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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

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.

Schmitz, K.R. & Sauer, R.T. (2014) Substrate delivery by the AAA+ ClpX and ClpC1 unfoldases activates the mycobacterial ClpP1P2 peptidase. Mol. Micro. 93, 617-628

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.

Mauldin, R.V. & Sauer, R.T. (2013) Allosteric regulation of DegS protease subunits though a shared energy landscape. Nat. Chem. Biol. 9, 90-96.

Barthelme, D. & Sauer, R.T. (2012) Identification of the Cdc48•20S proteasome as an ancient AAA+ proteolytic machine. Science 337, 843-846.

Glynn, S.E., Nager, A.R., Baker, T.A. & Sauer, R.T. (2012) Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine. Nat. Struct. Mol. Biol. 19, 616-622.


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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