Robert T. Sauer

Robert T. Sauer

Salvador E. Luria Professor of Biology 

Bob Sauer studies intracellular proteolytic machines responsible for protein-quality control and homeostasis.





Sarah Wylie



Assistant Phone


  • PhD, 1979, Harvard University
  • BA, 1972, Biophysics, Amherst College

Research Summary

We study the relationship between protein structure, function, sequence and folding. We focus on the molecular machines that degrade or remodel proteins, targeting proteins for these ATP-dependent reactions. Our experimental tools include biochemistry and single-molecule biophysics, structural biology, protein design and engineering, and molecular genetics.


  • Protein Society, Stein and Moore Award, 2013
  • Protein Society, Hans Neurath Award, 2007
  • Protein Society, Amgen Award, 2001
  • National Academy of Sciences, Member, 1996
  • American Academy of Arts and Sciences, Fellow, 1993

Key Publications

  1. Dissection of Axial-Pore Loop Function during Unfolding and Translocation by a AAA+ Proteolytic Machine. Iosefson, O, Olivares, AO, Baker, TA, Sauer, RT. 2015. Cell Rep 12, 1032-41.
    doi: 10.1016/j.celrep.2015.07.007PMID:26235618
  2. Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. Stinson, BM, Baytshtok, V, Schmitz, KR, Baker, TA, Sauer, RT. 2015. Nat Struct Mol Biol 22, 411-6.
    doi: 10.1038/nsmb.3012PMID:25866879
  3. Coordinated gripping of substrate by subunits of a AAA+ proteolytic machine. Iosefson, O, Nager, AR, Baker, TA, Sauer, RT. 2015. Nat Chem Biol 11, 201-6.
    doi: 10.1038/nchembio.1732PMID:25599533
  4. Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery. Schmitz, KR, Carney, DW, Sello, JK, Sauer, RT. 2014. Proc Natl Acad Sci U S A 111, E4587-95.
    doi: 10.1073/pnas.1417120111PMID:25267638
  5. Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine. Stinson, BM, Nager, AR, Glynn, SE, Schmitz, KR, Baker, TA, Sauer, RT. 2013. Cell 153, 628-39.
    doi: 10.1016/j.cell.2013.03.029PMID:23622246

Recent Publications

  1. Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug. Baytshtok, V, Fei, X, Shih, TT, Grant, RA, Santos, JC, Baker, TA, Sauer, RT. 2021. Cell Rep 34, 108639.
    doi: 10.1016/j.celrep.2020.108639PMID:33472065
  2. Multistep substrate binding and engagement by the AAA+ ClpXP protease. Saunders, RA, Stinson, BM, Baker, TA, Sauer, RT. 2020. Proc Natl Acad Sci U S A 117, 28005-28013.
    doi: 10.1073/pnas.2010804117PMID:33106413
  3. Structural basis of ClpXP recognition and unfolding of ssrA-tagged substrates. Fei, X, Bell, TA, Barkow, SR, Baker, TA, Sauer, RT. 2020. Elife 9, .
    doi: 10.7554/eLife.61496PMID:33089779
  4. Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate. Fei, X, Bell, TA, Jenni, S, Stinson, BM, Baker, TA, Harrison, SC, Sauer, RT. 2020. Elife 9, .
    doi: 10.7554/eLife.52774PMID:32108573
  5. Interactions between a subset of substrate side chains and AAA+ motor pore loops determine grip during protein unfolding. Bell, TA, Baker, TA, Sauer, RT. 2019. Elife 8, .
    doi: 10.7554/eLife.46808PMID:31251172
  6. Roles of the ClpX IGF loops in ClpP association, dissociation, and protein degradation. Amor, AJ, Schmitz, KR, Baker, TA, Sauer, RT. 2019. Protein Sci 28, 756-765.
    doi: 10.1002/pro.3590PMID:30767302
  7. Structural and Functional Analysis of E. coli Cyclopropane Fatty Acid Synthase. Hari, SB, Grant, RA, Sauer, RT. 2018. Structure 26, 1251-1258.e3.
    doi: 10.1016/j.str.2018.06.008PMID:30057024
  8. Mechanical Protein Unfolding and Degradation. Olivares, AO, Baker, TA, Sauer, RT. 2018. Annu Rev Physiol 80, 413-429.
    doi: 10.1146/annurev-physiol-021317-121303PMID:29433415
  9. Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation. Baytshtok, V, Chen, J, Glynn, SE, Nager, AR, Grant, RA, Baker, TA, Sauer, RT. 2017. J Biol Chem 292, 5695-5704.
    doi: 10.1074/jbc.M116.768978PMID:28223361
  10. The AAA+ FtsH Protease Degrades an ssrA-Tagged Model Protein in the Inner Membrane of Escherichia coli. Hari, SB, Sauer, RT. 2016. Biochemistry 55, 5649-5652.
    doi: 10.1021/acs.biochem.6b00920PMID:27677373
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