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Comment
. 2019 Dec;27(12):967-969.
doi: 10.1016/j.tim.2019.09.001. Epub 2019 Oct 14.

Glutamylation of Bacterial Ubiquitin Ligases by a Legionella Pseudokinase

Alan G Sulpizio  1 , Marena E Minelli  1 , Yuxin Mao  2
Affiliations
Comment

Glutamylation of Bacterial Ubiquitin Ligases by a Legionella Pseudokinase

Alan G Sulpizio et al. Trends Microbiol. 2019 Dec.

Abstract

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 pseudokinase-like Legionella effector, SidJ, in an ATP- and calmodulin-dependent manner.

Keywords: SdeA; SidE; SidJ; calmodulin; phosphoribosyl ubiquitination; post-translational modification.

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Figures

Figure 1.
Figure 1.. The Phosphoribosyl Ubiquitination (PR-ubiquitination) Pathway and Its Regulation by SidJ.
The SidE family effectors catalyze PR-ubiquitination using a molecule of NAD+. DupA and DupB are two PR-Ub-specific deubiquitinases (DUBs) that cleave the phosphoribosyl-ubiquitin (PR-Ub) moiety from PR-ubiquitinated substrates. Upon activation by calmodulin (CaM), the metaeffector SidJ catalyzes the glutamylation of SidE family ligases and hence inhibits the PR-ubiquitination activity of SidE. An unknown effector may exist in Legionella to revive SidE family ligases by removing glutamate modification from the ligases. Abbreviations: GLU, glutamate; NAM, nicotinamide; PPi, pyrophosphate.
See this image and copyright information in PMC

Comment on

References

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