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eEF-1

From Wikipedia, the free encyclopedia
Elongation factor 1 beta central acidic region, eukaryote
Identifiers
SymbolEF1_beta_acid
PfamPF10587
InterProIPR018940
SMARTSM01182
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Translation elongation factor EF1B, beta/delta subunit, guanine nucleotide exchange domain
Identifiers
SymbolEF1_GNE
PfamPF00736
InterProIPR014038
SMARTSM00888
CDDcd00292
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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

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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

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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

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References

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  1. ^ a b Andersen GR, Nyborg J (2001). "Structural studies of eukaryotic elongation factors". Cold Spring Harbor Symposia on Quantitative Biology. 66: 425–37. doi:10.1101/sqb.2001.66.425. PMID 12762045.
  2. ^ Vitagliano L, Masullo M, Sica F, Zagari A, Bocchini V (October 2001). "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. doi:10.1093/emboj/20.19.5305. PMC 125647. PMID 11574461.
  3. ^ a b c d e Sasikumar AN, Perez WB, Kinzy TG (2011). "The many roles of the eukaryotic elongation factor 1 complex". Wiley Interdisciplinary Reviews: RNA. 3 (4): 543–55. doi:10.1002/wrna.1118. PMC 3374885. PMID 22555874.
  4. ^ Kaminska M, Havrylenko S, Decottignies P, Gillet S, Le Maréchal P, Negrutskii B, Mirande M (March 2009). "Dissection of the structural organization of the aminoacyl-tRNA synthetase complex". The Journal of Biological Chemistry. 284 (10): 6053–60. doi:10.1074/jbc.M809636200. PMID 19131329.
  5. ^ 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, Bibcode:2009BMCEE...9...39C, doi:10.1186/1471-2148-9-39, PMC 2652445, PMID 19216746
  6. ^ Kamikawa R, Brown MW, Nishimura Y, Sako Y, Heiss AA, Yubuki N, et al. (June 2013). "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. Bibcode:2013BMCEE..13..131K. doi:10.1186/1471-2148-13-131. PMC 3699394. PMID 23800323.
  7. ^ Mikhailov KV, Janouškovec J, Tikhonenkov DV, Mirzaeva GS, Diakin AY, Simdyanov TG, et al. (September 2014). "A complex distribution of elongation family GTPases EF1A and EFL in basal alveolate lineages". Genome Biology and Evolution. 6 (9): 2361–7. doi:10.1093/gbe/evu186. PMC 4217694. PMID 25179686.
  8. ^ Saito K, Kobayashi K, Wada M, Kikuno I, Takusagawa A, Mochizuki M, et al. (November 2010). "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. Bibcode:2010PNAS..10719242S. doi:10.1073/pnas.1009599107. PMC 2984191. PMID 20974926.
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