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The flanking sequence contributes to the immobilisation of spermine at the G-quadruplex in the NHE (nuclease hypersensitivity element) III1 of the c-Myc promoter
Authors:Max A. Keniry  Elisabeth A. Owen
Affiliation:Research School of Chemistry, The Australian National University, Canberra, ACT 0200, Australia
Abstract:Defining the molecular basis of the DNA sequence selectivity of polyamine binding is central to understanding polyamine-dependent gene expression. We have studied, by selective NMR experiments, the variation of spermine mobility and conformation in the presence of G-quadruplexes formed by sequences of the purine-rich strand of the c-Myc promoter, nuclease hypersensitivity element III1 (NHE III1). All the NHE quadruplexes restrict spermine mobility and induce a spermine conformational change but the most effective immobilisation occurs when all five G-tracts of the NHE III1 are present. This suggests structure within the nucleotides flanking the G-quadruplex has a role in immobilising spermine.
Keywords:bp, base-pair   CD, circular dichroism   NHE III1, nuclease hypersensitivity element III1   NMR, nuclear magnetic resonance   NOE, Nuclear Overhauser Effect   NOESY, Nuclear Overhauser Effect spectroscopy   nt, nucleotide   SCP, selective cross-polarisation   TBA, thrombin-binding aptamer   TOCSY, total correlation spectroscopy
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