The <i>Legionella</i> Effector SdjA Is a Bifunctional Enzyme That Distinctly Regulates Phosphoribosyl Ubiquitination
Lei Song, Yongchao Xie, Chuang Li, Lidong Wang, Chunlin He, Yong Zhang, Jingya Yuan, Jingjing Luo, Xi Liu, Yu Xiu, Hang Li, Marina Gritsenko, Ernesto Nakayasu, Yue Feng, Zhao‐Qing Luo
Abstract
. SidJ inhibits the activity of the SidE family by a calmodulin (CaM)-dependent glutamylase activity. Here, we found that SdjA is a dual function protein: it is a CaM-dependent glutamylase against SdeB and SdeC but exhibits deglutamylase activity toward SdeA that has been modified by SidJ, indicating that SdjA functions to fine-tune the activity of SidEs. These findings have paved the way for future structural and functional analysis of SdjA, which may reveal novel mechanism for isopeptide bond cleavage and provide insights into the study of protein evolution.
Topics & Concepts
EffectorLegionella pneumophilaUbiquitinCell biologyBiogenesisBiologyLegionellaSecretionEnzymeChemistryBiochemistryGeneticsBacteriaGeneLegionella and Acanthamoeba researchNeutrophil, Myeloperoxidase and Oxidative MechanismsHeme Oxygenase-1 and Carbon Monoxide