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.

617-253-3163

Phone

68-571A

Office

Brenda Ellen Pepe

Assistant

617-253-6077

Assistant Phone

Education

PhD 1979, Harvard University

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.

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

  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. 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
  2. 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
  3. 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
  4. A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis. Baytshtok, V, Fei, X, Grant, RA, Baker, TA, Sauer, RT. 2016. Structure 24, 1766-1777.
    doi: 10.1016/j.str.2016.08.012PMID:27667691
  5. Highly Dynamic Interactions Maintain Kinetic Stability of the ClpXP Protease During the ATP-Fueled Mechanical Cycle. Amor, AJ, Schmitz, KR, Sello, JK, Baker, TA, Sauer, RT. 2016. ACS Chem. Biol. 11, 1552-1560.
    doi: 10.1021/acschembio.6b00083PMID:27003103
  6. Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines. Olivares, AO, Baker, TA, Sauer, RT. 2016. Nat. Rev. Microbiol. 14, 33-44.
    doi: 10.1038/nrmicro.2015.4PMID:26639779
  7. Origin and Functional Evolution of the Cdc48/p97/VCP AAA+ Protein Unfolding and Remodeling Machine. Barthelme, D, Sauer, RT. 2016. J. Mol. Biol. 428, 1861-9.
    doi: 10.1016/j.jmb.2015.11.015PMID:26608813
  8. 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
  9. An ALS disease mutation in Cdc48/p97 impairs 20S proteasome binding and proteolytic communication. Barthelme, D, Jauregui, R, Sauer, RT. 2015. Protein Sci. 24, 1521-7.
    doi: 10.1002/pro.2740PMID:26134898
  10. Assaying the kinetics of protein denaturation catalyzed by AAA+ unfolding machines and proteases. Baytshtok, V, Baker, TA, Sauer, RT. 2015. Proc. Natl. Acad. Sci. U.S.A. 112, 5377-82.
    doi: 10.1073/pnas.1505881112PMID:25870262
More Publications