Identification of a 57S translation complex containing closed-loop factors and the 60S ribosome subunit
Abstract In eukaryotic translation the 60S ribosome subunit has not been proposed to interact with mRNA or closed-loop factors eIF4E, eIF4G, and PAB1. Using analytical ultracentrifugation with fluorescent detection system, we have identified a 57S translation complex that contains the 60S ribosome,...
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2018-07-01
|
| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-018-29832-6 |
| _version_ | 1824012313919750144 |
|---|---|
| author | Clyde L. Denis Thomas M. Laue Xin Wang |
| author_facet | Clyde L. Denis Thomas M. Laue Xin Wang |
| author_sort | Clyde L. Denis |
| collection | DOAJ |
| description | Abstract In eukaryotic translation the 60S ribosome subunit has not been proposed to interact with mRNA or closed-loop factors eIF4E, eIF4G, and PAB1. Using analytical ultracentrifugation with fluorescent detection system, we have identified a 57S translation complex that contains the 60S ribosome, mRNA, and the closed-loop factors. Previously published data by others also indicate the presence of a 50S-60S translation complex containing these same components. We have found that the abundance of this complex increased upon translational cessation, implying formation after ribosomal dissociation. Stoichiometric analyses of the abundances of the closed-loop components in the 57S complex indicate this complex is most similar to polysomal and monosomal translation complexes at the end of translation rather than at the beginning or middle of translation. In contrast, a 39S complex containing the 40S ribosome bound to mRNA and closed-loop factors was also identified with stoichiometries most similar to polysomal complexes engaged in translation, suggesting that the 39S complex is the previously studied 48S translation initiation complex. These results indicate that the 60S ribosome can associate with the closed-loop mRNA structure and plays a previously undetected role in the translation process. |
| first_indexed | 2024-12-18T21:47:10Z |
| format | Article |
| id | doaj.art-f913d2dae08f435f983fd4a9a50939cb |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-12-18T21:47:10Z |
| publishDate | 2018-07-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-f913d2dae08f435f983fd4a9a50939cb2022-12-21T20:50:39ZengNature PortfolioScientific Reports2045-23222018-07-018111210.1038/s41598-018-29832-6Identification of a 57S translation complex containing closed-loop factors and the 60S ribosome subunitClyde L. Denis0Thomas M. Laue1Xin Wang2Department of Molecular, Cellular, and Biomedical Sciences, University of New HampshireDepartment of Molecular, Cellular, and Biomedical Sciences, University of New HampshireDepartment of Molecular, Cellular, and Biomedical Sciences, University of New HampshireAbstract In eukaryotic translation the 60S ribosome subunit has not been proposed to interact with mRNA or closed-loop factors eIF4E, eIF4G, and PAB1. Using analytical ultracentrifugation with fluorescent detection system, we have identified a 57S translation complex that contains the 60S ribosome, mRNA, and the closed-loop factors. Previously published data by others also indicate the presence of a 50S-60S translation complex containing these same components. We have found that the abundance of this complex increased upon translational cessation, implying formation after ribosomal dissociation. Stoichiometric analyses of the abundances of the closed-loop components in the 57S complex indicate this complex is most similar to polysomal and monosomal translation complexes at the end of translation rather than at the beginning or middle of translation. In contrast, a 39S complex containing the 40S ribosome bound to mRNA and closed-loop factors was also identified with stoichiometries most similar to polysomal complexes engaged in translation, suggesting that the 39S complex is the previously studied 48S translation initiation complex. These results indicate that the 60S ribosome can associate with the closed-loop mRNA structure and plays a previously undetected role in the translation process.https://doi.org/10.1038/s41598-018-29832-6 |
| spellingShingle | Clyde L. Denis Thomas M. Laue Xin Wang Identification of a 57S translation complex containing closed-loop factors and the 60S ribosome subunit Scientific Reports |
| title | Identification of a 57S translation complex containing closed-loop factors and the 60S ribosome subunit |
| title_full | Identification of a 57S translation complex containing closed-loop factors and the 60S ribosome subunit |
| title_fullStr | Identification of a 57S translation complex containing closed-loop factors and the 60S ribosome subunit |
| title_full_unstemmed | Identification of a 57S translation complex containing closed-loop factors and the 60S ribosome subunit |
| title_short | Identification of a 57S translation complex containing closed-loop factors and the 60S ribosome subunit |
| title_sort | identification of a 57s translation complex containing closed loop factors and the 60s ribosome subunit |
| url | https://doi.org/10.1038/s41598-018-29832-6 |
| work_keys_str_mv | AT clydeldenis identificationofa57stranslationcomplexcontainingclosedloopfactorsandthe60sribosomesubunit AT thomasmlaue identificationofa57stranslationcomplexcontainingclosedloopfactorsandthe60sribosomesubunit AT xinwang identificationofa57stranslationcomplexcontainingclosedloopfactorsandthe60sribosomesubunit |