Wayne Anderson, PhD

Professor of Molecular Pharmacology & Biological Chemistry
Feinberg School of Medicine

Research Interests:
The interactions of proteins with nucleic acids, other proteins and small molecule ligands are central to the molecular basis of genetics. A molecular understanding of these interactions requires a knowledge of both three dimensional structures and biological functions of the molecules involved.

One area of work in the laboratory of Wayne Anderson is in protein-nucleic acid interactions and their roles in biological processes. Research is aimed at determining how protein-nucleic acid interactions affect the accuracy of replication and the consequences of DNA modification by mutagens and carcinogens. They have recently determined the structure of the E. coli DNA polymerase II, which is related to the human replicative polymerases. The crystal structure has revealed the arrangement of the polymerase and proofreading exonuclease active sites. The structure suggests how the enzyme binds DNA and further work will provide information on the mechanisms that contribute to the fidelity of replication.

Genome sequencing projects are producing a large database of sequence information. The next logical step in this process is determination of the biochemical functions and the structures of the encoded proteins. For many proteins sequence comparisons can identify a family of related proteins and allow tentative assignment of function. However, a large number of proteins are left with no known function. Our aim is determining the structures of selected proteins that are conserved in a wide range of species but belong to protein sequence families that have no structurally characterized members. This will help complete the catalog of protein structures as well as provide important information for functional studies. It is not surprising that many of these proteins are involved in the maintenance or regulation of expression of the genetic material.