Author

R. T. Sauer

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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Biophysics· 5 Biochemistry· 4 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 11 Research Focus:protein folding & dynamics· 7 Assay:cryo-EM· 5 Organism:E. coli· 5 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Research Focus:protein structure prediction· 2 Organism:bacteria (other)· 1

Frequent Co-Authors

T. A. Baker· 8 shared X. Fei· 5 shared T. A. Bell· 4 shared B. M. Stinson· 2 shared E. Yeh· 2 shared J. H. Davis· 2 shared K. Amberg-Johnson· 2 shared S. B. Hari· 2 shared

Activity by Year

2017-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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8 shared papersBiochemistry

T. A. Baker

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11 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

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

The non-dominant AAA+ ring in the ClpAP protease functions as an anti-stalling motor to accelerate protein unfolding and translocation

H. C. Kotamarthi, R. T. Sauer, T. Baker

This study investigates the role of the non-dominant D1 AAA+ ring in ClpAP protease by analyzing a variant with an inactive D1 ring, revealing its function in preventing stalling during protein unfolding and translocation.

bioRxiv · Mar 21, 2019Biophysics

A mutagenesis screen for essential plastid biogenesis genes in human malaria parasites

Y. Tang, T. R. Meister, M. Walczak, M. Pulkoski-Gross, S. B. Hari, R. T. Sauer, K. Amberg-Johnson, E. Yeh

The paper identifies essential genes for apicoplast biogenesis in P. falciparum through a mutagenesis screen, revealing new proteins and functions with potential drug targets.

bioRxiv · Aug 27, 2018Cell Biology

Small molecule inhibition of apicomplexan FtsH1 disrupts plastid biogenesis in human pathogens

K. Amberg-Johnson, S. B. Hari, S. M. Ganesan, H. A. Lorenzi, R. T. Sauer, J. C. Niles, E. Yeh

The paper identifies FtsH1 as a novel druggable target for antimalarial drugs by showing that its inhibition disrupts apicoplast biogenesis in Plasmodium falciparum and Toxoplasma gondii.

bioRxiv · Aug 19, 2017Microbiology