Post Doctoral Fellowships
Joel M. Harp, Ph.D.
The University of Tennessee - Oak Ridge National Laboratory
"X-ray Crystallographic Studies of MeCP2 on a Chromatin Substrate"
Mentor: Gerard J. Bunick
2-Year Award: $100,000
Final Report (November 2003)
The MeCP2 protein recognizes a chemical signal on DNA and binds to it. Portions of the MeCP2 protein then recruit other proteins to change the structure of chromatin and silence gene expression. Chromatin is the form in which our DNA is packaged and consists of repeating units called nucleosomes. Questions of how MeCP2 binds to DNA on nucleosomes and then modifies the nucleosomes are very difficult to answer. While graduate student at the University of Tennessee and the Oak Ridge National Laboratory, I worked on the structure of the nucleosome core particle using the techniques of macromolecular crystallography. I received a fellowship from RSRF while still at Tennessee with hopes of solving the structural basis of how MeCP2 recognizes methylated DNA on the nucleosome and how it then affects the structure of chromatin. While this work is still ongoing, the RSRF Fellowship has allowed me to move twice. Once to the University of Virginia where I worked with Drs. David Allis, Sepideh Khorasanizadeh, and Fraydoon Rastinejad. There I had an opportunity to work on proteins involved in the histone code as well as work on my primary interest in MeCP2. The second move has been to Vanderbilt University where I am now Director of the Macromolecular Crystallography Facility. This position provides opportunities to continue the studies begun during the term of the RSRF Fellowship and, hopefully, to begin new collaborations with Rett Syndrome researchers.
Joel M. Harp, Ph.D.The University of Tennessee - Oak Ridge National Laboratory
"X-ray Crystallographic Studies of MeCP2 on a Chromatin Substrate"
Mentor: Gerard J. Bunick
2-Year Award: $100,000
Final Report (November 2003)
The MeCP2 protein recognizes a chemical signal on DNA and binds to it. Portions of the MeCP2 protein then recruit other proteins to change the structure of chromatin and silence gene expression. Chromatin is the form in which our DNA is packaged and consists of repeating units called nucleosomes. Questions of how MeCP2 binds to DNA on nucleosomes and then modifies the nucleosomes are very difficult to answer. While graduate student at the University of Tennessee and the Oak Ridge National Laboratory, I worked on the structure of the nucleosome core particle using the techniques of macromolecular crystallography. I received a fellowship from RSRF while still at Tennessee with hopes of solving the structural basis of how MeCP2 recognizes methylated DNA on the nucleosome and how it then affects the structure of chromatin. While this work is still ongoing, the RSRF Fellowship has allowed me to move twice. Once to the University of Virginia where I worked with Drs. David Allis, Sepideh Khorasanizadeh, and Fraydoon Rastinejad. There I had an opportunity to work on proteins involved in the histone code as well as work on my primary interest in MeCP2. The second move has been to Vanderbilt University where I am now Director of the Macromolecular Crystallography Facility. This position provides opportunities to continue the studies begun during the term of the RSRF Fellowship and, hopefully, to begin new collaborations with Rett Syndrome researchers.