eEF-1

{{Short description|Eukaryotic elongation factors}}

{{lowercase}}

{{Pfam box

|InterPro=IPR018940

|Symbol=EF1_beta_acid

|Name=Elongation factor 1 beta central acidic region, eukaryote

|Pfam=PF10587

|SMART=SM01182

}}

{{Pfam box

|InterPro=IPR014038

|Name=Translation elongation factor EF1B, beta/delta subunit, guanine nucleotide exchange domain

|Symbol=EF1_GNE

|CDD=cd00292

|Pfam=PF00736

|SMART=SM00888

}}

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.{{cite journal | vauthors = Andersen GR, Nyborg J | title = Structural studies of eukaryotic elongation factors | journal = Cold Spring Harbor Symposia on Quantitative Biology | volume = 66 | pages = 425–37 | date = 2001 | pmid = 12762045 | doi = 10.1101/sqb.2001.66.425 }} Both are also found in archaea.{{cite journal | vauthors = Vitagliano L, Masullo M, Sica F, Zagari A, Bocchini V | title = The crystal structure of Sulfolobus solfataricus elongation factor 1alpha in complex with GDP reveals novel features in nucleotide binding and exchange | journal = The EMBO Journal | volume = 20 | issue = 19 | pages = 5305–11 | date = October 2001 | pmid = 11574461 | doi = 10.1093/emboj/20.19.5305 | pmc = 125647 | doi-access = free }}

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. Components as currently recognized and named include:{{cite journal | vauthors = Sasikumar AN, Perez WB, Kinzy TG | title = The many roles of the eukaryotic elongation factor 1 complex | journal = Wiley Interdisciplinary Reviews: RNA | volume = 3 | issue = 4 | pages = 543–55 | date = 2011 | pmid = 22555874 | pmc = 3374885 | doi = 10.1002/wrna.1118 }}

class=wikitable

! Current Nomenclature !! Old Nomenclature !! Human Genes !! Canonical Function

eEF1AeEF1αEEF1A1, EEF1A2
EEF1A1P43
aa-tRNA delivery to the ribosome; associates with aa-tRNA synthase complex.
eEF1BαeEF1β (animal, fungi)
eEF1β' (plant)
EEF1B2
EEF1B2P1, EEF1B2P2, EEF1B2P3
GEF for eEF1A.
eEF1BβeEF1β (plant)(None)Additional GEF for eEF1A in plants with CDF-kinase-controlled activity.
eEF1BγeEF1γEEF1GStructural component.
eEF1BδeEF1δEEF1DAdditional GEF for eEF1A in animals.
eEF1εeEF1εEEF1E1Not really an elongation factor. Scaffolding for the aa-tRNA synthase complex.{{cite journal | vauthors = Kaminska M, Havrylenko S, Decottignies P, Gillet S, Le Maréchal P, Negrutskii B, Mirande M | title = Dissection of the structural organization of the aminoacyl-tRNA synthetase complex | journal = The Journal of Biological Chemistry | volume = 284 | issue = 10 | pages = 6053–60 | date = March 2009 | pmid = 19131329 | doi = 10.1074/jbc.M809636200 | doi-access = free }}
Val-RSVal-RSVARSValyl-tRNA synthetase, binds eEF1Bδ in rabbits.

The precise manner eEF1B subunit attaches onto eEF1A varies by organ and species. eEF1A also binds actin.

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.{{citation | journal = BMC Evol. Biol. | year = 2009 | volume = 9 | pages = 39 | doi = 10.1186/1471-2148-9-39 | pmc = 2652445 | title = Gain and loss of elongation factor genes in green algae |author1=Ellen Cocquyt |author2=Heroen Verbruggen |author3=Frederik Leliaert |author4=Frederick W Zechman |author5=Koen Sabbe |author6=Olivier De Clerck | issue = 1 | pmid=19216746 | bibcode = 2009BMCEE...9...39C | doi-access = free }} 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.{{cite journal | vauthors = Kamikawa R, Brown MW, Nishimura Y, Sako Y, Heiss AA, Yubuki N, Gawryluk R, Simpson AG, Roger AJ, Hashimoto T, Inagaki Y | display-authors = 6 | title = Parallel re-modeling of EF-1α function: divergent EF-1α genes co-occur with EFL genes in diverse distantly related eukaryotes | journal = BMC Evolutionary Biology | volume = 13 | pages = 131 | date = June 2013 | issue = 1 | pmid = 23800323 | pmc = 3699394 | doi = 10.1186/1471-2148-13-131 | bibcode = 2013BMCEE..13..131K | doi-access = free }}

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.{{cite journal | vauthors = Mikhailov KV, Janouškovec J, Tikhonenkov DV, Mirzaeva GS, Diakin AY, Simdyanov TG, Mylnikov AP, Keeling PJ, Aleoshin VV | display-authors = 6 | title = A complex distribution of elongation family GTPases EF1A and EFL in basal alveolate lineages | journal = Genome Biology and Evolution | volume = 6 | issue = 9 | pages = 2361–7 | date = September 2014 | pmid = 25179686 | pmc = 4217694 | doi = 10.1093/gbe/evu186 | doi-access = free }}

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.{{cite journal | vauthors = Saito K, Kobayashi K, Wada M, Kikuno I, Takusagawa A, Mochizuki M, Uchiumi T, Ishitani R, Nureki O, Ito K | display-authors = 6 | title = Omnipotent role of archaeal elongation factor 1 alpha (EF1α in translational elongation and termination, and quality control of protein synthesis | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 107 | issue = 45 | pages = 19242–7 | date = November 2010 | pmid = 20974926 | doi = 10.1073/pnas.1009599107 | pmc = 2984191 | bibcode = 2010PNAS..10719242S | doi-access = free }}

See also

References

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