Cysteine biosynthesis contributes to β-methylamino-l-alanine tolerance in Escherichia coli.
- Publisher:
- Elsevier BV
- Publication Type:
- Journal Article
- Citation:
- Research in microbiology, 2021, 172, (6), pp. 103852
- Issue Date:
- 2021-07-08
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Full metadata record
Field | Value | Language |
---|---|---|
dc.contributor.author | Italiano, CJ | |
dc.contributor.author | Pu, L | |
dc.contributor.author | Violi, JP | |
dc.contributor.author | Duggin, IG | |
dc.contributor.author | Rodgers, KJ | |
dc.date.accessioned | 2022-01-04T02:17:21Z | |
dc.date.available | 2021-06-29 | |
dc.date.available | 2022-01-04T02:17:21Z | |
dc.date.issued | 2021-07-08 | |
dc.identifier.citation | Research in microbiology, 2021, 172, (6), pp. 103852 | |
dc.identifier.issn | 0923-2508 | |
dc.identifier.issn | 1769-7123 | |
dc.identifier.uri | http://hdl.handle.net/10453/152640 | |
dc.description.abstract | In contrast to mammalian cells, bacteria such as Escherichia coli have been shown to display tolerance towards the neurotoxin β-methylamino-l-alanine (BMAA) suggesting that these prokaryotes possess a way to metabolise BMAA or its products, resulting in their export, degradation, or detoxification. Single gene deletion mutants of E. coli K-12 with inactivated amino acid biosynthesis pathways were treated with 500 μg/ml BMAA and the resulting growth was monitored. Wild type E. coli and most of the gene deletion mutants displayed unaltered growth in the presence of BMAA over 12 h. Conversely, deletion of genes in the cysteine biosynthesis pathway, cysE, cysK or cysM resulted in a BMAA dose-dependent growth delay in minimal medium. Through further studies of the ΔcysE strain, we observed increased susceptibility to oxidative stress from H<sub>2</sub>O<sub>2</sub> in minimal medium, and disruptions in glutathione levels and oxidation state. The cysteine biosynthesis pathway is therefore linked to the tolerance of BMAA and oxidative stress in E. coli, which potentially represents a mechanism of BMAA detoxification. | |
dc.format | Print-Electronic | |
dc.language | eng | |
dc.publisher | Elsevier BV | |
dc.relation | http://purl.org/au-research/grants/arc/DP160105005 | |
dc.relation | http://purl.org/au-research/grants/arc/FT160100010 | |
dc.relation.ispartof | Research in microbiology | |
dc.relation.hasversion | Accepted version | en |
dc.relation.isbasedon | 10.1016/j.resmic.2021.103852 | |
dc.rights | info:eu-repo/semantics/embargoedAccess | |
dc.subject | 0605 Microbiology, 1108 Medical Microbiology | |
dc.subject.classification | Microbiology | |
dc.subject.mesh | Amino Acids, Diamino | |
dc.subject.mesh | Culture Media | |
dc.subject.mesh | Cyanobacteria Toxins | |
dc.subject.mesh | Cysteine | |
dc.subject.mesh | Cysteine Synthase | |
dc.subject.mesh | Drug Tolerance | |
dc.subject.mesh | Escherichia coli | |
dc.subject.mesh | Escherichia coli Proteins | |
dc.subject.mesh | Gene Deletion | |
dc.subject.mesh | Glutathione | |
dc.subject.mesh | Hydrogen Peroxide | |
dc.subject.mesh | Metabolic Networks and Pathways | |
dc.subject.mesh | Oxidation-Reduction | |
dc.subject.mesh | Oxidative Stress | |
dc.subject.mesh | Serine O-Acetyltransferase | |
dc.title | Cysteine biosynthesis contributes to β-methylamino-l-alanine tolerance in Escherichia coli. | |
dc.type | Journal Article | |
utslib.citation.volume | 172 | |
utslib.location.activity | France | |
utslib.for | 0605 Microbiology | |
utslib.for | 1108 Medical Microbiology | |
pubs.organisational-group | /University of Technology Sydney | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science | |
pubs.organisational-group | /University of Technology Sydney/Strength - CHT - Health Technologies | |
pubs.organisational-group | /University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science/School of Life Sciences | |
pubs.organisational-group | /University of Technology Sydney/Centre for Health Technologies (CHT) | |
utslib.copyright.status | open_access | * |
utslib.copyright.embargo | 2022-10-21T00:00:00+1000Z | |
dc.date.updated | 2022-01-04T02:17:13Z | |
pubs.issue | 6 | |
pubs.publication-status | Published | |
pubs.volume | 172 | |
utslib.citation.issue | 6 |
Abstract:
In contrast to mammalian cells, bacteria such as Escherichia coli have been shown to display tolerance towards the neurotoxin β-methylamino-l-alanine (BMAA) suggesting that these prokaryotes possess a way to metabolise BMAA or its products, resulting in their export, degradation, or detoxification. Single gene deletion mutants of E. coli K-12 with inactivated amino acid biosynthesis pathways were treated with 500 μg/ml BMAA and the resulting growth was monitored. Wild type E. coli and most of the gene deletion mutants displayed unaltered growth in the presence of BMAA over 12 h. Conversely, deletion of genes in the cysteine biosynthesis pathway, cysE, cysK or cysM resulted in a BMAA dose-dependent growth delay in minimal medium. Through further studies of the ΔcysE strain, we observed increased susceptibility to oxidative stress from H2O2 in minimal medium, and disruptions in glutathione levels and oxidation state. The cysteine biosynthesis pathway is therefore linked to the tolerance of BMAA and oxidative stress in E. coli, which potentially represents a mechanism of BMAA detoxification.
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