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Issue 9, 2014
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Structure, mechanics, and binding mode heterogeneity of LEDGF/p75–DNA nucleoprotein complexes revealed by scanning force microscopy

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Abstract

LEDGF/p75 is a transcriptional coactivator implicated in the pathogenesis of AIDS and leukemia. In these contexts, LEDGF/p75 acts as a cofactor by tethering protein cargo to transcriptionally active regions in the human genome. Our study – based on scanning force microscopy (SFM) imaging – is the first to provide structural information on the interaction of LEDGF/p75 with DNA. Two novel approaches that allow obtaining insights into the DNA conformation inside nucleoprotein complexes revealed (1) that LEDGF/p75 can bind at least in three different binding modes, (2) how DNA topology and protein dimerization affect these binding modes, and (3) geometrical and mechanical aspects of the nucleoprotein complexes. These structural and mechanical details will help us to better understand the cellular mechanisms of LEDGF/p75 as a transcriptional coactivator and as a cofactor in disease.

Graphical abstract: Structure, mechanics, and binding mode heterogeneity of LEDGF/p75–DNA nucleoprotein complexes revealed by scanning force microscopy

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Supplementary files

Article information


Submitted
02 Jan 2014
Accepted
21 Jan 2014
First published
29 Jan 2014

This article is Open Access

Nanoscale, 2014,6, 4611-4619
Article type
Paper
Author version available

Structure, mechanics, and binding mode heterogeneity of LEDGF/p75–DNA nucleoprotein complexes revealed by scanning force microscopy

W. Vanderlinden, J. Lipfert, J. Demeulemeester, Z. Debyser and S. De Feyter, Nanoscale, 2014, 6, 4611
DOI: 10.1039/C4NR00022F

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