generallabinfo

 

BobstockPhoto

(left to right) Santiago Lima, Jungsan Sohn and wife, Sarah Barkow and friend,
Brent Cezairliyan and Eyal Gur at the
Bobstock Dinner Celebration (July 2008), Le Meridien, Cambridge, MA

 

SAUER LAB

BIOLOGY DEPARTMENT

General Information

The lab uses biophysical, genetic, structural, and design strategies to study the relationship between the sequence, stability, and three-dimensional structures of proteins.

We are also interested in the mechanisms that intracellular proteases use to select the correct targets and how ATP-dependent proteases catalyze protein denaturation.

 

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Select Recent Publications

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.

Nager, A.R., Baker, T.A. & Sauer, R.T. (2011) Stepwise unfolding of a beta-barrel protein by the AAA+ ClpXP protease. J. Mol. Biol. 413, 4-16.

Davis, J.H., Baker, T.A. & Sauer, R.T. (2011) Small-molecule control of protein degradation using split adaptors. ACS Chem. Biol. 6, 1205–1213.

Aubin-Tam, M.E., Olivares, A.O., Sauer, R.T., Baker, T.A. & Lang, M.J. (2011) Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine. Cell 145, 257-267.

Kim, S., Grant, R.A. & Sauer, R.T. (2011) Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages. Cell 145, 67-78.

Sundar, S., McGinness, K.E., Baker, T.A. & Sauer, R.T. (2010) Multiple sequence signals direct recognition and degradation of protein substrates by the AAA+ protease HslUV. J. Mol. Biol. 403, 420-429.

 

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

To locate us, please use the following url: http://whereis.mit.edu/map-jpg

Contact: Webmaster as follows:
sauer-www [at] mit.edu
(Email format [at] = @)

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