PXD011771 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Laboratory evolution of Escherichia coli enables life based on fluorinated amino acids |
Description | Organofluorine compounds are toxic to various living beings in different habitats. This usher the development of strategies based on the metabolic capacity of various fast-growing microbial strains to evolve an effective adaptation strategy for efficient environmental cleaning. We tackle this problem by trying to answer an essential question: can fluorinated amino acids be used as xenobiotics in general to build up biomass, or do large amounts of fluorine in the cells render them nonviable? To gain information about the effect of long-term exposure of a cellular proteome to fluorine, we constructed an experimental model based on bacterial adaptation in artificial fluorinated habitats. In particular, we propagated Escherichia coli (E. coli) in the presence of either 4- or 5-fluoroindole as essential precursors for the in situ synthesis of tryptophan (Trp) analogues. We found that full adaptation requires astonishingly few genetic mutations but is accompanied by large rearrangements in regulatory networks, membrane integrity and quality control of protein folding. These findings highlight the cellular mechanisms of the evolutionary adaption process and provide the molecular foundation for novel and innovative bioengineering of microbial strains potentially useful in bioaugmentation in fluorine-contaminated areas. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_05:15:30.213.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Ludwig Sinn |
SpeciesList | scientific name: Escherichia coli; NCBI TaxID: 562; |
ModificationList | 5'-fluoro-L-tryptophan; 6x(13)C labeled residue; 4'-fluoro-L-tryptophan; monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue |
Instrument | Orbitrap Fusion Lumos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2018-11-21 00:15:34 | ID requested | |
1 | 2020-11-23 23:08:03 | announced | |
⏵ 2 | 2024-10-22 05:15:30 | announced | 2024-10-22: Updated project metadata. |
Publication List
Dataset with its publication pending |
Keyword List
curator keyword: Biological |
submitter keyword: E coli, Fluorine, SILAC, noncanonical, Evolution, Multi-Omics |
Contact List
Juri Rappsilber |
contact affiliation | Bioanalytics, Institute of Biotechnology, Technische Universität Berlin, 13355 Berlin, Germany. Wellcome Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3BF, United Kingdom. |
contact email | juri.rappsilber@tu-berlin.de |
lab head | |
Ludwig Sinn |
contact affiliation | TU Berlin, Bioanalytics, J. Rappsilber PhD |
contact email | l.sinn@tu-berlin.de |
dataset submitter | |
Full Dataset Link List
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/2020/11/PXD011771 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD011771
- Label: PRIDE project
- Name: Laboratory evolution of Escherichia coli enables life based on fluorinated amino acids