Proteomics

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Analysis of SdeA modification by SidJ

ABSTRACT: Legionella pneumophila is a pathogenic gram-negative bacterium that evades host defense pathways to establish its intracellular replicative niche1. SidE family (SidEs) effectors mediate phosphoribosyl (PR)-dependent ubiquitination of host substrates and promote bacterial infection. Legionella effector, SidJ shares the genetic locus with the SidEs and opposes their toxicity in yeast and mammalian cells through an unknown mechanism. Deletion of SidJ alone leads to a significant defect in the growth of Legionella in both its natural host amoeba and in murine macrophages. Here, we show that SidJ is a glutamylase that modifies the catalytic residue in the mono-ADPribosyl transferase (mART) domain of SidEs thus blocking their ubiquitin ligase activity. This reaction requires SidJ binding to calmodulin (CaM), which acts as an essential mammalian co-factor for SidJ. Using quantitative proteomics, we also uncovered multiple host proteins as potential targets of SidJ-mediated glutamylation.

INSTRUMENT(S): Orbitrap Fusion Lumos, LTQ Orbitrap Elite, Q Exactive

ORGANISM(S): Homo Sapiens (human) Legionella Pneumophila Subsp. Pneumophila (strain Philadelphia 1 / Atcc 33152 / Dsm 7513)

TISSUE(S): Permanent Cell Line Cell, Kidney

SUBMITTER: Florian Bonn  

LAB HEAD: Ivan Dikic

PROVIDER: PXD014362 | Pride | 2019-07-16

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
20170412_FB_Sagar_SidJ_IP_1_1.raw Raw
20170412_FB_Sagar_SidJ_IP_1_2.raw Raw
20170412_FB_Sagar_SidJ_IP_1_3.raw Raw
20170412_FB_Sagar_SidJ_IP_1_4.raw Raw
20170412_FB_Sagar_SidJ_IP_1_5.raw Raw
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Publications

The family of bacterial SidE enzymes catalyses phosphoribosyl-linked serine ubiquitination and promotes infectivity of Legionella pneumophila, a pathogenic bacteria that causes Legionnaires' disease<sup>1-3</sup>. SidE 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 currently unknown<sup>4-6</sup>. Deletion of SidJ leads to a substantial defect in the growth of  ...[more]

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