Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation
Translational frameshifting is a mechanism that expands the coding capabilities of mRNA. Here, structures of 70S ribosome complexes with GTPase elongation factor G (EF-G), a +1-frameshifting-prone mRNA and tRNAs reveal the cooperation between the ribosome and EF-G to induce +1 frameshifting during t...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2021-07-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-021-24911-1 |
| _version_ | 1818997188575887360 |
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| author | Gabriel Demo Howard B. Gamper Anna B. Loveland Isao Masuda Christine E. Carbone Egor Svidritskiy Ya-Ming Hou Andrei A. Korostelev |
| author_facet | Gabriel Demo Howard B. Gamper Anna B. Loveland Isao Masuda Christine E. Carbone Egor Svidritskiy Ya-Ming Hou Andrei A. Korostelev |
| author_sort | Gabriel Demo |
| collection | DOAJ |
| description | Translational frameshifting is a mechanism that expands the coding capabilities of mRNA. Here, structures of 70S ribosome complexes with GTPase elongation factor G (EF-G), a +1-frameshifting-prone mRNA and tRNAs reveal the cooperation between the ribosome and EF-G to induce +1 frameshifting during the translocation step. |
| first_indexed | 2024-12-20T21:41:40Z |
| format | Article |
| id | doaj.art-9e96fbbefbf946cca2e64e5aa10017b3 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-20T21:41:40Z |
| publishDate | 2021-07-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-9e96fbbefbf946cca2e64e5aa10017b32022-12-21T19:25:48ZengNature PortfolioNature Communications2041-17232021-07-0112111210.1038/s41467-021-24911-1Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocationGabriel Demo0Howard B. Gamper1Anna B. Loveland2Isao Masuda3Christine E. Carbone4Egor Svidritskiy5Ya-Ming Hou6Andrei A. Korostelev7RNA Therapeutics Institute, Department of Biochemistry and Molecular Pharmacology, UMass Medical SchoolDepartment of Biochemistry and Molecular Biology, Thomas Jefferson UniversityRNA Therapeutics Institute, Department of Biochemistry and Molecular Pharmacology, UMass Medical SchoolDepartment of Biochemistry and Molecular Biology, Thomas Jefferson UniversityRNA Therapeutics Institute, Department of Biochemistry and Molecular Pharmacology, UMass Medical SchoolRNA Therapeutics Institute, Department of Biochemistry and Molecular Pharmacology, UMass Medical SchoolDepartment of Biochemistry and Molecular Biology, Thomas Jefferson UniversityRNA Therapeutics Institute, Department of Biochemistry and Molecular Pharmacology, UMass Medical SchoolTranslational frameshifting is a mechanism that expands the coding capabilities of mRNA. Here, structures of 70S ribosome complexes with GTPase elongation factor G (EF-G), a +1-frameshifting-prone mRNA and tRNAs reveal the cooperation between the ribosome and EF-G to induce +1 frameshifting during the translocation step.https://doi.org/10.1038/s41467-021-24911-1 |
| spellingShingle | Gabriel Demo Howard B. Gamper Anna B. Loveland Isao Masuda Christine E. Carbone Egor Svidritskiy Ya-Ming Hou Andrei A. Korostelev Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation Nature Communications |
| title | Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation |
| title_full | Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation |
| title_fullStr | Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation |
| title_full_unstemmed | Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation |
| title_short | Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation |
| title_sort | structural basis for 1 ribosomal frameshifting during ef g catalyzed translocation |
| url | https://doi.org/10.1038/s41467-021-24911-1 |
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