Glutamylation of Bacterial Ubiquitin Ligases by a Legionella Pseudokinase

Alan G Sulpizio; Marena E Minelli; Yuxin Mao

doi:10.1016/j.tim.2019.09.001

Glutamylation of Bacterial Ubiquitin Ligases by a Legionella Pseudokinase

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

Authors

Alan G Sulpizio¹, Marena E Minelli¹, Yuxin Mao²

Affiliations

¹ Weill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.
² Weill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA. Electronic address: ym253@cornell.edu.

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.

Publication types

Research Support, N.I.H., Extramural
Comment

MeSH terms

Bacterial Proteins
Legionella*
Ligases
Membrane Proteins
Ubiquitin*

Substances

Bacterial Proteins
Membrane Proteins
Ubiquitin
Ligases

Grants and funding

R01 GM116964/GM/NIGMS NIH HHS/United States