The Dimerization State of the Mammalian High Mobility Group Protein AT-Hook 2 (HMGA2)

PLoS One. 2015 Jun 26;10(6):e0130478. doi: 10.1371/journal.pone.0130478. eCollection 2015.


The mammalian high mobility group protein AT-hook 2 (HMGA2) is a chromosomal architectural transcription factor involved in cell transformation and oncogenesis. It consists of three positively charged "AT-hooks" and a negatively charged C-terminus. Sequence analyses, circular dichroism experiments, and gel-filtration studies showed that HMGA2, in the native state, does not have a defined secondary or tertiary structure. Surprisingly, using combined approaches of 1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride (EDC) chemical cross-linking, analytical ultracentrifugation, fluorescence resonance energy transfer (FRET), and mass spectrometry, we discovered that HMGA2 is capable of self-associating into homodimers in aqueous buffer solution. Our results showed that electrostatic interactions between the positively charged "AT-hooks" and the negatively charged C-terminus greatly contribute to the homodimer formation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Circular Dichroism
  • Dimerization
  • Ethyldimethylaminopropyl Carbodiimide / chemistry
  • Fluorescence Resonance Energy Transfer
  • HMGA2 Protein / chemistry*
  • Hydrodynamics
  • Mass Spectrometry
  • Mice


  • HMGA2 Protein
  • Ethyldimethylaminopropyl Carbodiimide