<i>In vivo</i> and <i>in vitro</i> analyses of the role of the Prc protease in inducing mucoidy in <i>Pseudomonas aeruginosa</i>.

ABSTRACT: In Pseudomonas aeruginosa, alginate biosynthesis gene expression is inhibited by the transmembrane anti-sigma factor MucA, which sequesters the AlgU sigma factor. Cell envelope stress initiates cleavage of the MucA periplasmic domain by site-1 protease AlgW, followed by further MucA degradation to release AlgU. However, after colonizing the lungs of people with cystic fibrosis, P. aeruginosa converts to a mucoid form that produces alginate constitutively. Mucoid isolates often have mucA mutations, with the most common being mucA22, which truncates the periplasmic domain. MucA22 is degraded constitutively, and genetic studies suggested that the Prc protease is responsible. Some studies also suggested that Prc contributes to induction in strains with wild-type Muc

SUBMITTER: Sommerfield AG 

PROVIDER: S-EPMC11500579 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature