Rodrigo Maillard
Office: 518 Regents Hall
Phone: 202-784-7146
Fax: 202-687-6209
ram279@georgetown.edu
Education/Background
B. Sc. 2002, Universidad Peruana Cayetano Heredia (Lima, Peru)
Ph.D. 2007, The University of Texas Medical Branch, Galveston
Postdoctoral Fellow 2007-2013, University of California, Berkeley
Research Interests
Mechanochemistry of Signaling
The ability of cells to grow, differentiate or survive to changes in their surrounding largely depends on the activity of signaling complexes. These signaling complexes mediate an extracellular stimulus or “signal” and the subsequent activation of intracellular proteins and other biomolecules, resulting in the regulation of gene expression, cell division or apoptosis (programmed cell death). Signaling complexes are composed of cell receptors, small ligands, lipids, membranes, and allosteric proteins. The carefully controlled spatial and temporal interactions among these macromolecules allow cells to respond and adapt to changes in their environment.
The Maillard laboratory is interested in studying the dynamics, energetics and mechanics of the macromolecular interactions occurring in signaling pathways. To quantify the interactions between small ligands, allosteric protein complexes and membranes, my laboratory uses various approaches including biochemical, bulk biophysical (spectroscopic and calorimetric) and single-molecule methods. In particular, we use novel optical tweezers instrumentation that allows the mechanical manipulation and application of force to individual biological macromolecules in order to study their dynamic behavior and functional mechanisms.
Selected Publications
Maillard RA, Liu T, Beasley DW, Barrett AD, Hilser V. and Lee JC. A Thermodynamic Mechanism for the Resistance to Antibody Neutralization in Flaviviruses. J Am Chem Soc. (in press DOI: 10.1021/ja503318x)
Bustamante CJ, Kaiser CM, Maillard RA, Goldman DH, Wilson CA (2014). Mechanisms of cellular proteostasis: insights from single-molecule approaches. Annu Rev Biophys. 43: 119-140
Sen M**, Maillard RA**, Nyquist K**, Rodriguez-Aliaga P, Pressé S, Martin A, Bustamante C (2013). The ClpXP protease unfolds substrates using a constant rate of pulling but different gears. Cell 155 (3): 636-646 (2013)
**Authors contributed equally to this work
Featured article in Cell (same volume) in ClpX Shifts into High Gear to Unfold Stable Proteins
Yu S, Maillard RA, Gibenko AV, Lee JC (2012). The N-terminal Capping Propensities of the D-helix Modulate the Allosteric Activation of the Escherichia coli cAMP Receptor Protein J. Biol. Chem. 287 (47): 39402-39411
Maillard RA, Chistol G, Sen M, Righini M, Tan J, Kaiser CM, Hodges C, Martin A, Bustamante C. (2011). ClpX(P) generates mechanical force to unfold and translocate its protein substrates. Cell 29 (3): 459-469
Featured article in Cell (same volume) in Protease Power Strokes Force Proteins to Unfold
Highlighted in Biopolymers (2011) 9 (8): III-IV
Zhang S, Evgeniy I, Maillard R, Gromowski G, Volk D, Schein C, Huang C, Gorenstein D, Lee JC, Barrett AD, Beasley DW (2010). Role of BC loop residues in structure, function and antigenicity of the West Nile virus envelope protein receptor-binding domain III. Virology 403 (1): 85-91
Maillard RA, Jordan M, Beasley DW, Barrett AD, Lee JC. (2008). Long Range Communication in the Envelope Protein Domain III and Its Effect on the Resistance of West Nile Virus to Antibody-mediated Neutralization. J Biol Chem. 283 (1): 613-622
Galletto R, Jezewska MJ, Maillard R and Wlodzimierz Bujalowski (2005). The Nucleotide-Binding Site of the Escherichia coli DnaC Protein. Molecular Topography of DnaC Protein – Nucleotide Cofactors Complexes. Cell Biochemistry and Biophysics 43 (3): 331-353
Galletto R, Maillard R, Jezewska MJ and Wlodzimierz Bujalowski (2004). Global Conformation of the Escherichia coli Replication Factor DnaC Protein in Absence and Presence of Nucleotide Cofactors. Biochemistry 43 (34): 10988-11001