Rick Russell

Molecular Biosciences

RNA Folding And Chaperone Proteins

Phone: 512-471-1514

Office Location
MBB 2.212

Postal Address
100 E. 24th Street Stop A5000
Austin, TX 78712

Ph.D., Johns Hopkins University (1997)
B.A., Earlham College (1991)

Research Interests

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

Mallam, A.L., Jarmoskaite, I., Tijerina, P., Del Campo, M., Siefert, S., Guo, L., Russell, R., and Lambowitz, A.M. (2011) Solution structures of DEAD-box RNA chaperones reveal conformational changes and nucleic acid tethering by a basic tail. Proc. Natl. Acad. Sci. U.S.A., in press.

Potratz, J.P., Del Campo, M., Wolf, R.Z., Lambowitz, A.M., and Russell, R. (2011) ATP-dependent roles of the DEAD-box protein Mss116p in group II intron splicing in vitro and in vivo. J. Mol. Biol. 411, 661-679.

Wan, Y., and Russell, R. (2011) Enhanced specificity against misfolding in a thermostable mutant of the Tetrahymena ribozyme. Biochemistry 50, 864-874.

Jarmoskaite, I., and Russell, R. (2011) DEAD-box proteins as RNA helicases and RNA chaperones. WIREs: RNA 2, 135-152.

Pan, C., and Russell, R. (2010) Roles of DEAD-box Proteins in RNA and RNP Folding. RNA Biol. 7, 28-37.

Wan, Y., Suh, H., Russell, R., and Herschlag, D. (2010) Multiple unfolding events during folding of the Tetrahymena group I ribozyme. J. Mol. Biol. 400, 1067-1077.

Chadee, A.B., Bhaskaran, H., and Russell, R. (2010) Protein roles in group I intron RNA folding: The tyrosyl-tRNA synthetase CYT-18 stabilizes the native state relative to a long-lived misfolded structure without compromising folding kinetics. J. Mol. Biol. 395, 656-670.

Flores, S.C., Wan, Y., Russell, R., and Altman, R.B. (2010) Predicting RNA structure by multiple template homology modeling. Pac. Symp. Biocomput., 2010, 216-227.

Wan, Y., Mitchell, D., and Russell, R. (2009) Catalytic activity as a probe of native RNA folding. Methods Enzymol. 468, 195-218.

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

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

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

Del Campo, M., Tijerina, P., Bhaskaran, H., Mohr, S., Yang, Q., Jankowsky, E., Russell, R., and Lambowitz, A.M. (2007) Do DEAD-box proteins promote group II intron splicing without unwinding RNA? Molecular Cell 28, 159-166.

Tijerina, P., Mohr, S., and Russell, R. (2007) DMS footprinting of structured RNAs and RNA-protein complexes. Nature Protocols 2, 2608-23.