Increased production of periplasmic proteins in Escherichia coli by directed evolution of the translation initiation region.

ABSTRACT: BACKGROUND:Recombinant proteins are often engineered with an N-terminal signal peptide, which facilitates their secretion to the oxidising environment of the periplasm (gram-negative bacteria) or the culture supernatant (gram-positive bacteria). A commonly encountered problem is that the signal peptide influences the synthesis and secretion of the recombinant protein in an unpredictable manner. A molecular understanding of this phenomenon is highly sought after, as it could lead to improved methods for producing recombinant proteins in bacterial cell factories. RESULTS:Herein we demonstrate that signal peptides contribute to an unpredictable translation initiation region. A directed evolution approach that selects a new translation initiation region, whilst leaving the amino acid sequence

SUBMITTER: Mirzadeh K 

PROVIDER: S-EPMC7137448 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature