The structural basis of protein targeting and translocation in bacteria.

In Gram-negative bacteria, two distinct targeting routes assist in the proper localization of secreted and membrane proteins and structural studies of the targeting and the translocating components provide insights into how substrates are recognized and suggest a mechanism by which proteins are transported through an aqueous pore in the cytoplasmic membrane.

Abstract

In Gram-negative bacteria, two distinct targeting routes assist in the proper localization of secreted and membrane proteins. Signal recognition particle (SRP) mainly targets ribosome-bound nascent membrane proteins, whereas SecB facilitates the targeting of periplasmic and outer membrane proteins. These routes converge at the translocase, a protein-conducting pore in the membrane that consists of the SecYEG complex associated with the peripheral ATPase, SecA. Recent structural studies of the targeting and the translocating components provide insights into how substrates are recognized and suggest a mechanism by which proteins are transported through an aqueous pore in the cytoplasmic membrane.