Assistant Professor
Department of Biochemistry and Molecular Biology
Bloomberg School of Public Health

scbailey@jhsph.edu

W8708 Hygiene Building
615 N. Wolfe Street Street
Baltimore, MD 21205

Office: 410-614-4742
Lab: 410-614-4894

Maintaining the integrity of genetic information is a fundamental requirement for the life of a cell and the survival of a species.  Cellular DNA is continuously subjected to insult from both exogenous and endogenous sources.  Thus the repair or tolerance of theses insults is a necessity for the cell.  Research in my laboratory focuses on the molecular basis of the processes that relate to genome integrity.  The strategy that we use is based primarily on structural studies using X-ray crystallography.  A central premise of our work is that in order for structural studies to provide understanding of these processes we must know the structure of the entire assembly that executes the process, captured at each step in the process.  From such studies we derive mechanistic models relating the physical features and chemistry of proteins and nucleic acids to their function.  Interrogation of these models using mutagenesis, biochemistry and cell-based techniques further relates structure to function and provides a more complete molecular description of the process at hand.

Selected Publications
Yin, F.F., S. Bailey, C.A. Innis, M. Ciubotaru, S. Kamtekar, T.A. Steitz, and D.G. Schatz. (2009) Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis. Nat. Struct. Mol. Biol. 16:499-508.

Durniak, K.J., S. Bailey, and T.A. Steitz. (2008) The structure of a transcribing T7 RNA polymerase in transition from initiation to elongation. Science 322:553-557.

Wing, R.A., S. Bailey, and T.A. Steitz. (2008) Insights into the replisome from the structure of a ternary complex of the DNA polymerase III alpha-subunit. J. Mol. Biol. 382:859-869.

Evans, R.N., G. Blaha, S. Bailey, and T.A. Steitz. (2008) The structure of LepA, the ribosomal back translocate. Proc. Natl. Acad. Sci. USA 105:4673-4678.

Bailey, S., W.A. Eliason, and T.A. Steitz. (2007) Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science 318:459-463.

Bailey, S., W.A. Eliason, and T.A. Steitz. (2007) The crystal structure of the Thermus aquaticus DnaB helicase monomer. Nucleic Acids Res. 35:4728-4736.

Bailey, S., R.A. Wing, and T.A. Steitz. (2006) The structure of T. aquaticus DNA Polymerase III is distinct from eukaryotic replicative DNA polymerases. Cell 126:893-904.

Bailey, S., S.E. Sedelnikova, P. Mesa, S. Ayora, J.P. Waltho, A.E. Aschroft, A.J. Baron, J.C. Alonso, and J.B. Rafferty. (2003) Structural analysis of Bacillus subtilis SPP1 phage helicase loader protein G39P. J. Biol. Chem. 278:15304-15312.

Bailey, S., S.E. Sedelnikova, P. Mesa, S. Ayora, J.C. Alonso, and J.B. Rafferty. (2003) Crystallization of the Bacillus subtilis SPP1 bacteriophage helicase loader protein G39P. Acta. Crystallogr. D59:1090-1092.

Abdelghany, H.M., S. Bailey, G.M. Blackburn, J.B. Raffertry, and A.G. McLennan. (2003) Analysis of the catalytic and binding residues of the diadenosine tetraphosphate pyrophosphohydrolase from Caenorhabditis elegans. J. Biol. Chem. 278:4435-4439.