Single-molecule studies of high-mobility group B architectural DNA bending proteins

Divakaran Murugesapillai, Micah J. McCauley, L James Maher III, Mark C. Williams

Research output: Contribution to journalReview article

12 Citations (Scopus)

Abstract

Protein–DNA interactions can be characterized and quantified using single molecule methods such as optical tweezers, magnetic tweezers, atomic force microscopy, and fluorescence imaging. In this review, we discuss studies that characterize the binding of high-mobility group B (HMGB) architectural proteins to single DNA molecules. We show how these studies are able to extract quantitative information regarding equilibrium binding as well as non-equilibrium binding kinetics. HMGB proteins play critical but poorly understood roles in cellular function. These roles vary from the maintenance of chromatin structure and facilitation of ribosomal RNA transcription (yeast high-mobility group 1 protein) to regulatory and packaging roles (human mitochondrial transcription factor A). We describe how these HMGB proteins bind, bend, bridge, loop and compact DNA to perform these functions. We also describe how single molecule experiments observe multiple rates for dissociation of HMGB proteins from DNA, while only one rate is observed in bulk experiments. The measured single-molecule kinetics reveals a local, microscopic mechanism by which HMGB proteins alter DNA flexibility, along with a second, much slower macroscopic rate that describes the complete dissociation of the protein from DNA.

Original languageEnglish (US)
Pages (from-to)17-40
Number of pages24
JournalBiophysical Reviews
Volume9
Issue number1
DOIs
StatePublished - Feb 1 2017

Fingerprint

High Mobility Group Proteins
DNA
Proteins
Optical Tweezers
Ribosomal RNA
Fungal Proteins
Atomic Force Microscopy
Optical Imaging
Product Packaging
Chromatin
Maintenance

Keywords

  • Bending
  • Binding
  • DNA
  • HMGB
  • Kinetics
  • Protein

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Molecular Biology

Cite this

Single-molecule studies of high-mobility group B architectural DNA bending proteins. / Murugesapillai, Divakaran; McCauley, Micah J.; Maher III, L James; Williams, Mark C.

In: Biophysical Reviews, Vol. 9, No. 1, 01.02.2017, p. 17-40.

Research output: Contribution to journalReview article

Murugesapillai, Divakaran ; McCauley, Micah J. ; Maher III, L James ; Williams, Mark C. / Single-molecule studies of high-mobility group B architectural DNA bending proteins. In: Biophysical Reviews. 2017 ; Vol. 9, No. 1. pp. 17-40.
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