دورية أكاديمية
Assessing the Role of Post-Translational Modifications of Mitochondrial RNA Polymerase
| العنوان: | Assessing the Role of Post-Translational Modifications of Mitochondrial RNA Polymerase |
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| المؤلفون: | Karlie R. Platz, Emma J. Rudisel, Katelynn V. Paluch, Taylor R. Laurin, Kristin E. Dittenhafer-Reed |
| المصدر: | International Journal of Molecular Sciences, Vol 24, Iss 22, p 16050 (2023) |
| بيانات النشر: | MDPI AG, 2023. |
| سنة النشر: | 2023 |
| المجموعة: | LCC:Biology (General) LCC:Chemistry |
| مصطلحات موضوعية: | post-translational protein modification, acetylation, phosphorylation, mitochondrial DNA, mitochondrial genome, mitochondrial proteins, Biology (General), QH301-705.5, Chemistry, QD1-999 |
| الوصف: | The mitochondrial proteome is subject to abundant post-translational modifications, including lysine acetylation and phosphorylation of serine, threonine, and tyrosine. The biological function of the majority of these protein modifications is unknown. Proteins required for the transcription and translation of mitochondrial DNA (mtDNA) are subject to modification. This suggests that reversible post-translational modifications may serve as a regulatory mechanism for mitochondrial gene transcription, akin to mechanisms controlling nuclear gene expression. We set out to determine whether acetylation or phosphorylation controls the function of mitochondrial RNA polymerase (POLRMT). Mass spectrometry was used to identify post-translational modifications on POLRMT. We analyzed three POLRMT modification sites (lysine 402, threonine 315, threonine 993) found in distinct structural regions. Amino acid point mutants that mimic the modified and unmodified forms of POLRMT were employed to measure the effect of acetylation or phosphorylation on the promoter binding ability of POLRMT in vitro. We found a slight decrease in binding affinity for the phosphomimic at threonine 315. We did not identify large changes in viability, mtDNA content, or mitochondrial transcript level upon overexpression of POLRMT modification mimics in HeLa cells. Our results suggest minimal biological impact of the POLRMT post-translational modifications studied in our system. |
| نوع الوثيقة: | article |
| وصف الملف: | electronic resource |
| اللغة: | English |
| تدمد: | 1422-0067 1661-6596 |
| Relation: | https://www.mdpi.com/1422-0067/24/22/16050; https://doaj.org/toc/1661-6596; https://doaj.org/toc/1422-0067 |
| DOI: | 10.3390/ijms242216050 |
| URL الوصول: | https://doaj.org/article/66ae531e8a03461c831bc5c7d1c1421d |
| رقم الأكسشن: | edsdoj.66ae531e8a03461c831bc5c7d1c1421d |
| قاعدة البيانات: | Directory of Open Access Journals |
Full Text Finder | تدمد: | 14220067 16616596 |
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| DOI: | 10.3390/ijms242216050 |