PXD019288 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | COPPER INDUCES PROTEIN AGGREGATION, A TOXIC PROCESS COMPENSATED BY MOLECULAR CHAPERONES. |
Description | Copper is a powerful antimicrobial and antiviral agent, which has interest through several biomedical applications. Nevertheless, how copper induces the cellular damage is not fully understood. Two main mechanisms are claimed to be involved, i.e. Cu catalyzed reactive oxygen species production (ROS) and replacements of other essential metal ions, such as Fe in Fe-S clusters by Cu. In the present work, we cumulate strong evidence for the importance of a third mechanism, which proposes that Cu damaging effects are due to its ability to cause massive protein aggregation in a ROS independent mechanism. We further show that Hsp33, a redox-regulated molecular chaperone in Escherichia coli, can prevent Cu-induced protein aggregation, suggesting an important role of the chaperoning system in defense against Cu-toxicity. A closer inspection of the mechanism of how Cu can activate Hsp33 revealed two intriguing features, i) a redox-state specificity of Cu+ vs Cu2+, and ii) an unprecedented mechanism of Hsp33-activation via a non-redox trans-metalation. Indeed, our data suggest that two Cu+ bind to the Zn-Cys4-finger site in Hsp33, which lead to a replacement of one Zn2+ by two Cu+ without Cys oxidation. In contrast, Cu2+ oxidizes the Cys in the Zn-finger, analogue to other oxidative stress effectors of Hsp33. Hence, the present results give several new insights in the antimicrobial mechanism of Cu and how bacteria defend against it. |
HostingRepository | PRIDE |
AnnounceDate | 2022-02-22 |
AnnouncementXML | Submission_2022-02-22_04:13:29.309.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Rosi Fassler |
SpeciesList | scientific name: Escherichia coli; NCBI TaxID: 562; |
ModificationList | iodoacetamide derivatized residue |
Instrument | Q Exactive HF |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2020-05-18 22:22:55 | ID requested | |
1 | 2022-02-10 08:52:06 | announced | |
⏵ 2 | 2022-02-22 04:13:29 | announced | 2022-02-22: Updated project metadata. |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: Hsp33, Escherichia coli, molecular chaperone,copper, aggregation |
Contact List
Dana Reichmann |
contact affiliation | Dept. of Biological Chemistry, room 1-637 The Alexander Silberman Institute of Life Science The Hebrew University of Jerusalem |
contact email | danare@mail.huji.ac.il |
lab head | |
Rosi Fassler |
contact affiliation | Hebrew University of Jerusalem |
contact email | rosi.fassler@mail.huji.ac.il |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD019288
- Label: PRIDE project
- Name: COPPER INDUCES PROTEIN AGGREGATION, A TOXIC PROCESS COMPENSATED BY MOLECULAR CHAPERONES.