A truncated variant of the ribosome-associated trigger factor specifically contributes to plant chloroplast ribosome biogenesis
Abstract Molecular chaperones are essential throughout a protein’s life and act already during protein synthesis. Bacteria and chloroplasts of plant cells share the ribosome-associated chaperone trigger factor (Tig1 in plastids), facilitating maturation of emerging nascent polypeptides. While typica...
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Nature Portfolio
2025-01-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-025-55813-1 |
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| author | Fabian Ries Jasmin Gorlt Sabrina Kaiser Vanessa Scherer Charlotte Seydel Sandra Nguyen Andreas Klingl Julia Legen Christian Schmitz-Linneweber Hinrik Plaggenborg Jediael Z. Y. Ng Dennis Wiens Georg K. A. Hochberg Markus Räschle Torsten Möhlmann David Scheuring Felix Willmund |
| author_facet | Fabian Ries Jasmin Gorlt Sabrina Kaiser Vanessa Scherer Charlotte Seydel Sandra Nguyen Andreas Klingl Julia Legen Christian Schmitz-Linneweber Hinrik Plaggenborg Jediael Z. Y. Ng Dennis Wiens Georg K. A. Hochberg Markus Räschle Torsten Möhlmann David Scheuring Felix Willmund |
| author_sort | Fabian Ries |
| collection | DOAJ |
| description | Abstract Molecular chaperones are essential throughout a protein’s life and act already during protein synthesis. Bacteria and chloroplasts of plant cells share the ribosome-associated chaperone trigger factor (Tig1 in plastids), facilitating maturation of emerging nascent polypeptides. While typical trigger factor chaperones employ three domains for their task, the here described truncated form, Tig2, contains just the ribosome binding domain. Tig2 is widely present in green plants and appears to have acquired an entirely different task than co-translational nascent polypeptide folding. Tig2 deletion results in remarkable leaf developmental defects of cold-exposed Arabidopsis thaliana plants and specific defects in plastidic ribosomes. Our data indicate that Tig2 functions during ribosome biogenesis by promoting the maturation of the large subunit. We hypothesize that Tig2 binding to the ribosomal tunnel-exit surface aids protecting this sensitive surface during assembly. Tig2 illustrates a fascinating concept of how a chaperone domain evolved individually, serving a completely different molecular task. |
| format | Article |
| id | doaj-art-a831b202a3224327b19a1d142103f640 |
| institution | Kabale University |
| issn | 2041-1723 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj-art-a831b202a3224327b19a1d142103f6402025-01-19T12:30:25ZengNature PortfolioNature Communications2041-17232025-01-0116111610.1038/s41467-025-55813-1A truncated variant of the ribosome-associated trigger factor specifically contributes to plant chloroplast ribosome biogenesisFabian Ries0Jasmin Gorlt1Sabrina Kaiser2Vanessa Scherer3Charlotte Seydel4Sandra Nguyen5Andreas Klingl6Julia Legen7Christian Schmitz-Linneweber8Hinrik Plaggenborg9Jediael Z. Y. Ng10Dennis Wiens11Georg K. A. Hochberg12Markus Räschle13Torsten Möhlmann14David Scheuring15Felix Willmund16Molecular Genetics of Eukaryotes, University of KaiserslauternMolecular Genetics of Eukaryotes, University of KaiserslauternPlant Pathology, University of KaiserslauternPlant Physiology, University of KaiserslauternPlant Development, Ludwig-Maximilians-University MunichMolecular Genetics of Eukaryotes, University of KaiserslauternPlant Development, Ludwig-Maximilians-University MunichMolecular Genetics, Humboldt-University of BerlinMolecular Genetics, Humboldt-University of BerlinMolecular Plant Sciences & Synmikro, University of MarburgMax-Planck-Institute for Terrestrial MicrobiologyMax-Planck-Institute for Terrestrial MicrobiologyMax-Planck-Institute for Terrestrial MicrobiologyMolecular Genetics, University of KaiserslauternPlant Physiology, University of KaiserslauternPlant Pathology, University of KaiserslauternMolecular Genetics of Eukaryotes, University of KaiserslauternAbstract Molecular chaperones are essential throughout a protein’s life and act already during protein synthesis. Bacteria and chloroplasts of plant cells share the ribosome-associated chaperone trigger factor (Tig1 in plastids), facilitating maturation of emerging nascent polypeptides. While typical trigger factor chaperones employ three domains for their task, the here described truncated form, Tig2, contains just the ribosome binding domain. Tig2 is widely present in green plants and appears to have acquired an entirely different task than co-translational nascent polypeptide folding. Tig2 deletion results in remarkable leaf developmental defects of cold-exposed Arabidopsis thaliana plants and specific defects in plastidic ribosomes. Our data indicate that Tig2 functions during ribosome biogenesis by promoting the maturation of the large subunit. We hypothesize that Tig2 binding to the ribosomal tunnel-exit surface aids protecting this sensitive surface during assembly. Tig2 illustrates a fascinating concept of how a chaperone domain evolved individually, serving a completely different molecular task.https://doi.org/10.1038/s41467-025-55813-1 |
| spellingShingle | Fabian Ries Jasmin Gorlt Sabrina Kaiser Vanessa Scherer Charlotte Seydel Sandra Nguyen Andreas Klingl Julia Legen Christian Schmitz-Linneweber Hinrik Plaggenborg Jediael Z. Y. Ng Dennis Wiens Georg K. A. Hochberg Markus Räschle Torsten Möhlmann David Scheuring Felix Willmund A truncated variant of the ribosome-associated trigger factor specifically contributes to plant chloroplast ribosome biogenesis Nature Communications |
| title | A truncated variant of the ribosome-associated trigger factor specifically contributes to plant chloroplast ribosome biogenesis |
| title_full | A truncated variant of the ribosome-associated trigger factor specifically contributes to plant chloroplast ribosome biogenesis |
| title_fullStr | A truncated variant of the ribosome-associated trigger factor specifically contributes to plant chloroplast ribosome biogenesis |
| title_full_unstemmed | A truncated variant of the ribosome-associated trigger factor specifically contributes to plant chloroplast ribosome biogenesis |
| title_short | A truncated variant of the ribosome-associated trigger factor specifically contributes to plant chloroplast ribosome biogenesis |
| title_sort | truncated variant of the ribosome associated trigger factor specifically contributes to plant chloroplast ribosome biogenesis |
| url | https://doi.org/10.1038/s41467-025-55813-1 |
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