Greg L. Hersch

TL;DR: Exciting progress has been made in understanding how AAA(+) machines recognize specific proteins as targets and then carry out ATP-dependent dismantling of the tertiary and/or quaternary structure of these molecules during the processes of protein degradation and the disassembly of macromolecular complexes.

TL;DR: These studies further emphasize commonalities between distant AAA+ family members, including protein and DNA translocases, helicases, motor proteins, clamp loaders, and other ATP-dependent enzymes.

TL;DR: It is shown that ClpX-ClpP affinity varies with the protein-processing task of Clp X and with the catalytic engagement of the active sites of ClPP.

TL;DR: By increasing the spacing between the protease and adaptor-binding determinants in the ssrA tag, substrates were obtained that displayed improved SspB-mediated binding to and degradation by ClpXP, and suggest that clashes between SSPB and ClpX weaken simultaneous binding.

TL;DR: Using computational design, an SspB heterodimer whose subunits did not form homodimers is engineered and it is demonstrated that both XB modules are required for strong binding and efficient substrate delivery to ClpXP.