Non-enzymatic acetylation inhibits glycolytic enzymes in Escherichia coli
Summary: Advanced mass spectrometry methods have detected thousands of post-translational phosphorylation and acetylation sites in bacteria, but their functional role and the enzymes catalyzing these modifications remain largely unknown. In addition to enzymatic acetylation, lysine residues can also...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2023-01-01
|
| Series: | Cell Reports |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124722018514 |
| _version_ | 1797960205686800384 |
|---|---|
| author | Evgeniya Schastnaya Peter Francis Doubleday Luca Maurer Uwe Sauer |
| author_facet | Evgeniya Schastnaya Peter Francis Doubleday Luca Maurer Uwe Sauer |
| author_sort | Evgeniya Schastnaya |
| collection | DOAJ |
| description | Summary: Advanced mass spectrometry methods have detected thousands of post-translational phosphorylation and acetylation sites in bacteria, but their functional role and the enzymes catalyzing these modifications remain largely unknown. In addition to enzymatic acetylation, lysine residues can also be chemically acetylated by the metabolite acetyl phosphate. In Escherichia coli, acetylation at over 3,000 sites has been linked to acetyl phosphate, but the functionality of this widespread non-enzymatic acetylation is even less clear than the enzyme-catalyzed one. Here, we investigate the role of acetyl-phosphate-mediated acetylation in E. coli central metabolism. Out of 19 enzymes investigated, only GapA and GpmA are acetylated at high stoichiometry, which inhibits their activity by interfering with substrate binding, effectively reducing glycolysis when flux to or from acetate is high. Extrapolating our results to the whole proteome, maximally 10% of the reported non-enzymatically acetylated proteins are expected to reach a stoichiometry that could inhibit their activity. |
| first_indexed | 2024-04-11T00:42:40Z |
| format | Article |
| id | doaj.art-848148b543d54ca08dee18b81ec0ca0a |
| institution | Directory Open Access Journal |
| issn | 2211-1247 |
| language | English |
| last_indexed | 2024-04-11T00:42:40Z |
| publishDate | 2023-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj.art-848148b543d54ca08dee18b81ec0ca0a2023-01-06T04:16:55ZengElsevierCell Reports2211-12472023-01-01421111950Non-enzymatic acetylation inhibits glycolytic enzymes in Escherichia coliEvgeniya Schastnaya0Peter Francis Doubleday1Luca Maurer2Uwe Sauer3Institute of Molecular Systems Biology, ETH Zurich, 8093 Zurich, Switzerland; Life Science Zurich PhD Program on Systems Biology, 8093 Zurich, SwitzerlandInstitute of Molecular Systems Biology, ETH Zurich, 8093 Zurich, SwitzerlandInstitute of Molecular Systems Biology, ETH Zurich, 8093 Zurich, SwitzerlandInstitute of Molecular Systems Biology, ETH Zurich, 8093 Zurich, Switzerland; Corresponding authorSummary: Advanced mass spectrometry methods have detected thousands of post-translational phosphorylation and acetylation sites in bacteria, but their functional role and the enzymes catalyzing these modifications remain largely unknown. In addition to enzymatic acetylation, lysine residues can also be chemically acetylated by the metabolite acetyl phosphate. In Escherichia coli, acetylation at over 3,000 sites has been linked to acetyl phosphate, but the functionality of this widespread non-enzymatic acetylation is even less clear than the enzyme-catalyzed one. Here, we investigate the role of acetyl-phosphate-mediated acetylation in E. coli central metabolism. Out of 19 enzymes investigated, only GapA and GpmA are acetylated at high stoichiometry, which inhibits their activity by interfering with substrate binding, effectively reducing glycolysis when flux to or from acetate is high. Extrapolating our results to the whole proteome, maximally 10% of the reported non-enzymatically acetylated proteins are expected to reach a stoichiometry that could inhibit their activity.http://www.sciencedirect.com/science/article/pii/S2211124722018514CP: Microbiology |
| spellingShingle | Evgeniya Schastnaya Peter Francis Doubleday Luca Maurer Uwe Sauer Non-enzymatic acetylation inhibits glycolytic enzymes in Escherichia coli Cell Reports CP: Microbiology |
| title | Non-enzymatic acetylation inhibits glycolytic enzymes in Escherichia coli |
| title_full | Non-enzymatic acetylation inhibits glycolytic enzymes in Escherichia coli |
| title_fullStr | Non-enzymatic acetylation inhibits glycolytic enzymes in Escherichia coli |
| title_full_unstemmed | Non-enzymatic acetylation inhibits glycolytic enzymes in Escherichia coli |
| title_short | Non-enzymatic acetylation inhibits glycolytic enzymes in Escherichia coli |
| title_sort | non enzymatic acetylation inhibits glycolytic enzymes in escherichia coli |
| topic | CP: Microbiology |
| url | http://www.sciencedirect.com/science/article/pii/S2211124722018514 |
| work_keys_str_mv | AT evgeniyaschastnaya nonenzymaticacetylationinhibitsglycolyticenzymesinescherichiacoli AT peterfrancisdoubleday nonenzymaticacetylationinhibitsglycolyticenzymesinescherichiacoli AT lucamaurer nonenzymaticacetylationinhibitsglycolyticenzymesinescherichiacoli AT uwesauer nonenzymaticacetylationinhibitsglycolyticenzymesinescherichiacoli |