PXD014362

PXD014362 is an original dataset announced via ProteomeXchange.

Title	Analysis of SdeA modification by SidJ
Description	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.
HostingRepository	PRIDE
AnnounceDate	2019-07-16
AnnouncementXML	Submission_2019-07-29_07:30:37.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Florian Bonn
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606; scientific name: Legionella pneumophila subsp. pneumophila str. Philadelphia 1; NCBI TaxID: 272624;
ModificationList	L-isoglutamyl triglutamic acid; L-isoglutamyl diglutamic acid
Instrument	Orbitrap Fusion Lumos; Q Exactive; LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2019-06-24 08:23:47	ID requested
1	2019-07-16 02:50:07	announced
⏵ 2	2019-07-29 07:30:38	announced	Updated publication reference for PubMed record(s): 31330532.

Bhogaraju S, Bonn F, Mukherjee R, Adams M, Pfleiderer MM, Galej WP, Matkovic V, Lopez-Mosqueda J, Kalayil S, Shin D, Dikic I, Inhibition of bacterial ubiquitin ligases by SidJ-calmodulin catalysed glutamylation. Nature, 572(7769):382-386(2019) [pubmed]

submitter keyword: Legionella pneumophila, Glutamylation

Ivan Dikic
contact affiliation	Institute of Biochemistry 2 and BMLS, University Hospital, Goethe University, Frankfurt, Germany
contact email	ivan.dikic@biochem2.de
lab head
Florian Bonn
contact affiliation	University of Frankfurt
contact email	bonn@med.uni-frankfurt.de
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/07/PXD014362

PRIDE project URI

• PRIDE
  1. PXD014362
     1. Label: PRIDE project
     2. Name: Analysis of SdeA modification by SidJ