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 these 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.

Genome Integrity, X-ray crystallography, Structural Biology, Nucleic Acid

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

Durniak, K.J., Bailey, S., and Steitz, T.A. (2008) The Structure of a Transcribing T7 RNA Polymerase in Transition from Initiation to Elongation. Science 322: 553-557.

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

Bailey, S., Eliason, W.A. and Steitz, T.A. (2007). Structure of Hexameric DnaB Helicase and its Complex with a Domain of DnaG Primase. Science 318: 459-463.

Bailey, S., Eliason, W.A. and Steitz, T.A. (2007). The Crystal Structure of the Thermus aquaticus DnaB Helicase Monomer. Nucleic Acids Res. 35: 4728-4736.

Bailey, S., Wing, R.A. and Steitz, T.A. (2006). The Structure of T. aquaticus DNA Polymerase III Is Distinct from Eukaryotic Replicative DNA Polymerases. Cell 126: 893-904.

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

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

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

Bailey, S., Sedelnikova, S.E., Blackburn, G.M., Abdelghany, H.M., Baker, P.J., McLennan, A.G. and Rafferty, J.B. (2002). The crystal structure of diadenosine tetraphosphate hydrolase from Caenorhabditis elegans in free and binary complex forms. Structure. 10: 589-600.

Bailey, S., Sedelnikova, S.E., Blackburn, G.M., Abdelghany, H.M., McLennan, A.G. and Rafferty, J.B. (2002). Crystallization of a complex of Caenorhabditis elegans diadenosine tetraphosphate hydrolase and a non-hydrolysable substrate analogue, AppCH2ppA. Acta. Crystallogr. D58: 526-528.

Abdelghany, H.M., Gasmi, L., Cartwright, J.L., Bailey, S., Rafferty, J.B. and McLennan, A.G. (2001) Cloning, characterization and crystallization of a diadenosine 5’5”’-P1,P4-tetraphosphate pyrophosphohydrolase from Caenorhabditis elegans. Biochem. Biophys. Acta. 1550: 27-36.