Research in the Bailey laboratory focuses on the molecular basis of the processes that relate to protein nucleic acid interaction. 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.
Honors and Awards
Ho-Ching Yang Memorial Faculty Award – JHSPH (May 2010)
Johns Hopkins Presidents Frontier Award – Finalist (January 2015)
Shikani/El Hibri Prize for Discovery and Innovation – JHSPH (February 2015)
Mulepati S, Heroux A, Bailey S (2014) Crystal structure of a CRISPR RNA-guided surveillance complex bound to a ssDNA target. Science 345: 1479-1484.
Chen H, Choi J, Bailey S (2014) Independent Cut Site Selection by the Two Nuclease Domains of the Cas9 RNA-guided Endoribonuclease. J. Biol. Chem. 289: 13284-13294.
Mulepati S, Bailey S (2013) In vitro Reconstitution of the Escherichia coli RNA-guided Immune System Reveals Unidirectional, ATP-dependent degradation of DNA target. J. Biol. Chem. 288: 22184-22192.
Mulepati S, Orr A, Bailey S. (2012) Crystal Structure of the Largest Subunit of a Bacterial RNA-guided Immune Complex and its Role in DNA Target Binding. J. Biol. Chem. 287: 22445-22449.
Mulepati S, Bailey S. (2011) Structural and biochemical analysis of the nuclease domain of the clustered regularly interspaced short palindromic repeat (CRISPR) associated protein 3 (cas3). J. Biol. Chem. 286: 31896-31903.