A truncated variant of the ribosome-associated trigger factor specifically contributes to plant chloroplast ribosome biogenesis

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 and Felix Willmund ()
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Fabian Ries: Molecular Genetics of Eukaryotes, University of Kaiserslautern
Jasmin Gorlt: Molecular Genetics of Eukaryotes, University of Kaiserslautern
Sabrina Kaiser: Plant Pathology, University of Kaiserslautern
Vanessa Scherer: Plant Physiology, University of Kaiserslautern
Charlotte Seydel: Plant Development, Ludwig-Maximilians-University Munich
Sandra Nguyen: Molecular Genetics of Eukaryotes, University of Kaiserslautern
Andreas Klingl: Plant Development, Ludwig-Maximilians-University Munich
Julia Legen: Molecular Genetics, Humboldt-University of Berlin
Christian Schmitz-Linneweber: Molecular Genetics, Humboldt-University of Berlin
Hinrik Plaggenborg: Molecular Plant Sciences & Synmikro, University of Marburg
Jediael Z. Y. Ng: Max-Planck-Institute for Terrestrial Microbiology
Dennis Wiens: Max-Planck-Institute for Terrestrial Microbiology
Georg K. A. Hochberg: Max-Planck-Institute for Terrestrial Microbiology
Markus Räschle: Molecular Genetics, University of Kaiserslautern
Torsten Möhlmann: Plant Physiology, University of Kaiserslautern
David Scheuring: Plant Pathology, University of Kaiserslautern
Felix Willmund: Molecular Genetics of Eukaryotes, University of Kaiserslautern

Nature Communications, 2025, vol. 16, issue 1, 1-16

Abstract: 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.

Date: 2025
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DOI: 10.1038/s41467-025-55813-1

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