Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome
Elongation factor 4 (EF4) is a member of the family of ribosome-dependent translational GTPase factors, along with elongation factor G and BPI-inducible protein A. Although EF4 is highly conserved in bacterial, mitochondrial, and chloroplast genomes, its exact biological function remains controversi...
| Main Authors: | , , , , , , |
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| Format: | Journal Article |
| Language: | English |
| Published: |
2017
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| Online Access: | https://hdl.handle.net/10356/81842 http://hdl.handle.net/10220/43494 |
| _version_ | 1811681570603401216 |
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| author | Kumar, Veerendra Ero, Rya Ahmed, Tofayel Goh, Kwok Jian Zhan, Yin Bhushan, Shashi Gao, Yong-Gui |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Kumar, Veerendra Ero, Rya Ahmed, Tofayel Goh, Kwok Jian Zhan, Yin Bhushan, Shashi Gao, Yong-Gui |
| author_sort | Kumar, Veerendra |
| collection | NTU |
| description | Elongation factor 4 (EF4) is a member of the family of ribosome-dependent translational GTPase factors, along with elongation factor G and BPI-inducible protein A. Although EF4 is highly conserved in bacterial, mitochondrial, and chloroplast genomes, its exact biological function remains controversial. Here we present the cryo-EM reconstitution of the GTP form of EF4 bound to the ribosome with P and E site tRNAs at 3.8-Å resolution. Interestingly, our structure reveals an unrotated ribosome rather than a clockwise-rotated ribosome, as observed in the presence of EF4-GDP and P site tRNA. In addition, we also observed a counterclockwise-rotated form of the above complex at 5.7-Å resolution. Taken together, our results shed light on the interactions formed between EF4, the ribosome, and the P site tRNA and illuminate the GTPase activation mechanism at previously unresolved detail. |
| first_indexed | 2024-10-01T03:43:03Z |
| format | Journal Article |
| id | ntu-10356/81842 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T03:43:03Z |
| publishDate | 2017 |
| record_format | dspace |
| spelling | ntu-10356/818422023-02-28T16:58:29Z Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome Kumar, Veerendra Ero, Rya Ahmed, Tofayel Goh, Kwok Jian Zhan, Yin Bhushan, Shashi Gao, Yong-Gui School of Biological Sciences Institute of Structural Biology Cryo-EM Ribosome structure Elongation factor 4 (EF4) is a member of the family of ribosome-dependent translational GTPase factors, along with elongation factor G and BPI-inducible protein A. Although EF4 is highly conserved in bacterial, mitochondrial, and chloroplast genomes, its exact biological function remains controversial. Here we present the cryo-EM reconstitution of the GTP form of EF4 bound to the ribosome with P and E site tRNAs at 3.8-Å resolution. Interestingly, our structure reveals an unrotated ribosome rather than a clockwise-rotated ribosome, as observed in the presence of EF4-GDP and P site tRNA. In addition, we also observed a counterclockwise-rotated form of the above complex at 5.7-Å resolution. Taken together, our results shed light on the interactions formed between EF4, the ribosome, and the P site tRNA and illuminate the GTPase activation mechanism at previously unresolved detail. NRF (Natl Research Foundation, S’pore) MOE (Min. of Education, S’pore) Accepted version 2017-07-31T02:56:37Z 2019-12-06T14:41:21Z 2017-07-31T02:56:37Z 2019-12-06T14:41:21Z 2016 Journal Article Kumar, V., Ero, R., Ahmed, T., Goh, K. J., Zhan, Y., Bhushan, S., et al. (2016). Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome. The Journal of Biological Chemistry, 291(25), 12943-12950. 0021-9258 https://hdl.handle.net/10356/81842 http://hdl.handle.net/10220/43494 10.1074/jbc.M116.725945 27137929 en The Journal of Biological Chemistry © 2016 The American Society for Biochemistry and Molecular Biology (ASBMB). This is the author created version of a work that has been peer reviewed and accepted for publication by The Journal of Biological Chemistry, The American Society for Biochemistry and Molecular Biology. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1074/jbc.M116.725945]. 17 p. application/pdf |
| spellingShingle | Cryo-EM Ribosome structure Kumar, Veerendra Ero, Rya Ahmed, Tofayel Goh, Kwok Jian Zhan, Yin Bhushan, Shashi Gao, Yong-Gui Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome |
| title | Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome |
| title_full | Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome |
| title_fullStr | Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome |
| title_full_unstemmed | Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome |
| title_short | Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome |
| title_sort | structure of the gtp form of elongation factor 4 ef4 bound to the ribosome |
| topic | Cryo-EM Ribosome structure |
| url | https://hdl.handle.net/10356/81842 http://hdl.handle.net/10220/43494 |
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