Direct visualization of the E. coli Sec translocase engaging precursor proteins in lipid bilayers.

ABSTRACT: Escherichia coli exports proteins via a translocase comprising SecA and the translocon, SecYEG. Structural changes of active translocases underlie general secretory system function, yet directly visualizing dynamics has been challenging. We imaged active translocases in lipid bilayers as a function of precursor protein species, nucleotide species, and stage of translocation using atomic force microscopy (AFM). Starting from nearly identical initial states, SecA more readily dissociated from SecYEG when engaged with the precursor of outer membrane protein A as compared to the precursor of galactose-binding protein. For the SecA that remained bound to the translocon, the quaternary structure varied with nucleotide, populating SecA₂ primarily with adenosine diphosphate (ADP)

SUBMITTER: Sanganna Gari RR 

PROVIDER: S-EPMC6561738 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature