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Journal articles
Sequence-dependent DNA flexibility mediates DNase I cleavage.
Abstract : Understanding the preference of nonspecific proteins for certain DNA structural features requires an accurate description of the properties of free DNA, especially regarding their possible predisposition to adopt a conformation that favors the formation of a complex. Exploiting previous exhaustive NMR studies performed on free DNA oligomers, we investigated the molecular basis of DNase I sensitivity under conditions where DNase I binding limits the probability of cleavage. We showed that cleavage intensity was correlated with adjacent 3' phosphate linkage flexibility, monitored by (31)P chemical shifts. Examining NMR-refined DNA structures highlighted that sequence-dependent flexible phosphates were associated with large minor groove variations that may promote the affinity of DNase I, according to relevant DNA-protein complexes. In sum, this work demonstrates that specificity in DNA-DNase I interaction is mediated by DNA flexibility, which influences the induced-fit transitions required to form productive complexes.
Cited literature [67 references]
https://hal-pasteur.archives-ouvertes.fr/pasteur-01416864
Contributor : Marc Lavigne <>
Submitted on : Friday, July 7, 2017 - 5:03:02 PM
Last modification on : Thursday, November 19, 2020 - 8:50:29 AM
Long-term archiving on: : Thursday, December 14, 2017 - 3:40:11 PM
Contributor : Marc Lavigne <>
Submitted on : Friday, July 7, 2017 - 5:03:02 PM
Last modification on : Thursday, November 19, 2020 - 8:50:29 AM
Long-term archiving on: : Thursday, December 14, 2017 - 3:40:11 PM