Tania A. Baker

Tania A. Baker

E. C. Whitehead Professor of Biology; Investigator, Howard Hughes Medical Institute

Tania Baker’s current research explores mechanisms and regulation of enzyme-catalyzed protein unfolding, ATP-dependent protein degradation, and remodeling of the proteome during cellular stress responses.

617-253-3594

Phone

68-523

Office

tabaker@mit.edu

Email

Building 68 - Koch Biology Building

Location

Lab Website
Tori Yetman

Assistant

617-324-7833

Assistant Phone

Education

  • PhD, 1988, Stanford University
  • BS, 1983, Biochemistry, University of Wisconsin-Madison

Research Summary

Our goal is to understand the mechanisms and regulation behind AAA+ unfoldases and macromolecular machines from the "Clp/Hsp100 family" of protein unfolding enzymes. We study these biological catalysts using biochemistry, structural biology, molecular biology, genetics, and single molecule biophysics. No longer accepting students.

Awards

  • Margaret MacVicar Faculty Fellow, 2008-2018
  • National Academy of Sciences, Member, 2007
  • American Academy of Arts and Sciences, Fellow, 2005
  • Howard Hughes Medical Institute, HHMI Investigator, 1994

Key Publications

  1. Structural Basis of an N-Degron Adaptor with More Stringent Specificity. Stein, BJ, Grant, RA, Sauer, RT, Baker, TA. 2016. Structure 24, 232-42.
    doi: 10.1016/j.str.2015.12.008PMID:26805523
  2. Mitochondrial ClpX Activates a Key Enzyme for Heme Biosynthesis and Erythropoiesis. Kardon, JR, Yien, YY, Huston, NC, Branco, DS, Hildick-Smith, GJ, Rhee, KY, Paw, BH, Baker, TA. 2015. Cell 161, 858-67.
    doi: 10.1016/j.cell.2015.04.017PMID:25957689
  3. Mechanochemical basis of protein degradation by a double-ring AAA+ machine. Olivares, AO, Nager, AR, Iosefson, O, Sauer, RT, Baker, TA. 2014. Nat Struct Mol Biol 21, 871-5.
    doi: 10.1038/nsmb.2885PMID:25195048
  4. Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine. Aubin-Tam, ME, Olivares, AO, Sauer, RT, Baker, TA, Lang, MJ. 2011. Cell 145, 257-67.
    doi: 10.1016/j.cell.2011.03.036PMID:21496645
  5. The molecular basis of N-end rule recognition. Wang, KH, Roman-Hernandez, G, Grant, RA, Sauer, RT, Baker, TA. 2008. Mol Cell 32, 406-14.
    doi: 10.1016/j.molcel.2008.08.032PMID:18995838
  6. Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Flynn, JM, Neher, SB, Kim, YI, Sauer, RT, Baker, TA. 2003. Mol Cell 11, 671-83.
    doi: 10.1016/s1097-2765(03)00060-1PMID:12667450
  7. A specificity-enhancing factor for the ClpXP degradation machine. Levchenko, I, Seidel, M, Sauer, RT, Baker, TA. 2000. Science 289, 2354-6.
    doi: 10.1126/science.289.5488.2354PMID:11009422

Recent Publications

  1. An asymmetric nautilus-like HflK/C assembly controls FtsH proteolysis of membrane proteins. Ghanbarpour, A, Telusma, B, Powell, BM, Zhang, JJ, Bolstad, I, Vargas, C, Keller, S, Baker, TA, Sauer, RT, Davis, JH et al.. 2025. EMBO J , .
    doi: 10.1038/s44318-025-00408-1PMID:40082723
  2. How the double-ring ClpAP protease motor grips the substrate to unfold and degrade stable proteins. Shih, TT, Sauer, RT, Baker, TA. 2024. J Biol Chem 300, 107861.
    doi: 10.1016/j.jbc.2024.107861PMID:39374782
  3. The membrane-cytoplasmic linker defines activity of FtsH proteases in Pseudomonas aeruginosa clone C. Mawla, GD, Kamal, SM, Cao, LY, Purhonen, P, Hebert, H, Sauer, RT, Baker, TA, Römling, U. 2024. J Biol Chem 300, 105622.
    doi: 10.1016/j.jbc.2023.105622PMID:38176647
  4. 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
  5. Lon degrades stable substrates slowly but with enhanced processivity, redefining the attributes of a successful AAA+ protease. Kasal, MR, Kotamarthi, HC, Johnson, MM, Stephens, HM, Lang, MJ, Sauer, RT, Baker, TA. 2023. Cell Rep 42, 113061.
    doi: 10.1016/j.celrep.2023.113061PMID:37660294
  6. 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
  7. 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
  8. 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
  9. AAA+ protease-adaptor structures reveal altered conformations and ring specialization. Kim, S, Fei, X, Sauer, RT, Baker, TA. 2022. Nat Struct Mol Biol 29, 1068-1079.
    doi: 10.1038/s41594-022-00850-3PMID:36329286
  10. Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysis. Sauer, RT, Fei, X, Bell, TA, Baker, TA. 2022. Crit Rev Biochem Mol Biol 57, 188-204.
    doi: 10.1080/10409238.2021.1979461PMID:34923891
More Publications

Multimedia