YidC from <i>Escherichia coli</i> Forms an Ion-Conducting Pore upon Activation by Ribosomes.

ABSTRACT: The universally conserved protein YidC aids in the insertion and folding of transmembrane polypeptides. Supposedly, a charged arginine faces its hydrophobic lipid core, facilitating polypeptide sliding along YidC's surface. How the membrane barrier to other molecules may be maintained is unclear. Here, we show that the purified and reconstituted E. coli YidC forms an ion-conducting transmembrane pore upon ribosome or ribosome-nascent chain complex (RNC) binding. In contrast to monomeric YidC structures, an AlphaFold parallel YidC dimer model harbors a pore. Experimental evidence for a dimeric assembly comes from our BN-PAGE analysis of native vesicles, fluorescence correlation spectroscopy studies, single-molecule fluorescence photobleaching observations, and crosslinking experiment

SUBMITTER: Knyazev DG 

PROVIDER: S-EPMC10741985 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature