Docking interactions determine substrate specificity of members of a widespread family of protein phosphatases.

ABSTRACT: How protein phosphatases achieve specificity for their substrates is a major outstanding question. PPM family serine/threonine phosphatases are widespread in bacteria and eukaryotes, where they dephosphorylate target proteins with a high degree of specificity. In bacteria, PPM phosphatases control diverse transcriptional responses by dephosphorylating anti-anti-sigma factors of the STAS domain family, exemplified by Bacillus subtilis phosphatases SpoIIE, which controls cell-fate during endospore formation, and RsbU, which initiates the general stress response. Using a combination of forward genetics, biochemical reconstitution, and AlphaFold2 structure prediction, we identified a conserved, tripartite substrate docking interface comprised of three variable loops on the surface of the PPM p

SUBMITTER: Caban-Penix S 

PROVIDER: S-EPMC11418112 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature