My lab focuses on addressing these questions using many approaches including biochemistry, structural biology and cell biology. Our ultimate goal is to identify factors needed for the precisely timed degradation of key substrates and to biochemically reconstitute regulated proteolysis using purified components. By understanding how mechanisms specific to our system enforce proper protein lifetimes, we hope to understand how regulated proteolysis is generally controlled. Furthermore, as ClpX is a member of a larger class of other molecular machines whose primary role is to aid in the proper folding of proteins, lessons learned from our studies will also shed light on a broader understanding of energy driven protein folding and unfolding.
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Versatile modes of peptide recognition by the ClpX N domain mediate alternative adaptor-binding specificities in different bacterial species (with T. Chowdhury, S. Ebrahim, R. T. Sauer, and T. A. Baker), Protein Science (2010)
ClpXP, an AAA+ protease, plays key roles in protein-quality control and many regulatory processes in...
Sinorhizobium meliloti CpdR1 is critical for co-ordinating cell cycle progression and the symbiotic chronic infection (with H. Kobayashi, N. J. Kobayashi, L. A. Simmons, and G. C. Walker), Molecular Microbiology (2009)
ATP-driven proteolysis plays a major role in regulating the bacterial cell cycle, development and stress...
Structure and substrate specificity of an SspB ortholog: design implications for AAA+ adaptors (with R. A. Grant, R. T. Sauer, and T. A. Baker), Structure (2007)
AAA+ proteases are frequently regulated by adaptors that modulate spatial and temporal control of protein...