EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequences
Abstract Polyproline sequences are deleterious to cells because they stall ribosomes. In bacteria, EF-P plays an important role in overcoming such polyproline sequence-induced ribosome stalling. Additionally, numerous bacteria possess an EF-P paralog called EfpL (also known as YeiP) of unknown funct...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2024-12-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-024-54556-9 |
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| author | Alina Sieber Marina Parr Julian von Ehr Karthikeyan Dhamotharan Pavel Kielkowski Tess Brewer Anna Schäpers Ralph Krafczyk Fei Qi Andreas Schlundt Dmitrij Frishman Jürgen Lassak |
| author_facet | Alina Sieber Marina Parr Julian von Ehr Karthikeyan Dhamotharan Pavel Kielkowski Tess Brewer Anna Schäpers Ralph Krafczyk Fei Qi Andreas Schlundt Dmitrij Frishman Jürgen Lassak |
| author_sort | Alina Sieber |
| collection | DOAJ |
| description | Abstract Polyproline sequences are deleterious to cells because they stall ribosomes. In bacteria, EF-P plays an important role in overcoming such polyproline sequence-induced ribosome stalling. Additionally, numerous bacteria possess an EF-P paralog called EfpL (also known as YeiP) of unknown function. Here, we functionally and structurally characterize EfpL from Escherichia coli and demonstrate its role in the translational stress response. Through ribosome profiling, we analyze the EfpL arrest motif spectrum and find additional sequences beyond the canonical polyproline motifs that both EF-P and EfpL can resolve. Notably, the two factors can also induce pauses. We further report that EfpL can sense the metabolic state of the cell via lysine acylation. Overall, our work characterizes the role of EfpL in ribosome rescue at proline-containing sequences, and provides evidence that co-occurrence of EF-P and EfpL is an evolutionary driver for higher bacterial growth rates. |
| format | Article |
| id | doaj-art-2fbdff9fdc5643b6bfb2161f50fa26ba |
| institution | Kabale University |
| issn | 2041-1723 |
| language | English |
| publishDate | 2024-12-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj-art-2fbdff9fdc5643b6bfb2161f50fa26ba2024-12-08T12:35:45ZengNature PortfolioNature Communications2041-17232024-12-0115111610.1038/s41467-024-54556-9EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequencesAlina Sieber0Marina Parr1Julian von Ehr2Karthikeyan Dhamotharan3Pavel Kielkowski4Tess Brewer5Anna Schäpers6Ralph Krafczyk7Fei Qi8Andreas Schlundt9Dmitrij Frishman10Jürgen Lassak11Faculty of Biology, Microbiology, Ludwig-Maximilians-Universität MünchenDepartment of Bioinformatics, Wissenschaftszentrum Weihenstephan, Technische Universität MünchenInstitute for Molecular Biosciences and Biomolecular Resonance Center (BMRZ), Goethe University FrankfurtInstitute for Molecular Biosciences and Biomolecular Resonance Center (BMRZ), Goethe University FrankfurtDepartment of Chemistry, Institut für Chemische Epigenetik (ICEM), Ludwig-Maximilians-Universität MünchenFaculty of Biology, Microbiology, Ludwig-Maximilians-Universität MünchenFaculty of Biology, Microbiology, Ludwig-Maximilians-Universität MünchenFaculty of Biology, Microbiology, Ludwig-Maximilians-Universität MünchenState Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen UniversityInstitute for Molecular Biosciences and Biomolecular Resonance Center (BMRZ), Goethe University FrankfurtDepartment of Bioinformatics, Wissenschaftszentrum Weihenstephan, Technische Universität MünchenFaculty of Biology, Microbiology, Ludwig-Maximilians-Universität MünchenAbstract Polyproline sequences are deleterious to cells because they stall ribosomes. In bacteria, EF-P plays an important role in overcoming such polyproline sequence-induced ribosome stalling. Additionally, numerous bacteria possess an EF-P paralog called EfpL (also known as YeiP) of unknown function. Here, we functionally and structurally characterize EfpL from Escherichia coli and demonstrate its role in the translational stress response. Through ribosome profiling, we analyze the EfpL arrest motif spectrum and find additional sequences beyond the canonical polyproline motifs that both EF-P and EfpL can resolve. Notably, the two factors can also induce pauses. We further report that EfpL can sense the metabolic state of the cell via lysine acylation. Overall, our work characterizes the role of EfpL in ribosome rescue at proline-containing sequences, and provides evidence that co-occurrence of EF-P and EfpL is an evolutionary driver for higher bacterial growth rates.https://doi.org/10.1038/s41467-024-54556-9 |
| spellingShingle | Alina Sieber Marina Parr Julian von Ehr Karthikeyan Dhamotharan Pavel Kielkowski Tess Brewer Anna Schäpers Ralph Krafczyk Fei Qi Andreas Schlundt Dmitrij Frishman Jürgen Lassak EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequences Nature Communications |
| title | EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequences |
| title_full | EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequences |
| title_fullStr | EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequences |
| title_full_unstemmed | EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequences |
| title_short | EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequences |
| title_sort | ef p and its paralog efpl yeip differentially control translation of proline containing sequences |
| url | https://doi.org/10.1038/s41467-024-54556-9 |
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