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- Author:
- Ruas, France Anne Dias; Barboza, Natália Rocha; Castro-Borges, William; Guerra-Sá, Renata
- Source:
- Journal of proteomics 2019 v.196 pp. 173-188
- ISSN:
- 1874-3919
- Subject:
- DNA repair; Meyerozyma guilliermondii; bacteria; biomass; bioremediation; byproducts; drainage; enzyme activity; gene expression regulation; haploidy; heavy metals; hyperaccumulators; liquid chromatography; manganese; mining; oxidative stress; peptides; pollution; protein composition; protein synthesis; proteins; proteome; proteomics; tandem mass spectrometry; yeasts; Brazil
- Abstract:
- ... Organisms, in general, respond to environmental stress by altering their pattern of protein expression (proteome), as an alternative to growing in stressful conditions. A strain of Meyerozyma guilliermondii resistant to manganese was isolated from a sample of water collected from mine drainage in southeastern Minas Gerais (Brazil), and demonstrated manganese detoxification capacity. Protein extrac ...
- DOI:
- 10.1016/j.jprot.2018.11.001
-
https://dx.doi.org/10.1016/j.jprot.2018.11.001
- Author:
- Türkowsky, Dominique; Lohmann, Patrick; Mühlenbrink, Marie; Schubert, Torsten; Adrian, Lorenz; Goris, Tobias; Jehmlich, Nico; von Bergen, Martin
- Source:
- Journal of proteomics 2019 v.192 pp. 10-17
- ISSN:
- 1874-3919
- Subject:
- Sulfurospirillum; anaerobes; anaerobic conditions; bacteria; biomass; dehalogenation; enzyme substrates; eukaryotic cells; ligands; mass spectrometry; melting; oxidoreductases; proteins; proteome; protocols; substrate specificity; temperature; tetrachloroethylene; thermal stability
- Abstract:
- ... Thermal proteome profiling (TPP) is increasingly applied in eukaryotes to investigate protein-ligand binding through protein melting curve shifts induced by the presence of a ligand. In anaerobic bacteria, identification of protein-substrate interactions is a major challenge. We applied TPP to Sulfurospirillum multivorans, which is able to use trichloroethene as electron acceptor for growth, to in ...
- DOI:
- 10.1016/j.jprot.2018.05.018
-
https://dx.doi.org/10.1016/j.jprot.2018.05.018