Identification of proteins induced by polycyclic aromatic hydrocarbon and proposal of the phenanthrene catabolic pathway in Amycolatopsis tucumanensis DSM 45259
In the present study the polycyclic aromatic hydrocarbon removal and metabolic adaptation of Amycolatopsis tucumanensis DSM 45259 were investigated. Analysis of one-dimensional gel electrophoresis of crude cell extracts revealed differential synthesis of proteins which were identified by MALDI-TOF....
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2019
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01476513_v175_n_p19_Bourguignon http://hdl.handle.net/20.500.12110/paper_01476513_v175_n_p19_Bourguignon |
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paper:paper_01476513_v175_n_p19_Bourguignon2023-06-08T15:12:55Z Identification of proteins induced by polycyclic aromatic hydrocarbon and proposal of the phenanthrene catabolic pathway in Amycolatopsis tucumanensis DSM 45259 Amycolatopsis Biodegradation Metabolites Phenanthrene metabolic pathway Proteomics aconitate hydratase alcohol dehydrogenase aldehyde dehydrogenase amidase chaperonin 60 DNA directed DNA polymerase gamma elongation factor Ts elongation factor Tu enoyl coenzyme A hydratase heat shock protein methane monooxygenase naphthalene oxygenase phenanthrene polycyclic aromatic hydrocarbon protein DnaK pyrene pyruvate dehydrogenase bacterium biodegradation catabolism metabolite PAH phenanthrene protein proteomics Amycolatopsis Article bacterial strain bioremediation catabolism controlled study energy yield nonhuman oxidative stress protein analysis protein degradation protein synthesis proteomics signal transduction two dimensional gel electrophoresis Amycolatopsis In the present study the polycyclic aromatic hydrocarbon removal and metabolic adaptation of Amycolatopsis tucumanensis DSM 45259 were investigated. Analysis of one-dimensional gel electrophoresis of crude cell extracts revealed differential synthesis of proteins which were identified by MALDI-TOF. To elucidate the phenanthrene metabolic pathway in A. tucumanensis DSM45259, two-dimensional electrophoresis and detection of phenanthrene degradation intermediates by GS-MS were performed. The presence of aromatic substrates resulted in changes in the abundance of proteins involved in the metabolism of aromatic compounds, oxidative stress response, energy production and protein synthesis. The obtained results allowed us to clarify the phenanthrene catabolic pathway, by confirming the roles of several proteins involved in the degradation process and comprehensive adaptation. This may clear the way for more efficient engineering of bacteria in the direction of more effective bioremediation applications. © 2019 2019 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01476513_v175_n_p19_Bourguignon http://hdl.handle.net/20.500.12110/paper_01476513_v175_n_p19_Bourguignon |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Amycolatopsis Biodegradation Metabolites Phenanthrene metabolic pathway Proteomics aconitate hydratase alcohol dehydrogenase aldehyde dehydrogenase amidase chaperonin 60 DNA directed DNA polymerase gamma elongation factor Ts elongation factor Tu enoyl coenzyme A hydratase heat shock protein methane monooxygenase naphthalene oxygenase phenanthrene polycyclic aromatic hydrocarbon protein DnaK pyrene pyruvate dehydrogenase bacterium biodegradation catabolism metabolite PAH phenanthrene protein proteomics Amycolatopsis Article bacterial strain bioremediation catabolism controlled study energy yield nonhuman oxidative stress protein analysis protein degradation protein synthesis proteomics signal transduction two dimensional gel electrophoresis Amycolatopsis |
| spellingShingle |
Amycolatopsis Biodegradation Metabolites Phenanthrene metabolic pathway Proteomics aconitate hydratase alcohol dehydrogenase aldehyde dehydrogenase amidase chaperonin 60 DNA directed DNA polymerase gamma elongation factor Ts elongation factor Tu enoyl coenzyme A hydratase heat shock protein methane monooxygenase naphthalene oxygenase phenanthrene polycyclic aromatic hydrocarbon protein DnaK pyrene pyruvate dehydrogenase bacterium biodegradation catabolism metabolite PAH phenanthrene protein proteomics Amycolatopsis Article bacterial strain bioremediation catabolism controlled study energy yield nonhuman oxidative stress protein analysis protein degradation protein synthesis proteomics signal transduction two dimensional gel electrophoresis Amycolatopsis Identification of proteins induced by polycyclic aromatic hydrocarbon and proposal of the phenanthrene catabolic pathway in Amycolatopsis tucumanensis DSM 45259 |
| topic_facet |
Amycolatopsis Biodegradation Metabolites Phenanthrene metabolic pathway Proteomics aconitate hydratase alcohol dehydrogenase aldehyde dehydrogenase amidase chaperonin 60 DNA directed DNA polymerase gamma elongation factor Ts elongation factor Tu enoyl coenzyme A hydratase heat shock protein methane monooxygenase naphthalene oxygenase phenanthrene polycyclic aromatic hydrocarbon protein DnaK pyrene pyruvate dehydrogenase bacterium biodegradation catabolism metabolite PAH phenanthrene protein proteomics Amycolatopsis Article bacterial strain bioremediation catabolism controlled study energy yield nonhuman oxidative stress protein analysis protein degradation protein synthesis proteomics signal transduction two dimensional gel electrophoresis Amycolatopsis |
| description |
In the present study the polycyclic aromatic hydrocarbon removal and metabolic adaptation of Amycolatopsis tucumanensis DSM 45259 were investigated. Analysis of one-dimensional gel electrophoresis of crude cell extracts revealed differential synthesis of proteins which were identified by MALDI-TOF. To elucidate the phenanthrene metabolic pathway in A. tucumanensis DSM45259, two-dimensional electrophoresis and detection of phenanthrene degradation intermediates by GS-MS were performed. The presence of aromatic substrates resulted in changes in the abundance of proteins involved in the metabolism of aromatic compounds, oxidative stress response, energy production and protein synthesis. The obtained results allowed us to clarify the phenanthrene catabolic pathway, by confirming the roles of several proteins involved in the degradation process and comprehensive adaptation. This may clear the way for more efficient engineering of bacteria in the direction of more effective bioremediation applications. © 2019 |
| title |
Identification of proteins induced by polycyclic aromatic hydrocarbon and proposal of the phenanthrene catabolic pathway in Amycolatopsis tucumanensis DSM 45259 |
| title_short |
Identification of proteins induced by polycyclic aromatic hydrocarbon and proposal of the phenanthrene catabolic pathway in Amycolatopsis tucumanensis DSM 45259 |
| title_full |
Identification of proteins induced by polycyclic aromatic hydrocarbon and proposal of the phenanthrene catabolic pathway in Amycolatopsis tucumanensis DSM 45259 |
| title_fullStr |
Identification of proteins induced by polycyclic aromatic hydrocarbon and proposal of the phenanthrene catabolic pathway in Amycolatopsis tucumanensis DSM 45259 |
| title_full_unstemmed |
Identification of proteins induced by polycyclic aromatic hydrocarbon and proposal of the phenanthrene catabolic pathway in Amycolatopsis tucumanensis DSM 45259 |
| title_sort |
identification of proteins induced by polycyclic aromatic hydrocarbon and proposal of the phenanthrene catabolic pathway in amycolatopsis tucumanensis dsm 45259 |
| publishDate |
2019 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01476513_v175_n_p19_Bourguignon http://hdl.handle.net/20.500.12110/paper_01476513_v175_n_p19_Bourguignon |
| _version_ |
1768545778505089024 |