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General Information

The Sauer Lab uses biophysical, biochemical, structural, and design strategies to study the mechanisms that intracellular proteases use to select the correct targets and how ATP-dependent proteases catalyze protein denaturation and degradation.


Select Recent Publications

Iosefson, O., Olivares, A.O., Baker, T.A. & Sauer, R.T. (2015) Dissection of axial-pore loop function during unfolding and translocation by a AAA+ proteolytic machine. Cell Reports 12, 1032-1041.

Stinson, B.M., Baytshtok, V., Schmitz, K.R., Baker, T.A. & Sauer, R.T. (2015) Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. Nat. Struct. Mol. Biol. 22, 411–416.

Baytshtok, V., Baker, T.A. & Sauer, R.T. (2015) Assaying the kinetics of protein denaturation catalyzed by AAA+ unfolding machines and proteases. Proc. Natl. Acad. Sci. USA 112, 5377–5382.

Schmitz, K.R., Carney, D.W., Sello, J.K. & Sauer, R.T. (2014) The crystal structure of M. tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery. Proc. Natl. Acad. Sci. USA 111, E4587-4595.

Cordova, J.C, Olivares, A.O., Shin, Y., Stinson, B.M., Calmat, S., Schmitz, K.R., Aubin-Tam, M-E. Baker, T.A., Lang, M.J., & Sauer R.T. (2014) Stochastic but highly coordinated protein unfolding and translocation by the ClpXP proteolytic machine. Cell 158, 647-658.

Kim, S. & Sauer, R.T. (2014) Distinct regulatory mechanisms balance DegP proteolysis to maintain cellular fitness during heat stress. Genes Dev. 28, 902-911.

Lima, S., Guo, M.S., Chaba. R., Gross, C.A. & Sauer, R.T. (2013) Dual molecular signals mediate the bacterial response to outer-membrane stress. Science 340, 837-841.

Stinson, B.M., Nager, A.R., Glynn, S.E., Schmitz, K.R., Baker, T.A, and Sauer, R.T. (2013) Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine. Cell 153, 628-639.

The Links





Sauer Lab, Massachusetts Insitute of Technology
77 Massachusetts Avenue, 68-571
Cambridge, MA 02139
Telephone: 617.253.6077, Fax: 617.258.0673

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