Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome.

ABSTRACT: Bacteria execute a variety of protein transport systems for maintaining the proper composition of their different cellular compartments. The SecYEG translocon serves as primary transport channel and is engaged in transporting two different substrate types. Inner membrane proteins are cotranslationally inserted into the membrane after their targeting by the signal recognition particle (SRP). In contrast, secretory proteins are posttranslationally translocated by the ATPase SecA. Recent data indicate that SecA can also bind to ribosomes close to the tunnel exit. We have mapped the interaction of SecA with translating and nontranslating ribosomes and demonstrate that the N terminus and the helical linker domain of SecA bind to an acidic patch on the surface of the ribosomal protein uL23. Intr

SUBMITTER: Knupffer L 

PROVIDER: S-EPMC6692507 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature