Research Summary - Our lab is using biophysical methods and molecular biology to study protein-nucleic acid interactions and macromolecular assembly. We are particularly interested in mechanisms of assembly and how kinetics and equilibria influence the final composition of assembly complexes and ultimately biological function. Experiments are aimed at determining the detailed function of proteins and how they recognize nucleic acids. These processes are studied by steady-state and life-time fluorescence measurements, circular dichroism, rapid scanning stopped-flow, and site-directed mutagenesis. Detailed quantitative measurements of these biological processes lead to elucidation of molecular mechanisms and how these processes can be regulated.

Selected publications

Scheper, G.C. van Kollenburg, B. Hu, J. Luo, Y., Goss, D.J. and Proud, C.G. (2002) Phosphorylation of eukaryotic initiation factor 4E markedly reduces its affinity for capped mRNA. J. Biol. Chem. 277, 3303-3309.

Spivak-Kroizman, T., Friedland, D.E., De Staercke, C., Gernert, K. M., Goss, D.J. and Hagedorn, C.H. (2002) Mutations in the S4-H2 loop of eIF4E which increase the affinity for m7GTP. FEBS Letters 25892, 1-6.

Khan, M.A. and Goss, D.J. (2004) "Phosphorylation States of Translational Initiation Factors Affect mRNA Cap Binding in Wheat" Biochemistry 43, 9092-9097.

Khan, M.A. and Goss, D.J. (2005) "Translation Initiation Factor (eIF4B) Affects the Rates of binding of the mRNA m7G cap Analogue to Wheat Germ eIFiso4F and eIFiso4F-PABP" Biochemistry 44, 4510-4516.

Friedland, D.E., Wooten, W.N.B., LaVoy, J.E., Hagedorn, C.H. and Goss, D.J. (2005) "A Mutant of Eukaryotic Protein Synthesis Initiation Factor eIF4EK119A ­­has an Increase Binding Affinity for both m7G Cap Analogues and eIF4G Peptides" Biochemistry 44, 4546-4550.