G-Equivalent Acceleration Tolerance in the Eutardigrade Species Hypsibius dujardini.

Tardigrades are microscopic organisms renowned for their ability to survive extreme environmental conditions. Tardigrade extreme-tolerance research has centered on the ability to withstand desiccation, low and high temperatures, and high hydrostatic pressure and radiation levels. Tardigrade tolerance to hypergravity, however, has yet to be described.

Structural determinants stabilizing the axial channel of ClpP for substrate translocation.

Acyldepsipeptides (ADEPs) antibiotics bind to Escherichia coli ClpP mimicking the interactions that the IGL/F loops in ClpA or ClpX ATPases establish with the hydrophobic pockets surrounding the axial pore of the tetradecamer that the protease forms. ADEP binding induces opening of the gates blocking the axial channel of ClpP and allowing protein substrates to be translocated and hydrolysed in the degradation chamber. To identify the structural determinants stabilizing the open conformation of the axial channel for efficient substrate translocation, we constructed ClpP variants with amino acid substitutions in the N-terminal region that forms the axial gates.