The Insertion Domain of Mti2 Facilitates the Association of Mitochondrial Initiation Factors with Mitoribosomes in <i>Schizosaccharomyces pombe</i>
Translation initiation in mitochondria involves unique mechanisms distinct from those in the cytosol or in bacteria. The <i>Schizosaccharomyces pombe</i> mitochondrial translation initiation factor 2 (Mti2) is the ortholog of human MTIF2, which plays a vital role in synthesizing proteins...
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MDPI AG
2025-05-01
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| author | Ying Luo Jürg Bähler Ying Huang |
| author_facet | Ying Luo Jürg Bähler Ying Huang |
| author_sort | Ying Luo |
| collection | DOAJ |
| description | Translation initiation in mitochondria involves unique mechanisms distinct from those in the cytosol or in bacteria. The <i>Schizosaccharomyces pombe</i> mitochondrial translation initiation factor 2 (Mti2) is the ortholog of human MTIF2, which plays a vital role in synthesizing proteins in mitochondria. Here, we investigate the insertion domain of Mti2, which stabilizes its interaction with the ribosome and is crucial for efficient translation initiation. Our results show that the insertion domain is critical for the proper folding and function of Mti2. The absence of the insertion domain disrupts cell growth and affects the expression of genes encoded by mitochondrial DNA. Additionally, we show that Mti2 physically interacts with the small subunits of mitoribosomes (mtSSU), and deletion of the insertion domain dissociates mitochondrial initiation factors from the mitoribosome, reducing the efficiency of mitochondrial translation. Altogether, these findings highlight the conserved role of the insertion domain in facilitating translation initiation in fission yeast and thus reveal shared principles of mitochondrial translation initiation in both fission yeast and humans. |
| format | Article |
| id | doaj-art-90acccb00ebb4e27a5f20cdbc5e2e6be |
| institution | OA Journals |
| issn | 2218-273X |
| language | English |
| publishDate | 2025-05-01 |
| publisher | MDPI AG |
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| series | Biomolecules |
| spelling | doaj-art-90acccb00ebb4e27a5f20cdbc5e2e6be2025-08-20T01:56:14ZengMDPI AGBiomolecules2218-273X2025-05-0115569510.3390/biom15050695The Insertion Domain of Mti2 Facilitates the Association of Mitochondrial Initiation Factors with Mitoribosomes in <i>Schizosaccharomyces pombe</i>Ying Luo0Jürg Bähler1Ying Huang2Jiangsu Key Laboratory for Microbes and Genomics, School of Life Sciences, Nanjing Normal University, 1 Wenyuan Road, Nanjing 210023, ChinaInstitute of Healthy Ageing, Department of Genetics, Evolution & Environment, University College London, London WC1E 6BT, UKJiangsu Key Laboratory for Microbes and Genomics, School of Life Sciences, Nanjing Normal University, 1 Wenyuan Road, Nanjing 210023, ChinaTranslation initiation in mitochondria involves unique mechanisms distinct from those in the cytosol or in bacteria. The <i>Schizosaccharomyces pombe</i> mitochondrial translation initiation factor 2 (Mti2) is the ortholog of human MTIF2, which plays a vital role in synthesizing proteins in mitochondria. Here, we investigate the insertion domain of Mti2, which stabilizes its interaction with the ribosome and is crucial for efficient translation initiation. Our results show that the insertion domain is critical for the proper folding and function of Mti2. The absence of the insertion domain disrupts cell growth and affects the expression of genes encoded by mitochondrial DNA. Additionally, we show that Mti2 physically interacts with the small subunits of mitoribosomes (mtSSU), and deletion of the insertion domain dissociates mitochondrial initiation factors from the mitoribosome, reducing the efficiency of mitochondrial translation. Altogether, these findings highlight the conserved role of the insertion domain in facilitating translation initiation in fission yeast and thus reveal shared principles of mitochondrial translation initiation in both fission yeast and humans.https://www.mdpi.com/2218-273X/15/5/695fission yeastmitochondrial translationtranslation initiation factorinsertion domain |
| spellingShingle | Ying Luo Jürg Bähler Ying Huang The Insertion Domain of Mti2 Facilitates the Association of Mitochondrial Initiation Factors with Mitoribosomes in <i>Schizosaccharomyces pombe</i> Biomolecules fission yeast mitochondrial translation translation initiation factor insertion domain |
| title | The Insertion Domain of Mti2 Facilitates the Association of Mitochondrial Initiation Factors with Mitoribosomes in <i>Schizosaccharomyces pombe</i> |
| title_full | The Insertion Domain of Mti2 Facilitates the Association of Mitochondrial Initiation Factors with Mitoribosomes in <i>Schizosaccharomyces pombe</i> |
| title_fullStr | The Insertion Domain of Mti2 Facilitates the Association of Mitochondrial Initiation Factors with Mitoribosomes in <i>Schizosaccharomyces pombe</i> |
| title_full_unstemmed | The Insertion Domain of Mti2 Facilitates the Association of Mitochondrial Initiation Factors with Mitoribosomes in <i>Schizosaccharomyces pombe</i> |
| title_short | The Insertion Domain of Mti2 Facilitates the Association of Mitochondrial Initiation Factors with Mitoribosomes in <i>Schizosaccharomyces pombe</i> |
| title_sort | insertion domain of mti2 facilitates the association of mitochondrial initiation factors with mitoribosomes in i schizosaccharomyces pombe i |
| topic | fission yeast mitochondrial translation translation initiation factor insertion domain |
| url | https://www.mdpi.com/2218-273X/15/5/695 |
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