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.

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.

• Authors: Max A Keniry, Elisabeth A Owen
• Journal: FEBS letters (FEBS Lett) Vol. 588 Issue 10 Pg. 1949-54 (May 21 2014) ISSN: 1873-3468 [Electronic] England
• PMID: 24735723 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Chemical References

• Oligonucleotides
• Proto-Oncogene Proteins c-myc
• Spermine

Topics

• Circular Dichroism
• G-Quadruplexes
• Gene Expression Regulation
• Magnetic Resonance Spectroscopy
• Models, Molecular
• Mutation
• Oligonucleotides (chemistry, genetics, metabolism)
• Promoter Regions, Genetic (genetics)
• Protein Binding
• Protein Conformation
• Proto-Oncogene Proteins c-myc (genetics)
• Spermine (chemistry, metabolism)