PXD011023 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Heat and pressure resistance relates to protein folding and aggregation |
Description | The locus of heat resistance (LHR) confers extreme heat resistance in E. coli. This study explored the role of the LHR in pressure resistance of E. coli, as well as its relationship with protein folding and aggregation in vivo. The role of LHR was investigated in E. coli MG1655 expressing a ibpA-yfp fusion. The expression of proteins by the LHR was determined by mass spectrometry based proteomics; inclusion bodies of untreated and treated cells were also analysed by proteomics, and by observation with fluorescence microscope. In total, 11 proteins of LHR were expressed, including sHSP20, ClpKGI, sHSP, YdfX1 and YdfX2, HdeD, KefB, Trx, PsiE, DegP, and a hypothetical proteins. The proteomic analysis of inclusion bodies revealed a differential abundance of proteins related to oxidative stress in strains carrying the LHR. The LHR reduced the presence of inclusion bodies after heat or pressure treatment, indicating that proteins expressed by the LHR prevent or reverse protein aggregation. The phenotype of the LHR was also mediated by the expression of a fragment containing only sHSP20, ClpKGI, sHSP. The LHR and the fragment encoding only for sHSP20, ClpKGI, sHSP also enhanced pressure resistance in E. coli MG1655 but had no effect on pressure resistance of E. coli LMM1010. In conclusion, the LHR confers pressure resistance to some strains of E. coli, and reduces protein aggregation. Pressure and heat resistance, however, are also dependent on additional LHR-encoded functions. |
HostingRepository | PRIDE |
AnnounceDate | 2020-01-27 |
AnnouncementXML | Submission_2020-01-27_07:40:54.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Stephanie Heinzlmeir |
SpeciesList | scientific name: Escherichia coli; NCBI TaxID: 562; |
ModificationList | iodoacetamide derivatized residue |
Instrument | LTQ Orbitrap Velos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2018-09-06 05:58:41 | ID requested | |
⏵ 1 | 2020-01-27 07:40:55 | announced | |
2 | 2024-10-22 04:48:38 | announced | 2024-10-22: Updated project metadata. |
Publication List
Dataset with its publication pending |
Keyword List
curator keyword: Biological |
submitter keyword: Escherichia coli, inclusion bodies, pressure resistance, food preservation |
Contact List
BayBioMS Bavarian Center for Biomolecular Mass Spectrometry |
contact affiliation | Technical University of Munich TUM School of Life Scienes Weihenstephan Freising, Germany |
contact email | stephanie.heinzlmeir@tum.de |
lab head | |
Stephanie Heinzlmeir |
contact affiliation | Chair of Proteomics and Bioanalytics, Technische Universität München, Germany |
contact email | stephanie.heinzlmeir@tum.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD011023
- Label: PRIDE project
- Name: Heat and pressure resistance relates to protein folding and aggregation