Title: Phosphate backbone neutralization increases duplex DNA flexibility: a model for protein binding.

Authors: Okonogi, Tamara M; Alley, Stephen C; Harwood, Eric A; Hopkins, Paul B; Robinson, Bruce H

Published In Proc Natl Acad Sci U S A, (2002 Apr 2)

Abstract: An important component of protein-DNA recognition is the charge neutralization of DNA backbone phosphates and subsequent protein-induced DNA bending. Replacement of phosphates by neutral methylphosphonates has previously been shown to be a model for protein-induced bending. In addition to bending, the neutralization process may change the inherent flexibility of the DNA--a feature never before tested. We have developed a method to measure the differential flexibility of duplex DNA when methylphosphonate substitutions are made and find that the local flexibility is increased up to 40%. These results imply that backbone-neutralization-dependent DNA flexibility augments DNA-binding motifs in protein-DNA recognition processes.

PubMed ID: 11929991

MeSH Terms: No MeSH terms associated with this publication