Iron Availability Influences Protein Carbonylation in <i>Arabidopsis thaliana</i> Plants
Protein carbonylation is an irreversible form of post-translational modification triggered by reactive oxygen species in animal and plant cells. It occurs either through the metal-catalyzed oxidation of Lys, Arg, Pro, and Thr side chains or the addition of α, β-unsaturated aldehydes and ketones to t...
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MDPI AG
2023-06-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/24/11/9732 |
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| author | Adesola J. Tola Tagnon D. Missihoun |
| author_facet | Adesola J. Tola Tagnon D. Missihoun |
| author_sort | Adesola J. Tola |
| collection | DOAJ |
| description | Protein carbonylation is an irreversible form of post-translational modification triggered by reactive oxygen species in animal and plant cells. It occurs either through the metal-catalyzed oxidation of Lys, Arg, Pro, and Thr side chains or the addition of α, β-unsaturated aldehydes and ketones to the side chains of Cys, Lys, and His. Recent genetic studies concerning plants pointed to an implication of protein carbonylation in gene regulation through phytohormones. However, for protein carbonylation to stand out as a signal transduction mechanism, such as phosphorylation and ubiquitination, it must be controlled in time and space by a still unknown trigger. In this study, we tested the hypothesis that the profile and extent of protein carbonylation are influenced by iron homeostasis in vivo. For this, we compared the profile and the contents of the carbonylated proteins in the <i>Arabidopsis thaliana</i> wild-type and mutant-deficient in three ferritin genes under normal and stress conditions. Additionally, we examined the proteins specifically carbonylated in wild-type seedlings exposed to iron-deficient conditions. Our results indicated that proteins were differentially carbonylated between the wild type and the triple ferritin mutant <i>Fer1-3-4</i> in the leaves, stems, and flowers under normal growth conditions. The profile of the carbonylated proteins was also different between the wild type and the ferritin triple mutant exposed to heat stress, thus pointing to the influence of iron on the carbonylation of proteins. Consistent with this, the exposure of the seedlings to iron deficiency and iron excess greatly influenced the carbonylation of certain proteins involved in intracellular signal transduction, translation, and iron deficiency response. Overall, the study underlined the importance of iron homeostasis in the occurrence of protein carbonylation in vivo. |
| first_indexed | 2024-03-11T03:04:45Z |
| format | Article |
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| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-11T03:04:45Z |
| publishDate | 2023-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-831e127178494abaa5912ae98389f7932023-11-18T08:03:16ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-06-012411973210.3390/ijms24119732Iron Availability Influences Protein Carbonylation in <i>Arabidopsis thaliana</i> PlantsAdesola J. Tola0Tagnon D. Missihoun1Groupe de Recherche en Biologie Végétale (GRBV), Department of Chemistry, Biochemistry and Physics, Université du Québec à Trois-Rivières, 3351 Boul. des Forges, Trois-Rivières, QC G9A 5H7, CanadaGroupe de Recherche en Biologie Végétale (GRBV), Department of Chemistry, Biochemistry and Physics, Université du Québec à Trois-Rivières, 3351 Boul. des Forges, Trois-Rivières, QC G9A 5H7, CanadaProtein carbonylation is an irreversible form of post-translational modification triggered by reactive oxygen species in animal and plant cells. It occurs either through the metal-catalyzed oxidation of Lys, Arg, Pro, and Thr side chains or the addition of α, β-unsaturated aldehydes and ketones to the side chains of Cys, Lys, and His. Recent genetic studies concerning plants pointed to an implication of protein carbonylation in gene regulation through phytohormones. However, for protein carbonylation to stand out as a signal transduction mechanism, such as phosphorylation and ubiquitination, it must be controlled in time and space by a still unknown trigger. In this study, we tested the hypothesis that the profile and extent of protein carbonylation are influenced by iron homeostasis in vivo. For this, we compared the profile and the contents of the carbonylated proteins in the <i>Arabidopsis thaliana</i> wild-type and mutant-deficient in three ferritin genes under normal and stress conditions. Additionally, we examined the proteins specifically carbonylated in wild-type seedlings exposed to iron-deficient conditions. Our results indicated that proteins were differentially carbonylated between the wild type and the triple ferritin mutant <i>Fer1-3-4</i> in the leaves, stems, and flowers under normal growth conditions. The profile of the carbonylated proteins was also different between the wild type and the ferritin triple mutant exposed to heat stress, thus pointing to the influence of iron on the carbonylation of proteins. Consistent with this, the exposure of the seedlings to iron deficiency and iron excess greatly influenced the carbonylation of certain proteins involved in intracellular signal transduction, translation, and iron deficiency response. Overall, the study underlined the importance of iron homeostasis in the occurrence of protein carbonylation in vivo.https://www.mdpi.com/1422-0067/24/11/9732carbonylated proteinsferritiniron deficiencyexcess ironmetal-catalyzed oxidationα, β-unsaturated aldehydes |
| spellingShingle | Adesola J. Tola Tagnon D. Missihoun Iron Availability Influences Protein Carbonylation in <i>Arabidopsis thaliana</i> Plants International Journal of Molecular Sciences carbonylated proteins ferritin iron deficiency excess iron metal-catalyzed oxidation α, β-unsaturated aldehydes |
| title | Iron Availability Influences Protein Carbonylation in <i>Arabidopsis thaliana</i> Plants |
| title_full | Iron Availability Influences Protein Carbonylation in <i>Arabidopsis thaliana</i> Plants |
| title_fullStr | Iron Availability Influences Protein Carbonylation in <i>Arabidopsis thaliana</i> Plants |
| title_full_unstemmed | Iron Availability Influences Protein Carbonylation in <i>Arabidopsis thaliana</i> Plants |
| title_short | Iron Availability Influences Protein Carbonylation in <i>Arabidopsis thaliana</i> Plants |
| title_sort | iron availability influences protein carbonylation in i arabidopsis thaliana i plants |
| topic | carbonylated proteins ferritin iron deficiency excess iron metal-catalyzed oxidation α, β-unsaturated aldehydes |
| url | https://www.mdpi.com/1422-0067/24/11/9732 |
| work_keys_str_mv | AT adesolajtola ironavailabilityinfluencesproteincarbonylationiniarabidopsisthalianaiplants AT tagnondmissihoun ironavailabilityinfluencesproteincarbonylationiniarabidopsisthalianaiplants |