Hans-Georg Koch

TL;DR: Using site-specific crosslinking, the results reveal a hierarchy in targeting of a Tat substrate such that for the primary interaction, TatC is both necessary and sufficient while a subsequent association with TatB likely mediates transfer from TatC to the actual Tat pore.

TL;DR: Depending upon the type of protein cargo that needs to be transported, the Signal Recognition Particle (SRP), the SRP receptor, SecA and chaperones are required to coordinate translation with transport and to target and energise the different transport systems.

TL;DR: The results, while confirming previous in vivo studies, provide the first in vitro evidence for the dependence of the integration of polytopic inner membrane proteins on SRP in E. coli and suggest that SRP and SecA/SecB have different substrate specificities resulting in two separate targeting mechanisms for membrane and secretory proteins inE.

TL;DR: This review summarizes recent biochemical and structural information on the prokaryotic and eukaryotic Sec translocons and describes the remarkably complex interaction network of the Sec complexes.

TL;DR: SRP-dependent protein targeting in bacteria and chloroplasts slightly deviate from the canonical mechanism found in eukaryotes, but the preferential substrates of SRP possess especially hydrophobic signal sequences.