Enhanced electrostatic force microscopy reveals higher-order DNA looping mediated by the telomeric protein TRF2

Shelterin protein TRF2 modulates telomere structures by promoting dsDNA compaction and T-loop formation. Advancement of our understanding of the mechanism underlying TRF2-mediated DNA compaction requires additional information regarding DNA paths in TRF2-DNA complexes. To uncover the location of DNA...

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Veröffentlicht in:	Scientific reports 2016-02, Vol.6 (1), p.20513-20513, Article 20513
Hauptverfasser:	Kaur, Parminder, Wu, Dong, Lin, Jiangguo, Countryman, Preston, Bradford, Kira C., Erie, Dorothy A., Riehn, Robert, Opresko, Patricia L., Wang, Hong
Format:	Artikel
Sprache:	eng
Schlagworte:	631/1647/2204 631/57/2265 Chromatin Compaction Deoxyribonucleic acid DNA DNA - chemistry DNA - metabolism Electrostatic properties HeLa Cells Histones Humanities and Social Sciences Humans Microscopy multidisciplinary Multiprotein Complexes - chemistry Multiprotein Complexes - metabolism Nucleic Acid Conformation Proteins Science Static Electricity Structure-function relationships Telomere-binding protein Telomeric Repeat Binding Protein 2 - chemistry Telomeric Repeat Binding Protein 2 - metabolism TRF2 protein
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