SAUER LAB General Lab Information About the Lab 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. HOME

 

	A Courtyard in Summer at M.I.T. (Gift of the Class of 1985)

Selected Sauer Lab Publications Bolon, D.N., Grant, R.A., Baker, T.A. & Sauer, R.T. (2005) Specificity versus stability in computational protein design. Proc. Natl. Acad. Sci. USA 102, 12724-12729. Martin, A., Baker, T.A. & Sauer, R.T. (2005) Rebuilt AAA+ motors reveal operating principles for ATP-fueled machines. Nature 437, 1115-1120. Hersch, G.L., Burton, R.E., Bolon, D.N., Baker, T.A. & Sauer, R.T. (2005) Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine. Cell 121, 1017-1027. Tabtiang, R.K., Cezairliyan, B.O., Grant, R.A, Cochrane, J.C. & Sauer, R.T. (2005) Consolidating critical binding determinants by non-cyclic rearrangement of protein secondary structure. Proc. Natl. Acad. Sci. USA 102, 2305-2309. Burton, R.E., Baker, T.A. & Sauer, R.T. (2005) Nucleotide-dependent substrate recognition by the AAA+ HslUV protease. Nat. Struct. & Mol. Biol. 12, 245-251. Joshi, S.A., Hersch, G.L., Baker, T.A. & Sauer, R.T. Communication between ClpX and ClpP during substrate processing and degradation. Nature Structural & Molecular Biology 11, 404-411 (2004). Bolon, D.N., Wah, D.A., Hersch, G.L., Baker, T.A. & Sauer, R.T. Bivalent tethering of SspB to ClpXP is required for efficient substrate delivery: a protein-design study. Molecular Cell 13, 443-449 (2004). Hayes, C.S. & Sauer, R.T. Cleavage of the A-site mRNA codon during ribosome pausing provides a mechanism for translational quality control. Molecular Cell 12, 903-911 (2003). Kenniston, J.A., Baker, T.A., Fernandez, J.M. & Sauer, R.T. Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine. Cell 114, 511-520 (2003). Walsh, N.P., Alba, B.M., Bose, B., Gross, C.A. & Sauer, R.T. OMP peptide signals initiate the envelope-stress response by activating DegS protease through relief of inhibitory interactions mediated by its PDZ domain. Cell 113, 61-71 (2003). Cordes, M.H.J., Burton, R.E., Walsh, N.P., McKnight, C.J. & Sauer, R.T. An Evolutionary Bridge to a New Protein Fold. Nature Structural Biology 7, 1129-1132 (2000).