Research Interests       Publications

The High Mobility Group A (HMGA) proteins are a class of nonhistone chromatin binding proteins that mediate neoplastic transformation. The Sumter lab is interested in elucidating the mechanism by which thiese proteins mediate transformation. To do so, we are identifying the domains and specific amino acids of HMGA1 that are critical for its DNA binding and transforming properties. We have identified several putative HMGA1a target genes and our preliminary results show that a protein variant lacking two of the AT hook DNA binding regions of the protein is capable of transforming cells with an efficiency comparable to wild-type. Further investigations of this finding are currently being conducted. We are also investigating the role that various post-translational modifications of HMGA1 play in the protein's ability to modulate chromatin structure and mediate neoplastic transformation. This work is currently funded by the National Science Foundation and will provide essential information regarding the importance of post-translational modification in regulating the function of various nuclear proteins. It is likely that understanding of the protein's mechanism in cancer initiation will facilitate the development of effective treatment therapies.

Students in my lab typically major in biology and/or chemistry and receive extensive training in molecular biology techniques such as cloning, mutagenesis, protein purification, transfection, tissue culture, and electrophoretic mobility shift assays. Several students are also evaluating the DNA binding properties of wild-type and mutant HMGA1 using fluorescence spectroscopy.

Julie Burton (now in medical school), Veda Evans, Kelly Pace, and Richard Anderson presented their research locally and at national meetings.