Dataset Information

AP-qMS of retron proteins in Salmonella enterica

ABSTRACT: We performed affinity purification coupled to quantitative mass spectrometry (AP-qMS) for proteins belonging to retrons of Salmonella enterica. We quantified the proteome of rcaT point mutants in Salmonella enterica. We quantified the proteome of phage P1vir in E. coli.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Escherichia Coli Salmonella Typhimurium (strain Lt2 / Sgsc1412 / Atcc 700720)

SUBMITTER: Andre Mateus

LAB HEAD: Athanasios Typas

PROVIDER: PXD022376 | Pride | 2022-06-13

REPOSITORIES: Pride

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			Action	DRS
	Bert_S1881_AM_rcoD_pulldown_FP_n1_R1_F1.raw	Raw
	Bert_S1881_AM_rcoD_pulldown_FP_n1_R1_F2.raw	Raw
	Bert_S1881_AM_rcoD_pulldown_FP_n1_R1_F3.raw	Raw
	Bert_S1881_AM_rcoD_pulldown_FP_n1_R1_F4.raw	Raw
	Bert_S1881_AM_rcoD_pulldown_FP_n1_R1_F5.raw	Raw

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Publications

Bacterial retrons encode phage-defending tripartite toxin-antitoxin systems.

Bobonis Jacob J Mitosch Karin K Mateus André A Karcher Nicolai N Kritikos George G Selkrig Joel J Zietek Matylda M Monzon Vivian V Pfalz Birgit B Garcia-Santamarina Sarela S Galardini Marco M Sueki Anna A Kobayashi Callie C Stein Frank F Bateman Alex A Zeller Georg G Savitski Mikhail M MM Elfenbein Johanna R JR Andrews-Polymenis Helene L HL Typas Athanasios A

Nature 20220718 7925

Retrons are prokaryotic genetic retroelements encoding a reverse transcriptase that produces multi-copy single-stranded DNA<sup>1</sup> (msDNA). Despite decades of research on the biosynthesis of msDNA<sup>2</sup>, the function and physiological roles of retrons have remained unknown. Here we show that Retron-Sen2 of Salmonella enterica serovar Typhimurium encodes an accessory toxin protein, STM14_4640, which we renamed as RcaT. RcaT is neutralized by the reverse transcriptase-msDNA antitoxin co ...[more]

PMID: 35850148

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Project description:Intracellular bacterial pathogens inject a cocktail of effector proteins into host cells to hijack diverse cellular processes and promote their survival and proliferation. Salmonella enterica serovar Typhimurium (STm) uses two Type 3 secretion system (T3SS) to deliver a suite of effector proteins into host cells, however, knowledge of their host-targets remains sparse. To systematically map STm effector-host protein-protein interactions (PPIs) during active infection, we generated a library of 32 STm strains expressing affinity-tagged effector proteins from their endogenous chromosomal loci. Tagged-effector strains were then used to infect macrophages or epithelial cells, and PPIs were detected by Affinity-Purification Quantitative Mass-Spectrometry (AP-QMS) under both native and cross-linking conditions. We recovered 25 previously described effector-host PPIs, along with 421 novel interactions across the two cell lines tested, as well as several effector-effector PPIs. While effectors converged on specific host cellular processes, which varied across cell types, most had multiple host targets. Using reciprocal co-immunoprecipitations, we could validated 13 out of 22 new PPIs, demonstrating an accuracy of at least 59% for the AP-QMS approach. To illustrate the utility of this resource for discovering novel infection biology, we first showed that SseJ and SseL cooperate to control cholesterol transport at the Salmonella Containing Vacuole (SCV) via the Niemann-Pick C1 protein (NPC1). Second, we uncovered that PipB directly binds and recruits the organelle contact site protein PDZD8 to the SCV. Third, we elucidated a novel mechanism whereby the effector kinase SteC promotes host actin bundling, by directly interacting and phosphorylating formin-like proteins. Overall, we provide a systems-wide host-bacterial pathogen physical interactome resource, to our knowledge the first in an infection context, with broad implications for effector function and cooperation.