A conserved allosteric element controls specificity and activity of functionally divergent PP2C phosphatases from Bacillus subtilis.

ABSTRACT: Reversible phosphorylation relies on highly regulated kinases and phosphatases that target specific substrates to control diverse cellular processes. Here, we address how protein phosphatase activity is directed to the correct substrates under the correct conditions. The serine/threonine phosphatase SpoIIE from Bacillus subtilis, a member of the widespread protein phosphatase 2C (PP2C) family of phosphatases, is activated by movement of a conserved α-helical element in the phosphatase domain to create the binding site for the metal cofactor. We hypothesized that this conformational switch could provide a general mechanism for control of diverse members of the PP2C family of phosphatases. The B. subtilis phosphatase RsbU responds to different signals, acts on a different substrates, and pro

SUBMITTER: Ho K 

PROVIDER: S-EPMC8080068 | biostudies-literature | 2021 Jan-Jun

REPOSITORIES: biostudies-literature