Yersinia Protein Kinase YopO Is Activated by A Novel G-actin Binding Process

Regulation of Yersinia Protein Kinase A (YpkA) Kinase Activity by Multisite Autophosphorylation and Identification of an N-terminal Substrate-binding Domain in YpkA

“…The efficiency of substrate-binding and -phosphorylation by YpkA is diminished by deletion of residues 40 -49 of YpkA, suggesting that they are important for substrate recognition. Trasak et al proposed a model in which actin binding induces autophosphorylation of YpkA on serine 90 and serine 95 (30). Using an in vivo labeling assay we demonstrated that a YpkA S90A/S95A mutant undergoes autophosphorylation and demonstrates substrate phosphorylation activity, indicating the presence of additional autophosphorylation sites.…”

“…Residues serine 90 and serine 95 were reported as autophosphorylation sites required for efficient activation and phosphorylation of exogenous substrates by YpkA (30). Both kinase and guanine nucleotide dissociation inhibitor domains of YpkA are important in the activity of full length YpkA (19,(31)(32).…”

“…Both kinase and guanine nucleotide dissociation inhibitor domains of YpkA are important in the activity of full length YpkA (19,(31)(32). The kinase activity of YpkA is dependent on its association with actin (21,30). Although YpkA has been shown to phosphorylate actin and otubain 1 in vitro, the physiological importance of these findings is unclear (21,24,25).…”

Insight into Bacterial Virulence Mechanisms against Host Immune Response via the Yersinia pestis-Human Protein-Protein Interaction Network

“…Previous studies have shown that VASP could promote actin polymerization (5,9,72). In order to see whether YpkA could affect the physiological function of VASP, we performed an actin polymerization assay using pyrene-labeled actin in the presence of the purified YpkA and VASP recombinant proteins (34).…”

Yersinia enterocolitica differentially modulates RhoG activity in host cells

“…Biolabs, Frankfurt, Germany) and transformed into Y. enterocolitica strain WA-C(pTTSS), resulting in strains WA-C(pTTSS+pYopER144A) and WA-C(pTTSS+pYopEΔMLD), respectively (Table 1). All GST-tagged proteins were purified from BL21 E. coli using glutathione-Sepharose 4B (GE Healthcare, Munich, Germany) as described elsewhere (Trasak et al, 2006). Where necessary, proteins were dialysed against PBS overnight at 4°C.…”