ArticleJournal of bacteriology2005
Methionine sulfoxide reduction and assimilation in Escherichia coli: new role for the biotin sulfoxide reductase BisC.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 65 citations in OpenAlex.
- Where metabolism and virulence meet-sulfoxide reductases as determinants of bacterial survival.Biochemical Society transactions · 2026Review
- Resident and EngraftingbioRxiv : the preprint server for biology · 2026Article
- Beyond anaerobic respiration-new physiological roles for DmsABC and other S-/N-oxide reductases inJournal of bacteriology · 2025Article
- Formylation facilitates the reduction of oxidized initiator methionines.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Carbon substrate re-orders relative growth of a bacterium using Mo-, V-, or Fe-nitrogenase for nitrogen fixation.Environmental microbiology · 2022Article
- Article
- Computation of condition-dependent proteome allocation reveals variability in the macro and micro nutrient requirements for growth.PLoS computational biology · 2021Article
- Deletion of both methionine sulfoxide reductase A and methionine sulfoxide reductase C genes renders Salmonella Typhimurium highly susceptible to hypochlorite stress and poultry macrophages.Molecular biology reports · 2021Article
- Halo(natrono)archaea from hypersaline lakes can utilize sulfoxides other than DMSO as electron acceptors for anaerobic respiration.Extremophiles : life under extreme conditions · 2021Article
- Methionine Redox Homeostasis in Protein Quality Control.Frontiers in molecular biosciences · 2021Review
- The DmsABC Sulfoxide Reductase Supports Virulence in Non-typeableFrontiers in microbiology · 2021Article
- Ionizing Radiation-induced Proteomic Oxidation inMolecular & cellular proteomics : MCP · 2020Article
- Reduction of Protein Bound Methionine Sulfoxide by a Periplasmic Dimethyl Sulfoxide Reductase.Antioxidants (Basel, Switzerland) · 2020Article
- Adaptations of Escherichia coli strains to oxidative stress are reflected in properties of their structural proteomes.BMC bioinformatics · 2020Article
- Molybdenum Enzymes and How They Support Virulence in Pathogenic Bacteria.Frontiers in microbiology · 2020Review
- Article
- Complete Genome Sequence of Escherichia coli BE104, an MC4100 Derivative Lacking the Methionine Reductive Pathway.Microbiology resource announcements · 2019Article
- Methionine Sulfoxide Reductases of Archaea.Antioxidants (Basel, Switzerland) · 2018Review
- Oxidative stress, protein damage and repair in bacteria.Nature reviews. Microbiology · 2017Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Methionine ranks among the amino acids most sensitive to oxidation, which converts it to a racemic mixture of methionine-S-sulfoxide (Met-S-SO) and methionine-R-sulfoxide (Met-R-SO). The methionine sulfoxide reductases MsrA and MsrB reduce free and protein-bound MetSO, MsrA being specific for Met-S-SO and MsrB for Met-R-SO. In the present study, we report that an Escherichia coli metB1 auxotroph lacking both msrA and msrB is still able to use either of the two MetSO enantiomers. This indicates that additional methionine sulfoxide reductase activities occur in E. coli. BisC, a poorly characterized biotin sulfoxide reductase, was identified as one of these new methionine sulfoxide reductases. BisC was purified and found to exhibit reductase activity with free Met-S-SO but not with free Met-R-SO as a substrate. Moreover, a metB1 msrA msrB bisC strain of E. coli was unable to use Met-S-SO for growth, but it retained the ability to use Met-R-SO. Mass spectrometric analyses indicated that BisC is unable to reduce protein-bound Met-S-SO. Hence, this study shows that BisC has an essential role in assimilation of oxidized methionines. Moreover, this work provides the first example of an enzyme that reduces free MetSO while having no activity on peptide-bound MetSO residues.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.