GTPases and the origin of the ribosome
Background This paper is an attempt to trace the evolution of the ribosome through the evolution of the universal P-loop GTPases that are involved with the ribosome in translation and with the attachment of the ribosome to the membrane. The GTPases involved in translation in Bacteria/Archaea are...
| Main Authors: | , |
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| Other Authors: | |
| Format: | Article |
| Language: | en_US |
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Springer (Biomed Central Ltd.)
2012
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| Online Access: | http://hdl.handle.net/1721.1/69628 https://orcid.org/0000-0002-1765-7530 |
| _version_ | 1811090771071205376 |
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| author | Smith, Temple F. Hartman, Hyman |
| author2 | Massachusetts Institute of Technology. Center for Biomedical Engineering |
| author_facet | Massachusetts Institute of Technology. Center for Biomedical Engineering Smith, Temple F. Hartman, Hyman |
| author_sort | Smith, Temple F. |
| collection | MIT |
| description | Background
This paper is an attempt to trace the evolution of the ribosome through the evolution of the universal P-loop GTPases that are involved with the ribosome in translation and with the attachment of the ribosome to the membrane. The GTPases involved in translation in Bacteria/Archaea are the elongation factors EFTu/EF1, the initiation factors IF2/aeIF5b + aeIF2, and the elongation factors EFG/EF2. All of these GTPases also contain the OB fold also found in the non GTPase IF1 involved in initiation. The GTPase involved in the signal recognition particle in most Bacteria and Archaea is SRP54.
Results
1) The Elongation Factors of the Archaea based on structural considerations of the domains have the following evolutionary path: EF1→ aeIF2 → EF2. The evolution of the aeIF5b was a later event; 2) the Elongation Factors of the Bacteria based on the topological considerations of the GTPase domain have a similar evolutionary path: EFTu→ IF→2→EFG. These evolutionary sequences reflect the evolution of the LSU followed by the SSU to form the ribosome; 3) the OB-fold IF1 is a mimic of an ancient tRNA minihelix.
Conclusion
The evolution of translational GTPases of both the Archaea and Bacteria point to the evolution of the ribosome. The elongation factors, EFTu/EF1, began as a Ras-like GTPase bringing the activated minihelix tRNA to the Large Subunit Unit. The initiation factors and elongation factor would then have evolved from the EFTu/EF1 as the small subunit was added to the evolving ribosome. The SRP has an SRP54 GTPase and a specific RNA fold in its RNA component similar to the PTC. We consider the SRP to be a remnant of an ancient form of an LSU bound to a membrane.
Reviewers
This article was reviewed by George Fox, Leonid Mirny and Chris Sander. |
| first_indexed | 2024-09-23T14:51:42Z |
| format | Article |
| id | mit-1721.1/69628 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T14:51:42Z |
| publishDate | 2012 |
| publisher | Springer (Biomed Central Ltd.) |
| record_format | dspace |
| spelling | mit-1721.1/696282022-10-01T22:58:48Z GTPases and the origin of the ribosome Smith, Temple F. Hartman, Hyman Massachusetts Institute of Technology. Center for Biomedical Engineering Massachusetts Institute of Technology. Department of Earth, Atmospheric, and Planetary Sciences Hartman, Hyman Hartman, Hyman Background This paper is an attempt to trace the evolution of the ribosome through the evolution of the universal P-loop GTPases that are involved with the ribosome in translation and with the attachment of the ribosome to the membrane. The GTPases involved in translation in Bacteria/Archaea are the elongation factors EFTu/EF1, the initiation factors IF2/aeIF5b + aeIF2, and the elongation factors EFG/EF2. All of these GTPases also contain the OB fold also found in the non GTPase IF1 involved in initiation. The GTPase involved in the signal recognition particle in most Bacteria and Archaea is SRP54. Results 1) The Elongation Factors of the Archaea based on structural considerations of the domains have the following evolutionary path: EF1→ aeIF2 → EF2. The evolution of the aeIF5b was a later event; 2) the Elongation Factors of the Bacteria based on the topological considerations of the GTPase domain have a similar evolutionary path: EFTu→ IF→2→EFG. These evolutionary sequences reflect the evolution of the LSU followed by the SSU to form the ribosome; 3) the OB-fold IF1 is a mimic of an ancient tRNA minihelix. Conclusion The evolution of translational GTPases of both the Archaea and Bacteria point to the evolution of the ribosome. The elongation factors, EFTu/EF1, began as a Ras-like GTPase bringing the activated minihelix tRNA to the Large Subunit Unit. The initiation factors and elongation factor would then have evolved from the EFTu/EF1 as the small subunit was added to the evolving ribosome. The SRP has an SRP54 GTPase and a specific RNA fold in its RNA component similar to the PTC. We consider the SRP to be a remnant of an ancient form of an LSU bound to a membrane. Reviewers This article was reviewed by George Fox, Leonid Mirny and Chris Sander. National Science Foundation (U.S.) (Grant DBI-0516000) 2012-03-09T18:10:15Z 2012-03-09T18:10:15Z 2010-05 2010-04 Article http://purl.org/eprint/type/JournalArticle 1745-6150 http://hdl.handle.net/1721.1/69628 Hartman, Hyman, and Temple F Smith. “GTPases and the Origin of the Ribosome.” Biology Direct 5.1 (2010): 36. Web. 9 Mar. 2012. https://orcid.org/0000-0002-1765-7530 en_US http://dx.doi.org/10.1186/1745-6150-5-36 Biology Direct Creative Commons Attribution http://creativecommons.org/licenses/by/2.0 application/pdf Springer (Biomed Central Ltd.) BioMed Central |
| spellingShingle | Smith, Temple F. Hartman, Hyman GTPases and the origin of the ribosome |
| title | GTPases and the origin of the ribosome |
| title_full | GTPases and the origin of the ribosome |
| title_fullStr | GTPases and the origin of the ribosome |
| title_full_unstemmed | GTPases and the origin of the ribosome |
| title_short | GTPases and the origin of the ribosome |
| title_sort | gtpases and the origin of the ribosome |
| url | http://hdl.handle.net/1721.1/69628 https://orcid.org/0000-0002-1765-7530 |
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