Histone H3 N-terminal tail provides tolerance to tartrazine induced stress in Saccharomyces cerevisiae
Tartrazine (TZN) is used in a wide variety of foods, medicines and cosmetics. Studies have associated TZN exposure with several side effects such as asthma, nausea, bronchitis, rhinitis, bronchospasm, etc. in humans. However, the mode of action of this molecule is not properly understood. In this st...
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Veröffentlicht in: | Biológia 2024-06, Vol.79 (6), p.1975-1981 |
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container_end_page | 1981 |
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container_issue | 6 |
container_start_page | 1975 |
container_title | Biológia |
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creator | Anand, Smriti Kumar, Sushant Kumari, Khushboo Azad, Gajendra Kumar |
description | Tartrazine (TZN) is used in a wide variety of foods, medicines and cosmetics. Studies have associated TZN exposure with several side effects such as asthma, nausea, bronchitis, rhinitis, bronchospasm, etc. in humans. However, the mode of action of this molecule is not properly understood. In this study, we used budding yeast to decipher the mechanism of TZN toxicity. Our data revealed that the deletion of H3 N-terminal tail H3-Δ(1–16), H3-Δ(1–20), H3-Δ(1–24), H3-Δ(1–28) lead to hypersensitivity for TZN indicating that the tail region mediates intracellular signaling for survivability upon TZN exposure. Next, we performed computational study to characterize TZN-interactome by STITCH tool. Our analysis revealed that TZN have only two interacting partner (CTT1 and CTA1) and both of them are involved in oxidative stress pathways. This data was validated by the rescue of TZN toxicity by supplementation of antioxidant. Altogether, our data indicate that TZN causes oxidative stress in budding yeast cells and the intracellular response to alleviate such stress requires N-terminal tail of histone H3. |
doi_str_mv | 10.1007/s11756-024-01653-1 |
format | Article |
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Studies have associated TZN exposure with several side effects such as asthma, nausea, bronchitis, rhinitis, bronchospasm, etc. in humans. However, the mode of action of this molecule is not properly understood. In this study, we used budding yeast to decipher the mechanism of TZN toxicity. Our data revealed that the deletion of H3 N-terminal tail H3-Δ(1–16), H3-Δ(1–20), H3-Δ(1–24), H3-Δ(1–28) lead to hypersensitivity for TZN indicating that the tail region mediates intracellular signaling for survivability upon TZN exposure. Next, we performed computational study to characterize TZN-interactome by STITCH tool. Our analysis revealed that TZN have only two interacting partner (CTT1 and CTA1) and both of them are involved in oxidative stress pathways. This data was validated by the rescue of TZN toxicity by supplementation of antioxidant. 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Studies have associated TZN exposure with several side effects such as asthma, nausea, bronchitis, rhinitis, bronchospasm, etc. in humans. However, the mode of action of this molecule is not properly understood. In this study, we used budding yeast to decipher the mechanism of TZN toxicity. Our data revealed that the deletion of H3 N-terminal tail H3-Δ(1–16), H3-Δ(1–20), H3-Δ(1–24), H3-Δ(1–28) lead to hypersensitivity for TZN indicating that the tail region mediates intracellular signaling for survivability upon TZN exposure. Next, we performed computational study to characterize TZN-interactome by STITCH tool. Our analysis revealed that TZN have only two interacting partner (CTT1 and CTA1) and both of them are involved in oxidative stress pathways. This data was validated by the rescue of TZN toxicity by supplementation of antioxidant. 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Studies have associated TZN exposure with several side effects such as asthma, nausea, bronchitis, rhinitis, bronchospasm, etc. in humans. However, the mode of action of this molecule is not properly understood. In this study, we used budding yeast to decipher the mechanism of TZN toxicity. Our data revealed that the deletion of H3 N-terminal tail H3-Δ(1–16), H3-Δ(1–20), H3-Δ(1–24), H3-Δ(1–28) lead to hypersensitivity for TZN indicating that the tail region mediates intracellular signaling for survivability upon TZN exposure. Next, we performed computational study to characterize TZN-interactome by STITCH tool. Our analysis revealed that TZN have only two interacting partner (CTT1 and CTA1) and both of them are involved in oxidative stress pathways. This data was validated by the rescue of TZN toxicity by supplementation of antioxidant. 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subjects | Biomedical and Life Sciences Bronchitis Bronchospasm Cell Biology Cosmetics Histone H3 Histones Hypersensitivity Intracellular Intracellular signalling Life Sciences Microbiology Mode of action Oxidative stress Plant Sciences Rhinitis Short Communication Side effects Survivability Tartrazine Toxicity Yeast Yeasts Zoology |
title | Histone H3 N-terminal tail provides tolerance to tartrazine induced stress in Saccharomyces cerevisiae |
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