Dataset Information

Neurospora crassa eisosome LC-MS

ABSTRACT: To identify proteins that localize to MCC/eisosomes in N. crassa, we isolated proteins that co-purified with the core MCC/eisosome protein LSP-1, which was tagged with GFP. Proteins that co-fractionated with LSP-1::GFP were then identified by mass spectrometry.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Neurospora Crassa Or74a

SUBMITTER: Qin Yang

LAB HEAD: Frank Kempken

PROVIDER: PXD020724 | Pride | 2021-09-09

REPOSITORIES: pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	Merged-samples_FungiDB-38_NcrassaOR74A.sf3	Other
	Q_50ul_insol.raw	Raw
	Qy600s2_200fmolbsa_25ul_01immunoprecipitationpurification.raw	Raw
	Qy600s2_200fmolbsa_25ul_02immunoprecipitationpurification.raw	Raw

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Publications

The Composition and the Structure of MCC/Eisosomes in Neurospora crassa.

Yang Qin Q Kempken Frank F

Frontiers in microbiology 20200918

MCC/eisosomes are protein-organized domains in the plasma membrane of fungi and algae. However, the composition and function(s) of MCC/eisosomes in the filamentous fungus Neurospora crassa were previously unknown. To identify proteins that localize to MCC/eisosomes in N. crassa, we isolated proteins that co-purified with the core MCC/eisosome protein LSP-1, which was tagged with GFP. Proteins that co-fractionated with LSP-1:GFP were then identified by mass spectrometry. Eighteen pr ...[more]

PMID: 33071997

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Project description:Pathogenic microorganisms often secrete proteins or nucleic acids that mimic the structure and/or function of molecules expressed within their host counterparts. This molecular mimicry empowers pathogens to target and subvert critical host processes and helps establish their infectious paradigm. We report here that the intracellular bacterium Legionella pneumophila (L.p.) secretes a toxin named SidI (substrate of icm/dot transporter I) which possesses a transfer RNA (tRNA) like fold and functions as a mannosyl transferase enzyme. The 3.1 Å cryo-EM structure of SidI reveals an N-terminal domain that exhibits a characteristic ‘inverted L-shape’ and charge conservation that is present in two known protein mimics of tRNAs, the bacterial elongation factor EF-G and the mammalian release factor eRF1. In addition, SidI’s C-terminal domain adopts a glycosyl transferase B fold and shares considerable homology to a known mannosyl transferase. This molecular coupling of fold and enzymatic function allows SidI to bind to and enzymatically modify components of the host translational apparatus, including the ribosome, resulting in a robust block of protein synthesis that is comparable to the potency exhibited by the toxin ricin. Additionally, we uncovered that the translational pausing activated by SidI elicits a stress response signature that is highly similar to one activated by elongation inhibitors that target the ribosome and induce ribosome collisions. SidI-mediated perturbations to the ribosome activate the stress kinases ZAKα and p38, that in turn drive the accumulation of the protein activating transcription factor 3 (ATF3). Intriguingly, ATF3 escapes the translation block imposed by SidI, translocates to the nucleus, and subsequently orchestrates the transcription of stress-inducible genes that culminates in the activation of a cell death program. Thus, using Legionella and its effectors as tools, we have unravelled the role of a ribosome to nuclear signaling pathway that regulates cell fate.

Dataset Information

Neurospora crassa eisosome LC-MS

Dataset's files

Publications

The Composition and the Structure of MCC/Eisosomes in <i>Neurospora crassa</i>.

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