DnaJ (Hsp40 Protein) Binding to Folded Substrate Impacts KplE1 Prophage Excision Efficiency
Résumé
Background: DnaJ positively modulates KplE1 prophage excision and is involved in lysogeny escape. Results: The recombination directionality factor TorI, from KplE1 prophage, interacts with the DnaJ chaperone, and they protect each other from limited trypsin digestion. Conclusion: DnaJ stabilizes TorI recombination directionality factor conformation. Significance: DnaJ cochaperone can bind folded substrates and induces the conformational stabilization of the TorI protein.
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