drug development. It is therefore essential to decipher the polymerase-clamp binding mode across various bacterial species. Here, two residues of the E. coli clamp binding pocket, EcS346 and EcM362, and their cognate residues in M. tuberculosis and B. subtilis clamps, were mutated. The effects of these mutations on the interaction of a model peptide with these variant clamps were evaluated by thermodynamic, molecular dynamics, X-rays crystallography, and biochemical analyses. EcM362 and corresponding residues in Gram positive clamps occupy a strategic position where a mobile residue is essential for an efficient peptide interaction. EcS346 has a more subtle function that modulates the pocket folding dynamics, while the equivalent residue in B. subtilis is essential for polymerase activity and might therefore be a Gram positive-specific molecular marker. Finally, the peptide binds through an induced-fit process to Gram negative and positive pockets, but the complex stability varies according to a pocket-specific network of interactions.
dc.language.isoENen_US
dc.subject.ensliding clamp
dc.subject.enligand−target interaction
dc.subject.ennew antibacterials development
dc.subject.enITC
dc.title.enInteraction of a Model Peptide on Gram Negative and Gram Positive Bacterial Sliding Clamps
dc.title.alternativeACS Infect. Dis.en_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1021/acsinfecdis.9b00089
dc.subject.halChimie/Matériauxen_US
bordeaux.journalACS infectious diseasesen_US
bordeaux.page1022-1034en_US
bordeaux.volume5en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248
bordeaux.issue6en_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-03182055
hal.version1
hal.date.transferred2021-03-26T09:11:57Z
hal.exporttrue
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