sidj - SidJ is a protein produced by pt kiyokuni Legionella pneumophila that orchestrates this intracellular pathogens establishment within the host cell SidJ prevents lysosome fusion with the vacuole within which the bacterium resides and replicates SidJ also modulates the toxicity of the SidE family ubiquitin ligases that catalyze phosphoribosyllinked host protein ubiquitination A unique deubiquitinase that deconjugates phosphoribosyllinked protein Legionella pneumophila encodes a family of phosphoribosyl ubiquitination ligases SidE essential for the bacterium to establish successful infection Four independent studies now show that the SidE family of ubiquitin ligases are regulated by a novel mechanism of glutamylation via a pseudokinaselike Legionella effector SidJ in an ATP and calmodulindependent manner Structural and mechanistic basis for protein glutamylation by the Effector proteins translocated by the DotIcm type IV secretion system determine the virulence of Legionella pneumophila L pneumophilaAmong these effectors members of the SidE family SidEs regulate several cellular processes through a unique phosphoribosyl ubiquitination mechanism mediated by another effector SidJ In Legionella pneumophila the effector SidJ induces the covalent attachment of glutamate moieties to SdeA in a calmodulindependent manner inhibiting SidEmediated ubiquitination and regulating The kinase domain transfers phosphate from ATP to substrates However the Legionella effector SidJ adopts a kinase fold yet catalyzes calmodulin CaMdependent glutamylation to inactivate the SidE ubiquitin ligases The structural and mechanistic basis in which the kinase domain catalyzes protein glutamylation is unknown Bacterial pseudokinase catalyzes protein polyglutamylation to inhibit Glutamylation of Bacterial Ubiquitin Ligases by a Legionella Regulation of phosphoribosyl ubiquitination by a calmodulin Nature Inhibition of bacterial ubiquitin ligases w210 by SidJcalmodulin Nature The family of bacterial SidE enzymes catalyses phosphoribosyllinked serine ubiquitination and promotes infectivity of Legionella pneumophila a pathogenic bacteria that causes Legionnaires disease 13SidE enzymes share the genetic locus with the Legionella effector SidJ that spatiotemporally opposes the toxicity of these enzymes in yeast and mammalian cells through a mechanism that is To elucidate the biological function of SidJ we performed sequence analyses and found that the Cterminus of SidJ contains the sequence IQxxxRxxRK which resembles the IQ motif found in a number proteins that mediates binding with calmodulin CaM in the absence of Ca 2 Figure 1A Rhoads and Friedberg 1997To test whether this predicted IQ motif in SidJ can mediate an interaction Inhibition of bacterial ubiquitin ligases by SidJcalmodulin catalysed Protein polyglutamylation catalyzed by the bacterial calmodulin eLife Virulence effector SidJ evolution in Legionella pneumophila is driven SidJ is a member of a twogene family its homolog SdjA which shares 52 identity and 60 similarity to SidJ is also a substrate of the DotIcm transporter 23Importantly all of the residues In cells infected with Legionella pneumophila the pseudo kinase SidJ is activated upon forming a complex with human calmodulin and catalyses glutamylation of SidE ubiquitin ligases which Enzymes with a protein kinase fold transfer phosphate from adenosine 5triphosphate ATP to substrates in a process known as phosphorylation Here we show that the iLegionellai metaeffector SidJ adopts a protein kinase fold yet unexpectedly catalyzes protein polyglutamylation SidJ is acti Bacterial pseudokinase catalyzes romanced protein polyglutamylation to inhibit
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