Biology:eEF-1
| Elongation factor 1 beta central acidic region, eukaryote | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | EF1_beta_acid | ||||||||
| Pfam | PF10587 | ||||||||
| InterPro | IPR018940 | ||||||||
| SMART | SM01182 | ||||||||
| |||||||||
| Translation elongation factor EF1B, beta/delta subunit, guanine nucleotide exchange domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | EF1_GNE | ||||||||
| Pfam | PF00736 | ||||||||
| InterPro | IPR014038 | ||||||||
| SMART | SM00888 | ||||||||
| CDD | cd00292 | ||||||||
| |||||||||
eEF-1 are two eukaryotic elongation factors. It forms two complexes, the EF-Tu homolog EF-1A and the EF-Ts homolog EF-1B, the former's guanide exchange factor.[1] Both are also found in archaea.[2]
Structure
The nomenclature for the eEF-1 subunits have somewhat shifted around circa 2001, as it was recognized that the EF-1A and EF-1B complexes are to some extent independent of each other.[1] Components as currently recognized and named include:[3]
| Current Nomenclature | Old Nomenclature | Human Genes | Canonical Function |
|---|---|---|---|
| eEF1A | eEF1α | EEF1A1, EEF1A2 EEF1A1P43 |
aa-tRNA delivery to the ribosome; associates with aa-tRNA synthase complex. |
| eEF1Bα | eEF1β (animal, fungi) eEF1β' (plant) |
EEF1B2 EEF1B2P1, EEF1B2P2, EEF1B2P3 |
GEF for eEF1A. |
| eEF1Bβ | eEF1β (plant) | (None) | Additional GEF for eEF1A in plants with CDF-kinase-controlled activity.[3] |
| eEF1Bγ | eEF1γ | EEF1G | Structural component. |
| eEF1Bδ | eEF1δ | EEF1D | Additional GEF for eEF1A in animals. |
| eEF1ε | eEF1ε | EEF1E1 | Not really an elongation factor. Scaffolding for the aa-tRNA synthase complex.[4] |
| Val-RS | Val-RS | VARS | Valyl-tRNA synthetase, binds eEF1Bδ in rabbits.[3] |
The precise manner eEF1B subunit attaches onto eEF1A varies by organ and species.[3] eEF1A also binds actin.[3]
Other species
Various species of green algae, red algae, chromalveolates, and fungi lack the EF-1α gene but instead possess a related gene called EFL (elongation factor-like). Although its function has not been studied in depth, it appears to be similar to EF-1α.
(As of 2009), only two organisms are known to have both EF-1α and EFL: the fungus Basidiobolus and the diatom Thalassiosira. The evolutionary history of EFL is unclear. It may have arisen one or more times followed by loss of EFL or EF-1α. The presence in three diverse eukaryotic groups (fungi, chromalveolates, and archaeplastida) is supposed to be the result of two or more horizontal gene transfer events, according to a 2009 review.[5] A 2013 report finds 11 more species with both genes, and provided an alternative hypothesis that an ancestor eukaryote may have both genes. In all known organisms where both genes are present, EF-1α tends to be transcriptionally repressed. If the hypothesis holds true, scientists would expect to find an organism that has a repressed EFL and a fully-functioning EF-1α.[6]
A 2014 review of EF-1α/EFL possessing eukaryotes considers both explanations insufficient on their own to explain the complex distribution of these two proteins in Eukaryotes.[7]
In eukaryotes, a related GTPase called eRF3 participates in translation termination. The archaeal EF-1α, on the other hand, performs all functions carried by these subfunctionalized variants.[8]
See also
References
- ↑ 1.0 1.1 "Structural studies of eukaryotic elongation factors". Cold Spring Harbor Symposia on Quantitative Biology 66: 425–37. 2001. doi:10.1101/sqb.2001.66.425. PMID 12762045.
- ↑ "The crystal structure of Sulfolobus solfataricus elongation factor 1alpha in complex with GDP reveals novel features in nucleotide binding and exchange". The EMBO Journal 20 (19): 5305–11. October 2001. doi:10.1093/emboj/20.19.5305. PMID 11574461.
- ↑ 3.0 3.1 3.2 3.3 3.4 "The many roles of the eukaryotic elongation factor 1 complex". Wiley Interdisciplinary Reviews: RNA 3 (4): 543–55. 2011. doi:10.1002/wrna.1118. PMID 22555874.
- ↑ "Dissection of the structural organization of the aminoacyl-tRNA synthetase complex". The Journal of Biological Chemistry 284 (10): 6053–60. March 2009. doi:10.1074/jbc.M809636200. PMID 19131329.
- ↑ Ellen Cocquyt; Heroen Verbruggen; Frederik Leliaert; Frederick W Zechman; Koen Sabbe; Olivier De Clerck (2009), "Gain and loss of elongation factor genes in green algae", BMC Evol. Biol. 9 (1): 39, doi:10.1186/1471-2148-9-39, PMID 19216746, Bibcode: 2009BMCEE...9...39C
- ↑ "Parallel re-modeling of EF-1α function: divergent EF-1α genes co-occur with EFL genes in diverse distantly related eukaryotes". BMC Evolutionary Biology 13 (1): 131. June 2013. doi:10.1186/1471-2148-13-131. PMID 23800323. Bibcode: 2013BMCEE..13..131K.
- ↑ "A complex distribution of elongation family GTPases EF1A and EFL in basal alveolate lineages". Genome Biology and Evolution 6 (9): 2361–7. September 2014. doi:10.1093/gbe/evu186. PMID 25179686.
- ↑ "Omnipotent role of archaeal elongation factor 1 alpha (EF1α in translational elongation and termination, and quality control of protein synthesis". Proceedings of the National Academy of Sciences of the United States of America 107 (45): 19242–7. November 2010. doi:10.1073/pnas.1009599107. PMID 20974926. Bibcode: 2010PNAS..10719242S.
External links
- Peptide+Elongation+Factor+1 at the US National Library of Medicine Medical Subject Headings (MeSH)
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