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Rick Russell

Molecular Biosciences

RNA Folding And Chaperone Proteins


Phone: 512-471-1514

Office Location
MBB 2.212

Postal Address
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

Strohkendl, I., Saifudden, F., Rybarski, J.R., Finkelstein, I.J., and Russell, R. (2018) Kinetic basis for DNA target specificity of CRISPR-Cas12a. Molecular Cell 71, 816-824.

Gracia, B., Al-Hashimi, H.M., Bisaria, N., Das, R., Herschlag, D., and Russell, R. (2018) Hidden structural modules in a cooperative RNA folding transition. Cell Reports 22, 3240-3250

Yangyuoru, P.M., Bradburn, D.A., Liu, Z., Xiao, T.S., and Russell, R. (2018) DHX36 disrupts DNA G-quadruplexes with high efficiency and specificity using a translocation-based helicase mechanism. J Biol Chem 293, 1924-1932.

Gilman, B., Tijerina, P., and Russell, R. (2017) Distinct RNA unwinding mechanisms of DEAD-box and DEAH-box RNA helicase proteins in remodeling structured RNAs and RNPs. Biochem Soc Trans 45, 1313-1321.

Busa, V.F., Rector, M.J., and Russell, R. (2017) The DEAD-box protein CYT-19 uses arginine residues in its C-tail to tether RNA substrates. Biochemistry 56, 3571-3578.

Gracia, B., Xue, Y., Bisaria, N., Herschlag, D., Al-Hashimi, H.M., and Russell, R. (2016) Modulation of local RNA folding allows control of RNA assembly pathway and rate. Mol Biol 428, 3972-3985.

Cannon, B., Kachroo, A., Jayaram, M., and Russell, R. (2015) Hexapeptides that inhibit processing of branched DNA structures induce a dynamic ensemble of Holliday junction conformations. J. Biol. Chem. 290, 22734-46.

Pan, C., Potratz, J.P., Cannon, B., Simpson, Z.B., Ziehr, J., Tijerina, P., and Russell, R. (2014) DEAD-box helicase proteins disrupt RNA tertiary structure through helix capture. PLOS Biology 12(10):e1001981.

 Jarmoskaite, I., Bhaskaran, H., Seifert, S., and Russell, R. (2014) DEAD-box protein CYT-19 is activated by exposed helices in a group I intron RNA. Proc. Natl. Acad. Sci. U.S.A. 111, E2928-36.

Jarmoskaite, I, and Russell, R. (2014) RNA helicase proteins as chaperones and remodelers. Ann. Rev. Biochem. 83, 697-725.

Mitchell, D., and Russell, R. (2014) Folding pathways of the Tetrahymena ribozyme. J. Mol. Biol., 426, 2300-2312.

Mitchell, D., Jarmoskaite, I., Seval, N., Seifert, S., and Russell R. (2013) The long-range P3 helix of the Tetrahymena ribozyme is disrupted during folding between the native and misfolded conformations. J. Mol. Biol. 425, 2670-2686.

Cannon, B., Kuhnlein, J., Yang, S.H., Cheng, A., Stark, J.M., Russell, R., and Paull, T.T. (2013) Visualization of local DNA unwinding by MRN using single molecule FRET. Proc. Natl. Acad. Sci. U.S.A., 110, 18868-11873.

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.