R. T. Sauer

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

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.

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.

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.

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

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.

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.

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.

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.

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

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.