CBIS Research Faculty
Research Faculty at CBIS
Catherine Royer

Catherine Royer

Constellation Chair

pressure effects on biomolecules, protein folding, protein interaction networks, live cell quantitative fluorescence imaging, transcription regulation

Dr. Royer obtained her Bachelors (Licence) degree in 1979 at the University of Pierre and Marie Curie - Paris 6 in Biochemistry and Chemistry. She obtained her Ph.D. in 1985 in the Department of Biochemistry in the School of Chemical Sciences at the University of Illinois at Urbana-Champaign under the direction of Professor Gregorio Weber. She carried out postdoctoral studies at the University of Paris 7, the CNRS at Gif-sur-Yvette and at LURE under the direction of Bernard Alpert, Guy Hervé and Jean-Claude Brochon. She then took a position as User Coordinator and Research Physicist at the Laboratory for Fluorescence Dynamics in the Department of Physics at the University of Illinois - Urbana Champaign. In 1990 she moved to an Assistant Professorship in the School of Pharmacy at the University of Wisconsin-Madison, where she was promoted to Associate Professor with tenure in 1995. In 1997 she took the position of INSERM Director of Research in the Center for Structural Biochemistry in Montpellier France where, in 2002, she became Associate Director of the institute and in 2007, Director. In 2013 She moved to Rensselaer Polytechnic Institute as a Professor of Biological Sciences and chaired Constellation Professor in Bioinformatics and Biocomputation.


Ph.D. University of Illinois at Urbana-Champaigne (Biochemistry)

Bachelors (Licence) degree University of Pierre and Marie Curie Paris 6 (Biochemistry and Chemistry)

Selected Publications

  • Zhang, S., Zhang, Y., Stenzoski, N., Peran, I., McCallum, S.A., Raleigh, D. & Royer, C.A. Pressure-Temperature Analysis of the Stability of the CTL9 Domain Reveals Hidden Intermediates Folding Intermediates of CTL9, Biophys. J. 2019 (in press).
  • Jenkins, K.A., Fossat, M.J., Zhang, S., Rai, D.K., Klein, S. Gillilan, R., White, Z., Gerlich, G., McCallum, S.A., Winter, R., Gruner, S.M., Barrick, D.& Royer, C.A. Consequences of Cavities on the Folding Landscape of a Repeat Protein Depend Upon Context, Proc. Natl. Acad. Sci. USA 115(35):E8153-E8161 (2018).
  • Dorsey, S., Tollis, S., Cheng, J., Black, L., Notley, S., Tyers, M. and Royer, C. A. G1/S Transcription Factor Copy Number is a Growth-Dependent Determinant of Cell Cycle Commitment in Yeast, Cell Systems, 6, 539+, (2018).
  • Zhang, Y., Berghaus, M., Klein, S., Jenkins, K., Zhang, S., McCallum, S. A., Morgan, J. E., Winter, R., Barrick, D. & Royer, C. A. High Pressure NMR and SAXS Reveals How Capping Modulates Folding Cooperativity of the pp32 Leucine Rich Repeat Protein, J. Mol. Biol. 430, 1336-1349 (2018).
  • Andra, KK, Dorsey, A, Royer, C, Menon, AK Structural mapping of fluorescently-tagged, functional nhTMEM16 scramblase in a lipid bilayer, J. Biol. Chem., RA118. 003648 (2018).
  • Møller, T.C., Hottin, J., Clerté, C., Zwier, J.M., Durroux, T., Rondard, P., Prézeau, L., Royer, C.A., Pin, J.-P., Margeat, E. & Kniazeff, J. Oligomerization of a G protein-coupled receptor in neurons controlled by its structural dynamics, Sci. Reports 8, 10414, (2018).
  • Knop, J.-M., Harish, B. Patra, S., Royer, C.A. & Winter, R., The Deep Sea Osmolyte TMAO and Macromolecular Crowders Rescue the Antiparallel Conformation of the Human Telomeric G-Quadruplex from Urea and Pressure Stress, Chemistry - A European Journal, 24, 14346-14351 (2018).
  • Roche, J., Royer, C.A. & Roumestand, C., Exploring protein conformational landscapes using high pressure NMR, Methods Enz., (in press) (2018).
  • Roche, J. & Royer, C. A. Lessons from Pressure Denaturation of Proteins, J. Royal Soc. Interface, 15, 20180244, 2018
  • Kitazawa, S., Fossat, M.J., McCallum, S.A., Garcia, A.E and Royer, C.A. NMR and Computation Reveal a Pressure-Sensitive Folded Conformation of Trp-Cage, J. Phys. Chem B., 121, 1258-1267 (2017).
  • Papini, C. & Royer, C.A., Scanning Number and Brightness Yields Absolute Protein Concentrations in Live Cells: A Crucial Parameter Controlling Functional Bio-molecular Interaction Networks, Biophysical Reviews 10, 87-96 (2018).
  • Bourges, A., Torres Montaguth, O.E., Ghosh, A., Tadesse, W.M., Declerck, N., Aertsen, A. and Royer, C.A. High pressure activation of the Mrr restriction endonuclease in Escherichia coli involves tetramer dissociation, Nuc. Acids. Res. 45, 5232-5332 (2017).
  • Gao, M., Harish, B., Berghaus, M., Seymen, R., Arns, L., McCallum, S., Royer, C. & Winter, R. Temperature and pressure limits of guanosine monophosphate self-assemblies, Scientific Rep. 7 (2017).
  • Zhang, Y., Kitazawa, S., Peran, I., Stenzoski, N., McCallum, S.A., Raleigh, D.P & Royer, C.A., High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States, J. Am. Chem. Soc., 13, 15260–15266 (2016).
  • Fossat, M. J., Dao, T. P., Jenkins, K., Dellarole, M., Yang, Y., McCallum, S. A., Garcia, A. E., Barrick, D., Roumestand, C. and Royer, C. A. High-Resolution Mapping of a Repeat Protein Folding Free Energy Landscape, Biophys. J. 111, 2368-2376 (2016).
  • Dellarole, M., Caro, J.A., Roche, J., Fossat, M., Barthe, P., Garcia-Moreno E., B. Royer, C.A. and Roumestand, C. Evolutionarily conserved pattern of interactions in a protein revealed by local thermal expansion properties, J. Am. Chem. Soc., (in press) 2015.
  • Moutin, E., Compan, V., Raynaud, F., Clerté, C., Bouquier, N., Labesse, G., Ferguson, M.,L., Fagni, L., Royer, C.A. , Perroy, J. , Stoichiometry of scaffold complexes in living neurons - DLC2 as a dimerization engine for GKAP, J. Cell Sci. 127, 3451-3462 (2014).
  • Roche J., Dellarole M., Caro J.A., Norberto D.R., Garcia A.E., Garcia-Moreno, E. B., Roumestand, C., Royer, C.A., Effect of Internal Cavities on Folding Rates and Routes Revealed by Real-time Pressure-Jump NMR Spectroscopy. J Am Chem Soc., 134, 14610-14618, (2013).
  • 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).
  • Fiche, JB., Cattoni, DI., Diekmann1, N., Langerak, J., Clerte, C., Royer, C.A., Margeat, E., Doan, T., Nöllmann, M., Recruitment, assembly and molecular architecture of the SpoIIIE DNA pump revealed by super-resolution microscopy, Plos Biology (e1001557.) (2013).
  • 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).
  • Roche J, Dellarole M, Caro JA, Guca E, Norberto DR, Yang Y, Garcia AE, Roumestand C, García-Moreno B, Royer CA. Remodeling of the folding free energy landscape of staphylococcal nuclease by cavity-creating mutations. Biochemistry. 51(47):9535-46 (2012)
  • 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, J. Am. Chem S., 133, 6020-7, (2011).
  • Ferguson, M. L., Le Coq, D., Jules, M., Aymerich, S., Declerck, N., and Royer, C. A., Absolute quantification of gene expression in individual bacterial cells using two-photon fluctuation microscopy, Anal. Biochem. 419, 250-9 (2011).
  • 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).
  • Rouget, J.B., Schroer, M.A., Jeworrek, C., Pühse, M., Saldana, J.L., Bessin, Y., Tolan, M., Barrick, D., Winter, R., Royer, C.A Unique features of the folding landscape of a repeat protein revealed by pressure perturbation, Biophys J., 98, 2712-2721. (2010).
  • le Maire, A.,Teyssier, C., Erb, C., Grimaldi, M., Alvarez, S., de Lera, A.R., Balaguer, P., Gronemeyer, H., Royer, C.A., Germain, P. & Bourguet, W. A unique secondary structure switch controls constitutive gene silencing by retinoic acid receptor, Nat Struct Mol Biol., 17, 801-807 (2010).