Insights into the Lysine Acetylome of the Haloarchaeon <i>Haloferax volcanii</i> during Oxidative Stress by Quantitative SILAC-Based Proteomics
Oxidative stress adaptation strategies are important to cell function and are linked to cardiac, neurodegenerative disease, and cancer. Representatives of the <i>Archaea</i> domain are used as model organisms based on their extreme tolerance to oxidants and close evolutionary relationshi...
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| Format: | Article |
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MDPI AG
2023-06-01
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| Series: | Antioxidants |
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| Online Access: | https://www.mdpi.com/2076-3921/12/6/1203 |
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| author | Ricardo L. Couto-Rodríguez Jin Koh Sixue Chen Julie A. Maupin-Furlow |
| author_facet | Ricardo L. Couto-Rodríguez Jin Koh Sixue Chen Julie A. Maupin-Furlow |
| author_sort | Ricardo L. Couto-Rodríguez |
| collection | DOAJ |
| description | Oxidative stress adaptation strategies are important to cell function and are linked to cardiac, neurodegenerative disease, and cancer. Representatives of the <i>Archaea</i> domain are used as model organisms based on their extreme tolerance to oxidants and close evolutionary relationship with eukaryotes. A study of the halophilic archaeon <i>Haloferax volcanii</i> reveals lysine acetylation to be associated with oxidative stress responses. The strong oxidant hypochlorite: (i) stimulates an increase in lysine acetyltransferase <i>Hv</i>Pat2 to <i>Hv</i>Pat1 abundance ratios and (ii) selects for lysine deacetylase <i>sir2</i> mutants. Here we report the dynamic occupancy of the lysine acetylome of glycerol-grown <i>H. volcanii</i> as it shifts in profile in response to hypochlorite. These findings are revealed by the: (1) quantitative multiplex proteomics of the SILAC-compatible parent and <i>Δsir2</i> mutant strains and (2) label-free proteomics of H26 ‘wild type’ cells. The results show that lysine acetylation is associated with key biological processes including DNA topology, central metabolism, cobalamin biosynthesis, and translation. Lysine acetylation targets are found conserved across species. Moreover, lysine residues modified by acetylation and ubiquitin-like sampylation are identified suggesting post-translational modification (PTM) crosstalk. Overall, the results of this study expand the current knowledge of lysine acetylation in <i>Archaea</i>, with the long-term goal to provide a balanced evolutionary perspective of PTM systems in living organisms. |
| first_indexed | 2024-03-11T02:49:18Z |
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| last_indexed | 2024-03-11T02:49:18Z |
| publishDate | 2023-06-01 |
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| series | Antioxidants |
| spelling | doaj.art-013a4c10fa1c40b1a9393363756b6da52023-11-18T09:02:54ZengMDPI AGAntioxidants2076-39212023-06-01126120310.3390/antiox12061203Insights into the Lysine Acetylome of the Haloarchaeon <i>Haloferax volcanii</i> during Oxidative Stress by Quantitative SILAC-Based ProteomicsRicardo L. Couto-Rodríguez0Jin Koh1Sixue Chen2Julie A. Maupin-Furlow3Department of Microbiology and Cell Science, Institute of Food and Agricultural Sciences, University of Florida, Gainesville, FL 32611, USAProteomics and Mass Spectrometry, Interdisciplinary Center for Biotechnology Research, University of Florida, Gainesville, FL 32610, USAProteomics and Mass Spectrometry, Interdisciplinary Center for Biotechnology Research, University of Florida, Gainesville, FL 32610, USADepartment of Microbiology and Cell Science, Institute of Food and Agricultural Sciences, University of Florida, Gainesville, FL 32611, USAOxidative stress adaptation strategies are important to cell function and are linked to cardiac, neurodegenerative disease, and cancer. Representatives of the <i>Archaea</i> domain are used as model organisms based on their extreme tolerance to oxidants and close evolutionary relationship with eukaryotes. A study of the halophilic archaeon <i>Haloferax volcanii</i> reveals lysine acetylation to be associated with oxidative stress responses. The strong oxidant hypochlorite: (i) stimulates an increase in lysine acetyltransferase <i>Hv</i>Pat2 to <i>Hv</i>Pat1 abundance ratios and (ii) selects for lysine deacetylase <i>sir2</i> mutants. Here we report the dynamic occupancy of the lysine acetylome of glycerol-grown <i>H. volcanii</i> as it shifts in profile in response to hypochlorite. These findings are revealed by the: (1) quantitative multiplex proteomics of the SILAC-compatible parent and <i>Δsir2</i> mutant strains and (2) label-free proteomics of H26 ‘wild type’ cells. The results show that lysine acetylation is associated with key biological processes including DNA topology, central metabolism, cobalamin biosynthesis, and translation. Lysine acetylation targets are found conserved across species. Moreover, lysine residues modified by acetylation and ubiquitin-like sampylation are identified suggesting post-translational modification (PTM) crosstalk. Overall, the results of this study expand the current knowledge of lysine acetylation in <i>Archaea</i>, with the long-term goal to provide a balanced evolutionary perspective of PTM systems in living organisms.https://www.mdpi.com/2076-3921/12/6/1203<i>Archaea</i>halophilesoxidative stressmass spectrometrySILAClysine acetylation |
| spellingShingle | Ricardo L. Couto-Rodríguez Jin Koh Sixue Chen Julie A. Maupin-Furlow Insights into the Lysine Acetylome of the Haloarchaeon <i>Haloferax volcanii</i> during Oxidative Stress by Quantitative SILAC-Based Proteomics Antioxidants <i>Archaea</i> halophiles oxidative stress mass spectrometry SILAC lysine acetylation |
| title | Insights into the Lysine Acetylome of the Haloarchaeon <i>Haloferax volcanii</i> during Oxidative Stress by Quantitative SILAC-Based Proteomics |
| title_full | Insights into the Lysine Acetylome of the Haloarchaeon <i>Haloferax volcanii</i> during Oxidative Stress by Quantitative SILAC-Based Proteomics |
| title_fullStr | Insights into the Lysine Acetylome of the Haloarchaeon <i>Haloferax volcanii</i> during Oxidative Stress by Quantitative SILAC-Based Proteomics |
| title_full_unstemmed | Insights into the Lysine Acetylome of the Haloarchaeon <i>Haloferax volcanii</i> during Oxidative Stress by Quantitative SILAC-Based Proteomics |
| title_short | Insights into the Lysine Acetylome of the Haloarchaeon <i>Haloferax volcanii</i> during Oxidative Stress by Quantitative SILAC-Based Proteomics |
| title_sort | insights into the lysine acetylome of the haloarchaeon i haloferax volcanii i during oxidative stress by quantitative silac based proteomics |
| topic | <i>Archaea</i> halophiles oxidative stress mass spectrometry SILAC lysine acetylation |
| url | https://www.mdpi.com/2076-3921/12/6/1203 |
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