Schaik, J.J.M van (2021) Identifying acetylation status-related interaction partners of C/EBPα in relation to mitochondrial function. Master's Research Project 1, Biomedical Sciences.
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Abstract
One of the transcription factors that regulates transcription these mitochondrial genes is CCAAT/enhancer-binding protein alpha. C/EBPα is deacetylated into its active form by sirtuin1 when nutrients are scarce, allowing it to induce transcription of mitochondrial genes. In times of abundance, C/EBPα is acetylated by p300, reducing transcription of the same mitochondrial genes. This study aimed to address whether the C/EBPα-acetylation status alters the binding to other proteins that may be involved in a transcription. Flp-In T-REx-293 cells were used to express C/EBPα in its wild-type-, hyperacetylated-, and hypoacetylated- form in order to identify interaction partners through co-Ip. Immunoblot analysis revealed C/EBPβ liver-enriched transcriptional inhibitory protein (LIP) to specifically bind to the hyperacetylated form of C/EBPα, possibly pointing to a role of LIP in preventing the activation of C/EBPα. This finding is preliminary and requires further investigation. This study also addressed the relation between C/EBPα acetylation status and mitochondrial function. Oxygen consumption rate was determined but the data from these experiments lack consistency and statistical strength. Overall, this study did not identify potential acetylation status-related interaction-partners of C/EBPα. C/EBPβ (LIP) was found to interact with the hyperacetylation-mimicking C/EBPα- mutant, potentially playing a role in preventing C/EBPα from inducing transcription of mitochondrial genes.
| Item Type: | Thesis (Master's Research Project 1) |
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| Supervisor name: | Calkhoven, C.F. and Hartung, J. |
| Degree programme: | Biomedical Sciences |
| Thesis type: | Master's Research Project 1 |
| Language: | English |
| Date Deposited: | 09 Jul 2021 13:20 |
| Last Modified: | 09 Jul 2021 13:20 |
| URI: | https://fse.studenttheses.ub.rug.nl/id/eprint/25090 |
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