Automation-aided construction and characterization of Bacillus subtilis PrsA strains for the secretion of amylases.

ABSTRACT: Proteins face an obstacle race on their way to successful folding. Chaperones facilitate the proper folding of proteins by ensuring they remain on the correct path toward their final tertiary structure. In bacilli, the PrsA chaperone is essential for the correct folding and stabilization of proteins within the cell wall. Overexpression of the PrsA chaperone has been shown to improve the successful folding and secretion of many biotechnologically relevant secreted enzymes. This resulted in a double benefit: firstly, it promotes the efficient release of properly folded enzymes from the cell wall, and second, it reduces the folding stress for the cell, thereby enhancing the overall fitness of the production organism. This paper presents a workflow in which different wild-type PrsA molecules i

SUBMITTER: Hamburger F 

PROVIDER: S-EPMC11798935 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature