The dimerization state of the mammalian high mobility group protein AT-hook 2 (HMGA2)
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.
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Publication
Contributors
Frost L, Baez M A M, Harrilal C, Garabedian A, Fernandez-Lima F, Leng F
Year
2015
Journal
PLoS ONE
Volume
10
Issue
6
Pages
e0130478
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