Polytopic membrane protein folding at L17 in the ribosome tunnel initiates cyclical changes at the translocon.

ABSTRACT: Multi-spanning membrane protein loops are directed alternately into the cytosol or ER lumen during cotranslational integration. Nascent chain exposure is switched after a newly synthesized transmembrane segment (TMS) enters the ribosomal tunnel. FRET measurements revealed that each TMS is initially extended, but folds into a compact conformation after moving 6-7 residues from the peptidyltransferase center, irrespective of loop size. The ribosome-induced folding of each TMS coincided with its photocrosslinking to ribosomal protein L17 and an inversion of compartmental exposure. This correlation indicates that successive TMSs fold and bind at a specific ribosomal tunnel site that includes L17, thereby triggering structural rearrangements of multiple components in and on both sides of the ER

SUBMITTER: Lin PJ 

PROVIDER: S-EPMC3187706 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature