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Department of Chemistry & Biochemistry
The University of Texas at Austin
1 University Station A5300
Austin, TX 78712-0165





















Contact Information


Office: MBB: 2.148
Phone: 471-1514

Lab


Office: MBB 2.148
Phone: 471-1517
Fax: 232-3432

Rick Russell


rick_russell@mail.utexas.edu
Associate Professor, Faculty


Research Group


Russell Lab

Education


PhD, Johns Hopkins University, 1997
BA, Earlham College, 1991

Affiliations


Institute for Cellular and Molecular Biology;

RNA folding and chaperone proteins


Our group combines biochemical and biophysical approaches to study the processes of RNA folding and assembly with proteins. Some of nature's most complex and important enzyme machines are composed of RNA and protein. For these machines to function, each RNA and protein component must fold to its correct three-dimensional structure and all must assemble into a macromolecular complex. The goal of our research is to obtain a quantitative and rigorous molecular understanding of the processes and principles that govern RNA folding and assembly with proteins. We are also interested in RNA chaperones, proteins that are not required for function of the final complex but assist in RNA folding. The approaches used in the lab range from monitoring enzyme activity, which can be a powerful and specific probe for formation of a native structure, to single molecule fluorescence, which allows sensitive detection and characterization of folding and assembly intermediates.

Representative Publications



Mertz, J.A., Chadee, A.B., Byun, H., Russell, R., and Dudley, J.P. "Mapping of the functional boundaries and secondary structure of the Murine Mammary Tumor Virus Rem-responsive element." J. Biol. Chem. 284 (2009): 25642-25652.

Russell, R. "RNA misfolding and the action of chaperones" Frontiers in Bioscience 13 (2008): 1-20.

Chen, Y., Potratz, J.P., Tijerina, P., Del Campo, M., Lambowitz, A.M., and Russell, R. "DEAD-box Proteins can completely separate an RNA duplex using a single ATP" Proc. Natl. Acad. Sci. U.S.A. 105 (2008): 20203-20208.

Bevilacqua, P.C. and Russell, R. "Exploring the vast dynamic range of RNA dynamics" Curr. Opin. Chem. Biol. 12 (2008): 601-603.

Bhaskaran, H., and Russell R. "Kinetic redistribution of native and misfolded RNAs by a DEAD-box chaperone" Nature 449 (2007): 1014-1018.

Grohman, J.K., Del Campo, M., Bhaskaran, H., Tijerina, P., Lambowitz, A.M., and Russell, R. "Probing the mechanisms of DEAD-box proteins as general RNA chaperones: The C-terminal domain of CYT-19 mediates general recognition of RNA" Biochemistry 46 (2007): 3013-3022.

Lee, J.C., Gutell, R.R., Russell, R. "The UAA/GAN internal loop motif: A new RNA structural element that forms a cross-strand AAA stack and long-range tertiary interactions" J. Mol. Biol. 360 (2006): 978-988.

Tijerina, P., Bhaskaran, H., and Russell, R. "Non-specific binding to structured RNA and preferential unwinding of an exposed helix by the CYT-19 protein, a DEAD-box RNA chaperone" Proc. Natl. Acad. Sci. U.S.A. 103 (2006): 16698-16703.

Russell, R., Das, R., Suh, H., Travers, K., Laederach, A., Engelhardt, M., and Herschlag, D. "The paradoxical behavior of a highly structured misfolded intermediate in RNA folding" J. Mol. Biol. 363 (2006): 531-544.

Johnson, T.H., Tijerina, P., Chadee, A.B., Herschlag, D., and Russell, R. "Structural specificity conferred by a group I RNA peripheral element" Proc. Natl. Acad. Sci. U.S.A. 102 (2005): 10176-10181.