Manuela K. Hospenthal

This study characterizes the nuclease activity of full-length ComEC during DNA processing, showing how ComEA modulates this activity to ensure fidelity in natural transformation.

The paper determines crystal structures of COMMD family HN domains, revealing a conserved domain swapping mechanism regulated by hinge-loop conformational changes and phosphorylation.

The paper investigates the molecular mechanisms of DNA translocation during natural transformation by analyzing the nuclease and DNA binding activities of ComEC domains.

The paper presents the cryo-EM structure of the type 1 chaperone-usher pilus rod at 4.2 Å resolution, revealing its spring-like biomechanical properties.