PXD055134-1

PXD055134 is an original dataset announced via ProteomeXchange.

Title	Revealing novel protein interaction partners of glyphosate in Escherichia coli
Description	Despite all debates about its safe use, glyphosate still is the most widely applied active ingredient in herbicide products with renewed approval in the European Union until 2033. Non-target organisms are commonly exposed to glyphosate as a matter of its mode of application, with its broader environmental and biological impacts remaining under investigation. Glyphosate displays structural similarity to phosphoenolpyruvate (PEP), thereby competitively inhibiting the 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS), crucial for the synthesis of aromatic amino acids in plants, fungi, bacteria, and archaea. The majority of microbes, including the gut bacterium Escherichia coli (E. coli), possess a glyphosate-sensitive class I EPSPS, making them vulnerable to glyphosate's effects. Yet, little is known about glyphosate’s interactions with other bacterial proteins or its broader modes of action at the proteome level. Here, we employed a quantitative proteomics and thermal proteome profiling (TPP) approach, to identify novel protein binding partners of glyphosate in the E. coli proteome. Glyphosate exposure significantly altered amino acid synthesizing pathways, including increased abundance in shikimate pathway proteins, suggesting a compensatory mechanism. Extracellular riboflavin concentrations were elevated upon glyphosate exposure, while intracellular levels remained stable. Thermal proteome profiling indicated an effect of glyphosate on the thermal stability of certain proteins beyond the target enzyme EPSPS, including AroH and ProA. An elevated structural similarity between the substrates of the interaction candidates and glyphosate, similar to the competitive binding between PEP and glyphosate at the EPSPS, could be a reason for their interaction with the herbicide. Overall, glyphosate induced metabolic disturbances in E. coli, extending beyond its primary target, thereby providing new insights into glyphosate's broader impact on microbial systems.
HostingRepository	PRIDE
AnnounceDate	2025-01-02
AnnouncementXML	Submission_2025-01-02_04:07:55.556.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Nico Jehmlich
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2024-08-23 07:19:47	ID requested
⏵ 1	2025-01-02 04:07:56	announced

10.1016/j.envint.2024.109243;

Aldehoff AS, T, ü, rkowsky D, Lohmann P, Homsi MN, Rolle-Kampczyk U, Ueberham E, Lehmann J, Bergen MV, Jehmlich N, Haange SB, Revealing novel protein interaction partners of glyphosate in Escherichia coli. Environ Int, 195():109243(2025) [pubmed]

submitter keyword: thermal proteome profiling, Escherichia coli, acute and chronic exposure,Glyphosate, protein interaction partner

Nico Jehmlich
contact affiliation	Helmholtz-Centre for Environmental Research - UFZ GmbH Department of Molecular Toxicology Permoserstrasse 15, 04318 Leipzig, Germany
contact email	nico.jehmlich@ufz.de
lab head
Nico Jehmlich
contact affiliation	Helmholtz-Centre for Environmental Research - UFZ
contact email	nico.jehmlich@ufz.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD055134
     1. Label: PRIDE project
     2. Name: Revealing novel protein interaction partners of glyphosate in Escherichia coli