<< Full experiment listing


DataSet Summary

  • HostingRepository: PRIDE
  • AnnounceDate: 2019-06-12
  • AnnouncementXML: Submission_2019-06-13_07:05:34.xml
  • DigitalObjectIdentifier:
  • ReviewLevel: Peer-reviewed dataset
  • DatasetOrigin: Original data
  • RepositorySupport: Unsupported dataset by repository
  • PrimarySubmitter: Karel Harant
  • Title: Resolving oxidative damage to methionine by an unexpected membrane-associated stereoselective reductase discovered using chiral fluorescent probes
  • Description: Non-enzymatic oxidative processes in living organisms are one of the inevitable consequences of respiration and environmental conditions. They can lead to the formation of two stereoisomers (R and S) of methionine sulfoxide, and the redox balance between methionine and methionine sulfoxide in proteins has profound functional consequences. Methionine oxidation can be reverted enzymatically by methionine sulfoxide reductases (Msrs). The two enzyme classes known to fulfil this role are MsrA (reducing (S)-sulfoxides), and MsrB (reducing (R)-sulfoxides). They are strictly stereoselective and conserved throughout the tree of life. Under stress conditions such as stationary phase and nutrient starvation, E.coli upregulates expression of MsrA but similar effect has not been described for MsrB, raising a conundrum of the pathway enabling reduction of the (R)-isomer of methionine sulfoxide in these conditions. Using the recently developed chiral fluorescent probes Sulfox-1 we show that in stationary phase stressed E. coli, MsrA does have a stereocomplementary, (R)-sulfoxide-reducing counterpart. However, this activity is not provided by MsrB as expected, but instead by the DMSO reductase complex DmsABC, widely conserved in bacteria. This finding reveals an unexpected diversity in the metabolic enzymes of redox regulation concerning methionine, which should be taken into account in any antibacterial strategies exploiting oxidative stress.
  • SpeciesList: scientific name: Escherichia coli; NCBI TaxID: 562;
  • ModificationList: iodoacetamide derivatized residue
  • Instrument: LTQ FT

Dataset History

VersionDatetimeStatusChangeLog Entry
02019-04-23 07:52:26ID requested
12019-06-12 06:12:47announced
22019-06-13 07:05:43announcedUpdated publication reference for PubMed record(s): 31166082.

Publication List

  1. Makukhin N, Havelka V, Poláchová E, Rampírová P, Tarallo V, Strisovsky K, Míšek J, Resolving oxidative damage to methionine by an unexpected membrane-associated stereoselective reductase discovered using chiral fluorescent probes. FEBS J, ():(2019) [pubmed]

Keyword List

  1. submitter keyword: methionine sulfoxide, E.coli , oxidative damage

Contact List

    Kvido Strisovsky
    • contact affiliation: Institute of Organic Chemistry and Biochemistry, Czech Academy of Science, Flemingovo n.2, 16000 Prague, Czech Republic
    • contact email: kvido.strisovsky@uochb.cas.cz
    • lab head:
    Karel Harant
    • contact affiliation: Charles University
    • contact email: harant@natur.cuni.cz
    • dataset submitter:

Full Dataset Link List

  1. Dataset FTP location
  2. PRIDE project URI
Repository Record List

If you have a question or comment about ProteomeXchange, please contact us!
to receive all new ProteomeXchange dataset release announcements!