MifM-instructed translation arrest involves nascent chain interactions with the exterior as well as the interior of the ribosome.

ABSTRACT: Bacillus subtilis MifM is a monitoring substrate of the YidC pathways of protein integration into the membrane and controls the expression of the YidC2 (YqjG) homolog by undergoing regulated translational elongation arrest. The elongation arrest requires interactions between the MifM nascent polypeptide and the ribosomal components near the peptidyl transferase center (PTC) as well as at the constriction site of the ribosomal exit tunnel. Here, we addressed the roles played by more N-terminal regions of MifM and found that, in addition to the previously-identified arrest-provoking elements, the MifM residues 41-60 likely located at the tunnel exit and outside the ribosome contribute to the full induction of elongation arrest. Mutational effects of the cytosolically exposed part of the ribo

SUBMITTER: Fujiwara K 

PROVIDER: S-EPMC6037786 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature