Jeffrey N. Davidson, Ph.D.
Doctoral Studies: Harvard University.
Postdoctoral: Eleanor Roosevelt Institute for Cancer Research.
The alpha fetoprotein (AFP) gene is regulated both developmentally and tissue-specifically. In collaboration with Brett Spear’s laboratory, I use genome sequence data from many mammalian species to explore the mechanisms by which the AFP gene is regulated. For example, a single nucleotide substitution in the human promoter leads to a person with life long persistent expression of AFP instead of repression after birth. Yet, normal dogs and rabbits have the nucleotide that would predict persistent expression of AFP. My research is targeted at determining whether or not the dog and rabbit AFP genes actually are repressed after birth.
Selected Recent Publications:
Long, L., J.N. Davidson, and B.T. Spear. Striking differences between the mouse and human alpha-fetoprotein enhancers. Genomics 83: 694-705 (2004).
Qiu, Y., Simmons, A., Haubner, A., Ream, A. and J.N. Davidson. Substitutions in the hamster CAD carbamoylphosphate synthetase alter allosteric response to 5-phosphoribosyl-alpha-pyrophosphate (PRPP) and UTP. Biochemical J. 378: 991-998 (2004).
Qiu, Y. and J.N. Davidson. Substitutions in the aspartate transcarbamoylase domain of hamster CAD disrupt oligomeric structure. Proc. Natl. Acad. Sci. USA 97: 97-102 (2000).
Simmons, A.J., J.M. Rawls, J. Piskur and J.N. Davidson. A mutation that uncouples allosteric regulation of carbamyl phosphate synthetase in Drosophila. J. Mol. Biol. 287: 277-286 (1999).
Qiu, Y. and J.N. Davidson. Aspartate-90 and arginine-269 of hamster aspartate transcarbamylase affect the oligomeric state of a chimaeric protein with an Escherichia coli maltose-binding domain. Biochem. J. 329: 243-247 (1998).
Davidson, J.N. and M. Peterson. Origin of genes encoding multienzymatic proteins in eukaryotes. Trends Genet. 13: 281-285 (1997).
Banerjei, L.C. and J.N. Davidson. Site-directed substitution of Ser1406 of hamster CAD with glutamic acid alters allosteric regulation of carbamyl phosphate synthetase II. Somat. Cell Mol. Genet. 23: 37-49 (1997).