Identification and characterization of a translation arrest motif in VemP by systematic mutational analysis.

ABSTRACT: VemP ( Vibrio protein export monitoring polypeptide) is a secretory protein comprising 159 amino acid residues, which functions as a secretion monitor in Vibrio and regulates expression of the downstream V.secDF2 genes. When VemP export is compromised, its translation specifically undergoes elongation arrest at the position where the Gln¹⁵⁶ codon of vemP encounters the P-site in the translating ribosome, resulting in up-regulation of V.SecDF2 production. Although our previous study suggests that many residues in a highly conserved C-terminal 20-residue region of VemP contribute to its elongation arrest, the exact role of each residue remains unclear. Here, we constructed a reporter system to easily and exactly monito

SUBMITTER: Mori H 

PROVIDER: S-EPMC5827439 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature