Relative impact of three growth conditions on the Escherichia coli protein acetylome
Summary: Nε-lysine acetylation is a common posttranslational modification observed in Escherichia coli. In the present study, integrative analysis of the proteome and acetylome was performed using label-free quantitative mass spectrometry to analyze the relative influence of three factors affecting...
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| Format: | Article |
| Language: | English |
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Elsevier
2024-02-01
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| Series: | iScience |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2589004224002384 |
| _version_ | 1797323801496649728 |
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| author | Gema Lozano-Terol Riccardo Zenezini Chiozzi Julia Gallego-Jara Rosa Alba Sola-Martínez Adrián Martínez Vivancos Álvaro Ortega Albert J.R. Heck Manuel Cánovas Díaz Teresa de Diego Puente |
| author_facet | Gema Lozano-Terol Riccardo Zenezini Chiozzi Julia Gallego-Jara Rosa Alba Sola-Martínez Adrián Martínez Vivancos Álvaro Ortega Albert J.R. Heck Manuel Cánovas Díaz Teresa de Diego Puente |
| author_sort | Gema Lozano-Terol |
| collection | DOAJ |
| description | Summary: Nε-lysine acetylation is a common posttranslational modification observed in Escherichia coli. In the present study, integrative analysis of the proteome and acetylome was performed using label-free quantitative mass spectrometry to analyze the relative influence of three factors affecting growth. The results revealed differences in the proteome, mainly owing to the type of culture medium used (defined or complex). In the acetylome, 7482 unique acetylation sites were identified. Acetylation is directly related to the abundance of proteins, and the level of acetylation in each type of culture is associated with extracellular acetate concentration. Furthermore, most acetylated lysines in the exponential phase remained in the stationary phase without dynamic turnover. Interestingly, unique acetylation sites were detected in proteins whose presence or abundance was linked to the type of culture medium. Finally, the biological function of the acetylation changes was demonstrated for three central metabolic proteins (GapA, Mdh, and AceA). |
| first_indexed | 2024-03-08T05:34:23Z |
| format | Article |
| id | doaj.art-deb364d3ef9d406ea29b32f3e20ae1f8 |
| institution | Directory Open Access Journal |
| issn | 2589-0042 |
| language | English |
| last_indexed | 2024-03-08T05:34:23Z |
| publishDate | 2024-02-01 |
| publisher | Elsevier |
| record_format | Article |
| series | iScience |
| spelling | doaj.art-deb364d3ef9d406ea29b32f3e20ae1f82024-02-06T04:12:43ZengElsevieriScience2589-00422024-02-01272109017Relative impact of three growth conditions on the Escherichia coli protein acetylomeGema Lozano-Terol0Riccardo Zenezini Chiozzi1Julia Gallego-Jara2Rosa Alba Sola-Martínez3Adrián Martínez Vivancos4Álvaro Ortega5Albert J.R. Heck6Manuel Cánovas Díaz7Teresa de Diego Puente8Department of Biochemistry and Molecular Biology and Immunology (B), Faculty of Chemistry, University of Murcia, Campus of Espinardo, Regional Campus of International Excellence “Campus Mare Nostrum”, 30100 Murcia, SpainBiomolecular Mass Spectrometry and Proteomics, Bijvoet Centre for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padulaan 8, Utrecht 3584 CH, the NetherlandsDepartment of Biochemistry and Molecular Biology and Immunology (B), Faculty of Chemistry, University of Murcia, Campus of Espinardo, Regional Campus of International Excellence “Campus Mare Nostrum”, 30100 Murcia, SpainDepartment of Biochemistry and Molecular Biology and Immunology (B), Faculty of Chemistry, University of Murcia, Campus of Espinardo, Regional Campus of International Excellence “Campus Mare Nostrum”, 30100 Murcia, SpainDepartment of Biochemistry and Molecular Biology and Immunology (B), Faculty of Chemistry, University of Murcia, Campus of Espinardo, Regional Campus of International Excellence “Campus Mare Nostrum”, 30100 Murcia, SpainDepartment of Biochemistry and Molecular Biology and Immunology (B), Faculty of Chemistry, University of Murcia, Campus of Espinardo, Regional Campus of International Excellence “Campus Mare Nostrum”, 30100 Murcia, SpainBiomolecular Mass Spectrometry and Proteomics, Bijvoet Centre for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padulaan 8, Utrecht 3584 CH, the NetherlandsDepartment of Biochemistry and Molecular Biology and Immunology (B), Faculty of Chemistry, University of Murcia, Campus of Espinardo, Regional Campus of International Excellence “Campus Mare Nostrum”, 30100 Murcia, SpainDepartment of Biochemistry and Molecular Biology and Immunology (B), Faculty of Chemistry, University of Murcia, Campus of Espinardo, Regional Campus of International Excellence “Campus Mare Nostrum”, 30100 Murcia, Spain; Corresponding authorSummary: Nε-lysine acetylation is a common posttranslational modification observed in Escherichia coli. In the present study, integrative analysis of the proteome and acetylome was performed using label-free quantitative mass spectrometry to analyze the relative influence of three factors affecting growth. The results revealed differences in the proteome, mainly owing to the type of culture medium used (defined or complex). In the acetylome, 7482 unique acetylation sites were identified. Acetylation is directly related to the abundance of proteins, and the level of acetylation in each type of culture is associated with extracellular acetate concentration. Furthermore, most acetylated lysines in the exponential phase remained in the stationary phase without dynamic turnover. Interestingly, unique acetylation sites were detected in proteins whose presence or abundance was linked to the type of culture medium. Finally, the biological function of the acetylation changes was demonstrated for three central metabolic proteins (GapA, Mdh, and AceA).http://www.sciencedirect.com/science/article/pii/S2589004224002384Natural sciencesBiological sciencesBiochemistryMicrobiologyMicrobial physiologyApplied microbiology |
| spellingShingle | Gema Lozano-Terol Riccardo Zenezini Chiozzi Julia Gallego-Jara Rosa Alba Sola-Martínez Adrián Martínez Vivancos Álvaro Ortega Albert J.R. Heck Manuel Cánovas Díaz Teresa de Diego Puente Relative impact of three growth conditions on the Escherichia coli protein acetylome iScience Natural sciences Biological sciences Biochemistry Microbiology Microbial physiology Applied microbiology |
| title | Relative impact of three growth conditions on the Escherichia coli protein acetylome |
| title_full | Relative impact of three growth conditions on the Escherichia coli protein acetylome |
| title_fullStr | Relative impact of three growth conditions on the Escherichia coli protein acetylome |
| title_full_unstemmed | Relative impact of three growth conditions on the Escherichia coli protein acetylome |
| title_short | Relative impact of three growth conditions on the Escherichia coli protein acetylome |
| title_sort | relative impact of three growth conditions on the escherichia coli protein acetylome |
| topic | Natural sciences Biological sciences Biochemistry Microbiology Microbial physiology Applied microbiology |
| url | http://www.sciencedirect.com/science/article/pii/S2589004224002384 |
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