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Rensselaer Polytechnic Institute Department of Biological Sciences
Catherine Royer
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Department of Biological Sciences
1W14 Jonsson-Rowland Science Center
Rensselaer Polytechnic Institute
110 Eighth Street
Troy, NY 12180-3590

Phone: (518) 276-6446
Fax: (518) 276-2344

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Biology Home Undergraduate Graduate Faculty Research News and Events Contacts
Catherine Royer

Professor of Biology
Professor of Chemistry and Biological Chemistry
Constellation Professor of Biocomputation and Bioinformatics

Education and Training

Ph.D. University of Illinois at Urbana-Champaign, School of Chemical Sciences
Biochemistry

Postdoctoral Training: University of Paris 7 and Centre National pour la Recherche Scientifique, Paris, France

Contact

E-mail: royerc@rpi.edu
Phone: (518) 276-3697
Fax: (518) 276-2851

Office: Center for Biotechnology and Interdisciplinary Studies Rm. 3422B
Lab: Center for Biotechnology and Interdisciplinary Studies

Rensselaer Polytechnic Institute
110 8th Street,
Troy, NY 12180

Research Interests

Protein Folding. Protein interaction networks. Transcription regulation. Quantitative imaging. Pressure effects on biomolecules.

The structure, stability and dynamic properties of biomolecules are encoded in their specific amino acid or nucleotide sequences, which in turn have been selected via evolutionary pressure. A profound understanding of the physical determinants required for specific functional properties of biomolecules is necessary to predict, design and modulate biomolecular function.

The research in my laboratory focuses on understanding the physical principles underlying biomolecular structure, dynamics and interactions. We concentrate on two major areas.

1. The energetics of protein folding. In particular we are interested in using pressure as a thermodynamic perturbation in the study of protein folding. Pressure acts to reduce volume, and hence favors conformational states on the free energy landscapes of biomolecules that occupy smaller volumes. These states can be low-lying excited states, as well as partially or fully unfolded states. We have shown that the volume differences between conformational states of proteins depend largely upon the packing efficiency of the native, folded state. Coupling high pressure with NMR, fluorescence and Small Angle X-ray Scattering has allowed for highly detailed exploration of the structural and energetic properties of proteins.

2. Protein interaction networks. The affinities and rate constants for protein interactions in cellular regulatory networks have been finely tuned throughout evolution for optimal functional properties. The work in my group focuses on the quantitative measurement of protein interaction energetics in vitro and in vivo. We use fluorescence-based experimental techniques techniques to test the effects of ligands, solution conditions, and temperature on these interactions. In vivo and in live cells, we implement and develop new advanced microscopy methods, particularly fluorescence fluctuation methods for quantitative spatial and temporal mapping of protein production and interactions, including protein complex affinities and stoichiometries. We have applied the approach to investigate noise in stochastic gene expression in a metabolic switch. While we are particularly interested in protein interactions implicated in transcriptional regulation, but have investigated membrane protein oligomerization and ribosomal protein interactions, as well.

Selected Publications

Pressure Effects on Protein Folding:

Vidugiris, G.A.J., Markley, J. L. & Royer, C. A. Evidence for a Molten-Globule-Like Transition State in Protein Folding from Determination of Activation Volumes, Biochemistry 34, 4909-4912 (1995).

Panick, G., Vidugiris, GJA, Mallessa, R., Rapp, G., Winter R. & Royer C.A. Exploring the Temperature-Pressure Phase Diagram of staphylococcal Nuclease, Biochemistry 38, 4157-4164 (1999).

Seeman, H., Winter, R. & Royer, C.A. Volume, expansivity and isothermal compressibility changes associated with temperature and pressure unfolding of staphylococcal nuclease, J. Mol. Biol 307, 1091-102 (2001).

Silva, J. L., Foguel, D. & Royer, C.A.  New Insights into protein folding, dynamics and structure from high pressure studies, TiBS 26, 612-618. (2001).

Royer, C.A. Probing Protein Folding and Conformational Transitions in Proteins with Fluorescence, Chemical Reviews 106, 1769. (2006).

Mitra, L., Hata, K., Kono, R., Maeno, A., Isom, D., Rouget, J.B., Winter, R., Akasaka, K.,Garcia-Moreno E., B. & Royer, C.A., Vi-Value Analysis: A Pressure-Based Method for Mapping the Folding Transition State Ensemble of Proteins, JACS, 129, 14108-14109, (2007).

Rouget, J.-B., Aksel, T., Roche, J., Saldana, J.-L., Garcia, A. E., Barrick, D., and Royer, C. A. Size and sequence and the volume change of protein folding, JACS, 133(15):6020-7, (2011).

Roche, J., Caro, JJ.A., Norberto D. R., Barthe, P., Roumestand, C., Schlessmann, J.L., Garcia, A.E., Garcia-Moreno E., B. & Royer, C.A.  Cavities determine the pressure unfolding of proteins, Proc. Natl. Acad. Sci. USA 109, 6945-6950 (2012).

Roche J, Dellarole M, Caro JA, Norberto DR, Garcia AE, Garcia-Moreno E B, Roumestand C, Royer CA., Effect of Internal Cavities on Folding Rates and Routes Revealed by Real-time Pressure-Jump NMR Spectroscopy. J Am Chem Soc. 2013 (in press).

Protein Interactions

Reedstrom, R. J. & Royer, C. A. Evidence for Coupled Folding and Function in trp Repressor: Physical Characterization of the AV77 Super-repressor, J. Mol. Biol. 253, 266-276 (1995).

Margeat , E., Bourdoncle , A., Raphael Margueron , Nicolas Poujol,  Cavaillès, V. & Royer, C.A.  Ligands Differentially Modulate the Protein Interactions of the Human Estrogen Receptors a and b,  J. Mol. Biol. 326, 77-92 (2003).

Bourdoncle A, Labesse G, Margueron R, Castet A, Cavailles V, Royer CA. The nuclear receptor coactivator PGC-1alpha exhibits modes of interaction with the estrogen receptor distinct from those of SRC-1. J Mol Biol. 347, 921-34, (2005).

Allemand F, Haentjens J, Chiaruttini C, Royer C, Springer M. Escherichia coli ribosomal protein L20 binds as a single monomer to its own mRNA bearing two potential binding sites. Nucleic Acids Res. 35, 3016. (2007).

Zorrilla S, Doan T, Alfonso C, Margeat E, Ortega A, Rivas G, Aymerich S, Royer CA, Declerck N. Inducer-Modulated Cooperative Binding of the Tetrameric CggR Repressor to Operator DNA. Biophys J., 92(9):3215-27. (2007).

Zorrilla S,  Ortega A, Chaix D, Alfonso C, Rivas G, Aymerich S, Lillo P, Declerck N, Royer CA, (2008) Characterization of the CcpN repressor by FCCS and other biophysical approaches, Biophys J. 95, 4403-4415, (2008).

Savatier J, Jalaguier S, Ferguson ML, Cavaillès V, Royer CA. Estrogen receptor interactions and dynamics monitored in live cells by fluorescence cross-correlation spectroscopy Biochemistry 49, 772-781 (2010).

Ferguson, M. L., Le Coq, D., Jules, M., Aymerich, S., Radulescu, O., Declerck, N., and Royer, C. A., Reconciling molecular regulatory mechanisms with noise patterns of bacterial metabolic promoters in induced and repressed states, Proc. Natl. Acad. Sci. USA 109, 155-160, (2012).

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Rensselaer Polytechnic Institute Department of Biological Sciences
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