Robert T. Sauer

Robert T. Sauer

Professor Emeritus

Before closing his lab, Bob Sauer studied intracellular proteolytic machines responsible for protein-quality control and homeostasis.

617-253-3163

Phone

68-623A

Office

bobsauer@mit.edu

Email

Lab Website

Education

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

Research Summary

Before closing his lab, Bob Sauer studied the relationship between protein structure, function, sequence and folding. He focused on the molecular machines that degrade or remodel proteins, targeting proteins for these ATP-dependent reactions. His experimental tools included biochemistry and single-molecule biophysics, structural biology, protein design and engineering, and molecular genetics.

Awards

  • 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

Recent Publications

  1. A closed translocation channel in the substrate-free AAA+ ClpXP protease diminishes rogue degradation. Ghanbarpour, A, Cohen, SE, Fei, X, Kinman, LF, Bell, TA, Zhang, JJ, Baker, TA, Davis, JH, Sauer, RT. 2023. Nat Commun 14, 7281.
    doi: 10.1038/s41467-023-43145-xPMID:37949857
  2. The SspB adaptor drives structural changes in the AAA+ ClpXP protease during ssrA-tagged substrate delivery. Ghanbarpour, A, Fei, X, Baker, TA, Davis, JH, Sauer, RT. 2023. Proc Natl Acad Sci U S A 120, e2219044120.
    doi: 10.1073/pnas.2219044120PMID:36730206
  3. FtsH degrades dihydrofolate reductase by recognizing a partially folded species. Morehouse, JP, Baker, TA, Sauer, RT. 2022. Protein Sci 31, e4410.
    doi: 10.1002/pro.4410PMID:36630366
  4. FtsH degrades kinetically stable dimers of cyclopropane fatty acid synthase via an internal degron. Hari, SB, Morehouse, JP, Baker, TA, Sauer, RT. 2023. Mol Microbiol 119, 101-111.
    doi: 10.1111/mmi.15009PMID:36456794
  5. 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
  6. 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
  7. 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
  8. 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
  9. 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
  10. 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
More Publications