Author

T. A. Baker

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 5 Biophysics· 4 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 10 Research Focus:protein folding & dynamics· 6 Assay:cryo-EM· 5 Organism:E. coli· 5 Organism:bacteria (other)· 2 Research Focus:protein structure prediction· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1

Frequent Co-Authors

R. T. Sauer· 8 shared X. Fei· 5 shared T. A. Bell· 4 shared S. Kim· 3 shared B. M. Stinson· 2 shared J. H. Davis· 2 shared A. Fazal· 1 shared A. Garbhanpour· 1 shared

Activity by Year

2018-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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8 shared papersBiochemistry

R. T. Sauer

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Author profile →

10 papers

Recent·Most cited

The membrane-cytoplasmic linker defines activity of FtsH proteases in Pseudomonas aeruginosa clone C

G. D. Mawla, S. M. Kamal, L. Cao, P. Purhonen, H. Hebert, R. T. Sauer, T. A. Baker, U. Romling

This study shows that the MC linker in PaFtsH2 affects its substrate processing efficiency, and modifying it can enhance its function in Pseudomonas aeruginosa.

bioRxiv · Jun 19, 2023 · PreprintBiochemistry

The SspB adaptor drives structural changes in the AAA+ ClpXP protease during ssrA-tagged substrate delivery

A. Garbhanpour, X. Fei, T. A. Baker, J. H. Davis, R. T. Sauer

This paper presents a cryo-EM structure of the SspB adaptor bound to ClpXP and a tagged substrate, revealing structural changes in ClpX and its interaction with ClpP during substrate delivery.

bioRxiv · Nov 6, 2022Biochemistry

A closed translocation channel in the substrate-free AAA+ ClpXP protease diminishes rogue degradation

A. Ghanbarpour, S. E. Cohen, X. Fei, T. A. Bell, T. A. Baker, J. H. Davis, R. T. Sauer

The paper presents cryo-EM structures of E. coli ClpXP, showing that a closed axial channel in ClpX enhances degradation specificity by preventing non-specific substrate entry.

bioRxiv · Aug 27, 2022Biochemistry

AAA+ protease-adaptor structures reveal altered conformations and ring specialization

S. Kim, X. Fei, R. T. Sauer, T. A. Baker

The paper presents cryo-EM structures of ClpAPS complexes, revealing how pore loops interact with the ClpS NTE and showing asymmetry in engagement by the D1 and D2 rings.

bioRxiv · Feb 4, 2022Biophysics

ClpAP proteolysis does not require rotation of the ClpA unfoldase relative to ClpP

S. Kim, K. L. Zuromski, T. A. Bell, R. T. Sauer, T. A. Baker

This study shows that ClpA does not need to rotate relative to ClpP for proteolysis, though some flexibility may aid function.

eLife · Dec 1, 2020Peer-reviewedBiochemistry

Structural basis of ClpXP recognition and unfolding of ssrA-tagged substrates

X. Fei, T. A. Bell, S. R. Barkow, T. A. Baker, R. T. Sauer

The paper presents cryo-EM structures of ClpXP bound to the ssrA degron, revealing how it recognizes and unfolds ssrA-tagged substrates through a multistep process.

eLife · Oct 22, 2020Peer-reviewedBiophysics

Multistep substrate binding and engagement by the AAA+ ClpXP protease

R. A. Saunders, B. M. Stinson, T. A. Baker, R. T. Sauer

This study investigates the multistep binding and engagement of ssrA-tagged substrates by E. coli ClpXP using fluorescence-quenching assays and kinetic analysis, revealing a model of substrate recognition and unfolding.

bioRxiv · May 4, 2020Biophysics

Regulation of antimycin biosynthesis is controlled by the ClpXP protease

B. Bilyk, S. Kim, A. Fazal, T. A. Baker, R. F. Seipke

This paper shows that the ClpXP protease regulates the abundance of σAntA, an ECF σ factor controlling antimycin biosynthesis in Streptomyces.

mSphere · Apr 29, 2020Peer-reviewedMicrobiology

Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate

X. Fei, T. A. Bell, S. Jenni, B. M. Stinson, T. A. Baker, S. C. Harrison, R. T. Sauer

This study presents cryo-EM structures of the E. coli ClpXP protease complex, revealing how ClpX interacts with ClpP and substrates, and proposes models for its ATP-dependent proteolytic mechanism.

bioRxiv · Oct 31, 2019Biophysics

Mitochondrial ClpX activates an essential metabolic enzyme through partial unfolding

J. R. Kardon, J. A. Moroco, J. R. Engen, T. A. Baker

The paper investigates how mitochondrial ClpX partially unfolds ALAS to activate it by gating cofactor access.

bioRxiv · May 21, 2018Biochemistry