Boosting Secretion of Extracellular Protein by Escherichia coli via Cell Wall Perturbation.

ABSTRACT: Escherichia coli is one of the most widely used host microorganisms for recombinant protein expression and metabolic engineering, but it cannot efficiently secrete recombinant proteins to extracellular space. Here, extracellular protein secretion was enhanced in E. coli by deleting two d,d-carboxypeptidase genes (dacA and dacB, single and double deletions) to perturb the cell wall peptidoglycan network. Deletion of dacA and dacB enhanced the accumulation of intracellular soluble peptidoglycan in E. coli and affected cell morphology, resulting in a more irregular cell shape and the appearance of transparent bulges. Deletion of dacA and dacB appears to disrupt the normal rigid structure, presumably due to perturbation and destruc

SUBMITTER: Yang H 

PROVIDER: S-EPMC6182897 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature