Conserved mechanism of cell-wall synthase regulation revealed by the identification of a new PBP activator in <i>Pseudomonas aeruginosa</i>.

ABSTRACT: Penicillin-binding proteins (PBPs) are synthases required to build the essential peptidoglycan (PG) cell wall surrounding most bacterial cells. The mechanisms regulating the activity of these enzymes to control PG synthesis remain surprisingly poorly defined given their status as key antibiotic targets. Several years ago, the outer-membrane lipoprotein ^EcLpoB was identified as a critical activator of Escherichia coli PBP1b (^EcPBP1b), one of the major PG synthases of this organism. Activation of ^EcPBP1b is mediated through the association of ^EcLpoB with a regulatory domain on ^EcPBP1b called UB2H. Notably, Pseudomonas aeruginosa also encodes PBP1b (^PaPBP1b), which possesses a UB2H domain, but this bacterium lacks

SUBMITTER: Greene NG 

PROVIDER: S-EPMC5866570 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature