Functional identification of a Streptomyces lividans FKBP-like protein involved in the folding of overproduced secreted proteins.

ABSTRACT: Some bacterial peptidyl-prolyl cis/trans isomerases (PPIases) are involved in secretory protein folding after the translocation step. Streptomyces lividans has been used as a host for engineering extracellular overproduction of homologous and heterologous proteins in industrial applications. Although the mechanisms governing the major secretory pathway (Sec route) and the minor secretory pathway (Tat route) are reasonably well described, the function of proteins responsible for the extracellular secretory protein folding is not characterized as yet. We have characterized a Tat-dependent S. lividans FK506-binding protein-like lipoprotein (FKBP) that has PPIase activity. A mutant in the sli-fkbp gene induces a secretion stress response and affects secretion and ac

SUBMITTER: Vicente RL 

PROVIDER: S-EPMC6833217 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature