Elongation factor
From Proteopedia
(Difference between revisions)
(11 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | <StructureSection load=' | + | <StructureSection load='' size='350' side='right' caption='Structure of EF-Tu (cyan and magenta) with EF-Ts (green and yellow) (PDB entry [[1efu]])' scene='51/517376/Cv/1'> |
+ | __FORCETOC__ | ||
+ | |||
+ | == Function == | ||
'''Elongation factors''' (EF) facilitate translational elongation during the formation of peptide bonds in the ribosome.<br /> | '''Elongation factors''' (EF) facilitate translational elongation during the formation of peptide bonds in the ribosome.<br /> | ||
- | * '''EF-selB''' is selenocysteine-specific EF.<br /> | + | * '''EF-selB''' is selenocysteine-specific EF. See [[SelB]]<br /> |
* '''EF-Tu or EF 1-α''' (elongation factor thermo unstable) is a prokaryotic EF. EF-Tu contributes to translational accuracy. It catalyzes the addition of aminoacyl tRNA<ref>PMID:20798060</ref>. <br /> | * '''EF-Tu or EF 1-α''' (elongation factor thermo unstable) is a prokaryotic EF. EF-Tu contributes to translational accuracy. It catalyzes the addition of aminoacyl tRNA<ref>PMID:20798060</ref>. <br /> | ||
*'''EF-Ts or EF 1-β''' (elongation factor thermo stable) catalyzes the release of GDP from EF-Tu.<br /> | *'''EF-Ts or EF 1-β''' (elongation factor thermo stable) catalyzes the release of GDP from EF-Tu.<br /> | ||
Line 13: | Line 16: | ||
* '''EF-1 γ''' acts during the delivery of aminoacyl tRNA to the ribosome.<br /> | * '''EF-1 γ''' acts during the delivery of aminoacyl tRNA to the ribosome.<br /> | ||
* '''EF-2''' promotes the translocation of the nascent protein chain from the A site to the P site on the ribosome<ref>PMID:16246167</ref>.<br /> | * '''EF-2''' promotes the translocation of the nascent protein chain from the A site to the P site on the ribosome<ref>PMID:16246167</ref>.<br /> | ||
- | * '''EF-3''' is a unique EF in fungi hence it provides an anti-fungal drug target.<br /> | + | * '''EF-3''' is a unique EF in fungi hence it provides an anti-fungal drug target. See [[HEAT Repeat]]<br /> |
* '''EF Spt4, Spt5, Spt6''' are conserved among eukaryotes. They modulate the chromatin structure.<br /> | * '''EF Spt4, Spt5, Spt6''' are conserved among eukaryotes. They modulate the chromatin structure.<br /> | ||
* '''EF-CA150''' is believed to play a role in coupling transcription and splicing.<br /> | * '''EF-CA150''' is believed to play a role in coupling transcription and splicing.<br /> | ||
- | * '''Elongin B and C | + | * '''Elongin complex''' or '''SIII''' activates elongation by RNA polymerase II by suppressing transient pausing of the enzyme<ref>PMID:7660129</ref>. The complex is composed of elongin A, B and C. '''Elongin A''' (EloA) is the active component of the complex. '''Elongin B and C''' (EloBC) are the regulatory subunits of it. '''Von Hippel-Landau tumor suppressor protein''' (VHL) binds to EloBC and inhibits transcriptional elongation.<br /> |
+ | * '''Negative EF''' (NELF) are involved in regulating the pausing of RNA Pol II polymerase transcripton<ref>PMID:38401543</ref>.<br /> | ||
- | <scene name='51/517376/Cv/ | + | <scene name='51/517376/Cv/4'>Complex EF-Tu with EF-Ts is heterotetramer</scene>, or, more exactly <scene name='51/517376/Cv/5'>heterodimer of homodimers</scene> (PDB entry [[1efu]]).<ref>PMID:8596629</ref> |
- | + | ==3D structures of elongation factor== | |
- | + | [[Elongation factor 3D structures]] | |
</StructureSection> | </StructureSection> | ||
- | ==3D structures of elongation factor== | ||
- | |||
- | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
- | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
- | |||
- | *EF-Tu | ||
- | |||
- | **[[1efm]], [[1efc]], [[1dg1]], [[2fx3]], [[1etu]] – EcEF – ''Escherichia coli''<BR /> | ||
- | **[[1qzd]] – EcEF – Cryo EM<BR /> | ||
- | **[[3u2q]] – EcEF + drug<BR /> | ||
- | **[[1mj1]] – EcEF + Phe-tRNA + S12 + S13 + L11 – Cryo EM<BR /> | ||
- | **[[3ep2]] - EcEF + tRNA + S12 + L11 + 16SRRNA + 23SRRNA – Cryo EM<BR /> | ||
- | **[[1ttt]], [[1ob5]] – TaEF + Phe-tRNA + GDPNP - ''Thermus aquaticus''<BR /> | ||
- | **[[1b23]] - TaEF + Cys-tRNA<BR /> | ||
- | **[[1ls2]] – yEF + Phe-tRNA – yeast – Cryo EM<BR /> | ||
- | **[[3wxm]] – ApEF + plethora protein – ''Aeropyrum pernix''<br /> | ||
- | **[[4h9g]], [[4lbv]], [[4lbw]], [[4lby]], [[4lbz]], [[4lc0]] – TtEF – ''Thermus thermophilus''<br /> | ||
- | **[[4j0q]] – EF – ''Pseudomonas putida''<br /> | ||
- | |||
- | *''EF-Tu complex with antibiotics'' | ||
- | |||
- | **[[1ob2]] - yEF + Phe-tRNA + antibiotic<BR /> | ||
- | **[[4v8q]] - TtEF + antibiotic in 30S ribosome<BR /> | ||
- | **[[1ha3]] - TtEF + antibiotic + GDP<BR /> | ||
- | **[[2c77]], [[2c78]] - TtEF + antibiotic + GTP analog<br /> | ||
- | **[[4v68]] – TtEF + antibiotic in 70S ribosome – Cryo EM<BR /> | ||
- | **[[2bvn]] - EcEF + GDP<BR />NP + antibiotic<BR /> | ||
- | **[[1d8t]], [[2hcj]], [[2hdn]], [[3u6b]], [[3u6k]], [[4g5g]] – EcEF + antibiotic | ||
- | |||
- | *''EF-Tu complex with nucleotide'' | ||
- | |||
- | **[[1efu]] – EcEF + GDP<BR /> | ||
- | **[[1exm]] – TtEF + GTP analog<br /> | ||
- | **[[1eft]] – TaEF + GNP – ''Thermus aquaticus''<BR /> | ||
- | **[[1tui]] – TaEF + GDP<BR /> | ||
- | **[[1d2e]] – bEF + GDP – bovine<BR /> | ||
- | **[[1jny]], [[1skq]] – SsEF + GDP – ''Sulfolobus solfataricus''<br /> | ||
- | **[[3wya]] – PhEF + GDP - ''Pyrococcus horikoshii''<br /> | ||
- | |||
- | *''EF-Tu complex with protein'' | ||
- | |||
- | **[[3vmf]] – ApEF + translation termination factor<br /> | ||
- | **[[3wy9]] – PhEF + L12 <br /> | ||
- | **[[4p3y]] – EcEF + thiol:disulfide interchange protein <br /> | ||
- | |||
- | *''EF-Tu with EF-Ts'' | ||
- | |||
- | **[[1efu]], [[3agp]], [[3agq]] – EcEF + EcEF-Ts<BR /> | ||
- | **[[3avt]], [[3avu]] , [[3avv]], [[3avw]], [[3avx]], [[3avy]], [[3vnu]] , [[3vnv]], [[4fwt]] – EcEF + EcEF-Ts + RNA<br /> | ||
- | **[[3mmp]] – EcEF + EcEF-Ts + RNA replicase beta chain<br /> | ||
- | **[[4q7j]] – EcEF + EcEF-Ts + Q beta replicase + S1<br /> | ||
- | **[[1aip]] - TtEF + TtEF-Ts - ''Thermus thermophilus''<BR /> | ||
- | **[[1xb2]] – bEF + EF-Ts - bovine<BR /> | ||
- | **[[1f60]] – yEF + EF-Ts C terminal<BR /> | ||
- | **[[1g7c]] - yEF + EF-Ts C terminal + GDPNP<BR /> | ||
- | **[[1ije]], [[1ijf]] - yEF + EF-Ts C terminal + GDP<BR /> | ||
- | **[[2b7b]] - yEF + EF-Ts C terminal (mutant) + GDP<BR /> | ||
- | **[[2b7c]] - yEF + EF-Ts C terminal (mutant) | ||
- | |||
- | *''EF-Tu in the ribosome'' | ||
- | |||
- | **[[3eq3]], [[3eq4]] – EcEF in 80S ribosome – Cryo EM<BR /> | ||
- | **[[4v6l]], [[4v6k]], [[4v69]] - EcEF in 30S ribosome – Cryo EM<BR /> | ||
- | **[[1zc8]], [[3dwu]] – TtEF in 70S ribosome – Cryo EM<BR /> | ||
- | **[[4v5g]], [[4v5l]], [[4v5p]], [[4v5q]], [[4v5r]], [[4v5s]] - TtEF in 70S ribosome | ||
- | |||
- | *EF-SII | ||
- | |||
- | **[[1tfi]] – hEF – human – NMR<BR /> | ||
- | **[[3ndq]] - hEF domain II<BR /> | ||
- | **[[1enw]] – yEF domain II – NMR<BR /> | ||
- | **[[1eo0]] - yEF domain I – NMR<BR /> | ||
- | **[[2xex]] – SaEF – ''Staphylococcus aureus''<BR /> | ||
- | **[[1pqv]], [[1y1v]] – yEF + RNA polymerase II<BR /> | ||
- | **[[1y1y]], [[3gtm]] – yEF + RNA polymerase II + RNA<BR /> | ||
- | **[[1wjt]] – mEF N terminal – mouse – NMR<BR /> | ||
- | **[[2m1h]] – EF PWWP domain – ''Trypanosoma brucei'' – NMR<br /> | ||
- | |||
- | *EF-ELL2 | ||
- | |||
- | **[[2e5n]] – hEF N2 domain - NMR<BR /> | ||
- | |||
- | *EF-G | ||
- | |||
- | **[[1efg]], [[1elo]], [[1ktv]], [[1wdt]], [[2dy1]] – TtEF<BR /> | ||
- | **[[4m1k]], [[4myt]], [[4myu]] – TtEF (mutant)<br /> | ||
- | **[[1pn6]], [[3izp]] – TtEF – Cryo EM<BR /> | ||
- | **[[4v8u]] – TtEF in 70S ribosome <BR /> | ||
- | **[[4v9h]], [[4v9j]], [[4v9k]], [[4v9l]], [[4v9m]], [[4v90]] – TtEF in 30S ribosome <BR /> | ||
- | **[[4v9o]], [[4v9p]] – EcEF in 30S ribosome <BR /> | ||
- | **[[4v9b]] – EcEF in 30S ribosome – Cryo-EM<BR /> | ||
- | **[[4v9d]] – EcEF in 30S ribosome + antibiotics – Cryo-EM<BR /> | ||
- | **[[1fnm]], [[2bm0]], [[2bm1]] – TtEF (mutant) <BR /> | ||
- | **[[2bcw]] – TtEF + L11 + L7/L12 <br /> | ||
- | **[[2xex]] – SaEF<BR /> | ||
- | **[[3zz0]], [[3zzt]], [[3zzu]] – SaEF (mutant) <BR /> | ||
- | **[[2bv3]] - TtEF (mutant) + GTP analog<br /> | ||
- | **[[2j7k]] - TtEF (mutant) + GDP analog<br /> | ||
- | **[[2om7]], [[2wri]], [[2wrk]] – TtEF in 70S ribosome – Cryo EM<BR /> | ||
- | **[[4v5m]], [[4v5n]] - TtEF in 70S ribosome<BR /> | ||
- | **[[1dar]], [[2efg]] – TtEF + GDP<BR /> | ||
- | **[[1jqm]], [[1jqs]] – EcEF + L11 – Cryo EM<BR /> | ||
- | **[[1zn0]], [[2rdo]], [[3j0e]], [[4v6t]] – EcEF in 30S ribosome – Cryo-EM<BR /> | ||
- | **[[4fn5]] – PaEF - ''Pseudomonas aeruginosa''<br /> | ||
- | |||
- | *EF-GreA/GreB | ||
- | |||
- | **[[2pn0]] – EF – ''Nitrosomonas europaea''<BR /> | ||
- | **[[2p4v]] – EcEF-GreB<br /> | ||
- | **[[1grj]] – EcEF-GreA<br /> | ||
- | |||
- | *EF-NusA | ||
- | |||
- | **[[1wcl]], [[1wcn]] – EcEF C terminal – NMR<BR /> | ||
- | **[[2kwp]] - EcEF N terminal – NMR<BR /> | ||
- | **[[2jzb]] – EcEF + RNA polymerase subunit α - NMR<BR /> | ||
- | |||
- | *EF-P | ||
- | |||
- | **[[1ueb]] – TtEF<BR /> | ||
- | **[[4v6a]] – TtEF in 70S ribosome<BR /> | ||
- | **[[3oyy]] – PaEF <BR /> | ||
- | **[[3tre]] – EF – ''Coxiella burnetii''<br /> | ||
- | **[[3a5z]] – EcEF + lysyl-tRNA synthetase<br /> | ||
- | **[[1yby]] – EF – ''Clostridium thermocellum''<br /> | ||
- | |||
- | *EF-Ts | ||
- | |||
- | **[[1tfe]] – TtEF<BR /> | ||
- | **[[1b64]] – hEF guanine exchange factor domain – NMR<BR /> | ||
- | **[[2cp9]] – UBA domain – NMR<BR /> | ||
- | **[[1gh8]] – EF – ''Methanobacterium thermoautotrophicum'' – NMR<BR /> | ||
- | **[[2yy3]] – PhEF <BR /> | ||
- | **[[2uz8]] – hEF (mutant) | ||
- | |||
- | *EF-1 α-2 | ||
- | |||
- | **[[4c0s]] – rEF – rabbit<br /> | ||
- | |||
- | *EF-1 δ-1 | ||
- | |||
- | **[[2mvm]], [[2mvn]] – hEF CAR domain – NMR<br /> | ||
- | |||
- | *EF-1G | ||
- | |||
- | **[[1nhy]] – yEF N terminal | ||
- | **[[1pbu]] – hEF C terminal (mutant) - NMR<BR /> | ||
- | |||
- | *EF-2 | ||
- | |||
- | **[[1n0v]] – yEF<BR /> | ||
- | **[[1u2r]] – yEF + GDP<BR /> | ||
- | **[[1n0u]], [[2e1r]], [[2npf]] – yEF + antifungal drug<BR /> | ||
- | **[[1zm2]], [[1zm3]], [[1zm4]], [[1zm9]], [[3b78]], [[3b82]], [[3b8h]], [[2zit]] – yEF + exotoxin<BR /> | ||
- | **[[1s1h]] - hEF in 40S ribosome – Cryo EM<BR /> | ||
- | **[[4cxg]], [[4cxh]] - rEF in 40S ribosome – Cryo EM<BR /> | ||
- | **[[2p8w]], [[2p8x]], [[3dny]] - yEF in 80S ribosome – Cryo EM<BR /> | ||
- | **[[2p8y]], [[2p8z]] - yEF+ antifungal drug in 80S ribosome – Cryo EM<BR /> | ||
- | |||
- | *EF-3 | ||
- | |||
- | **[[2ix3]] – yEF<BR /> | ||
- | **[[2iwh]] – yEF + ADPNP<BR /> | ||
- | **[[2iw3]] – yEF + ADP<BR /> | ||
- | **[[2ix8]] – yEF in 80S ribosome – Cryo EM<BR /> | ||
- | |||
- | *EF-4 (lepA) | ||
- | |||
- | **[[2ywh]], [[2ywe]], [[2ywf]], [[2ywg]] - AalepA + nucleotide - ''Aquifex aeolicus''<BR /> | ||
- | **[[3cb4]] - EclepA <BR /> | ||
- | **[[3deg]] - EclepA in 70S ribosome + GMPPNP – Cryo EM<BR /> | ||
- | |||
- | *EF-SelB | ||
- | |||
- | **[[1lva]] – MtEF C terminal – ''Moorella thermoacetica''<BR /> | ||
- | **[[2v9v]] – MtEF winged helix domain<BR /> | ||
- | **[[1wsu]], [[2uwm]] – MtEF + RNA<BR /> | ||
- | **[[2ply]] – MtEF (mutant) + RNA<BR /> | ||
- | **[[1wb2]], [[4aca]] – MmEF – ''Methanococcus maripaludis''<BR /> | ||
- | **[[1wb3]], [[4acb]] – MmEF + GTP analog<br /> | ||
- | **[[4ac9]], [[1wb1]] – MmEF + GDP<BR /> | ||
- | **[[2pjp]] – EcEF + RNA | ||
- | |||
- | *EF-Spt5 | ||
- | |||
- | **[[2do3]], [[2e6z]], [[2e70]] – hEF KOW motif – NMR<BR /> | ||
- | **[[2exu]] – yEF<BR /> | ||
- | **[[3h7h]] – hEF + hEF-Spt4 | ||
- | |||
- | *EF-Spt6 | ||
- | |||
- | **[[3gxw]], [[3gxx]], [[3pjp]] – EF SH2 domain – ''Candida glabrata''<BR /> | ||
- | **[[3psf]], [[3psi]] – yEF core domain<BR /> | ||
- | **[[3psj]], [[3psk]] – yEF SH2 domain<BR /> | ||
- | **[[2l3t]] - yEF SH2 domain]] - NMR<BR /> | ||
- | **[[3oak]] – yEF + transcription factor IWS1 | ||
- | |||
- | *EF-CA150 | ||
- | |||
- | **[[2dod]], [[2doe]], [[2dof]], [[2e71]], [[2kiq]], [[2kis]] – hEF FF domain – NMR<BR /> | ||
- | **[[3hfh]] – hEF FF domain<BR /> | ||
- | **[[2ysi]]– mEF WW domain - NMR<BR /> | ||
- | |||
- | *Elongin BC complex | ||
- | |||
- | **[[1lqb]], [[1lm8]] – hEloBC + von-Hippel Lindau disease tumor suppressor + hypoxia inducible factor 1 α<br /> | ||
- | **[[3zrc]], [[3ztc]], [[3ztd]], [[3zun]] - hEloBC + von-Hippel Lindau disease tumor suppressor + inhibitor<br /> | ||
- | **[[3zrf]] - hEloBC + von-Hippel Lindau disease tumor suppressor<br /> | ||
- | **[[2c9w]], [[2izv]], [[2jz3]] – hEloBC + suppressor of cytokine signaling<br /> | ||
- | **[[3dcg]] – hEloBC + virion infectivity factor<br /> | ||
- | **[[2xai]] - hEloBC + ankyrin rep<br /> | ||
- | **[[1vcb]] – hEloBC + VHL<br /> | ||
- | **[[2fnj]] - mEloBC + GUSTAVUS | ||
- | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Current revision
|
References
- ↑ Takeshita D, Tomita K. Assembly of Q{beta} viral RNA polymerase with host translational elongation factors EF-Tu and -Ts. Proc Natl Acad Sci U S A. 2010 Sep 7;107(36):15733-8. Epub 2010 Aug 23. PMID:20798060 doi:http://dx.doi.org/10.1073/pnas.1006559107
- ↑ Jorgensen R, Merrill AR, Andersen GR. The life and death of translation elongation factor 2. Biochem Soc Trans. 2006 Feb;34(Pt 1):1-6. PMID:16246167 doi:http://dx.doi.org/10.1042/BST20060001
- ↑ Aso T, Lane WS, Conaway JW, Conaway RC. Elongin (SIII): a multisubunit regulator of elongation by RNA polymerase II. Science. 1995 Sep 8;269(5229):1439-43. PMID:7660129
- ↑ Su BG, Vos SM. Distinct negative elongation factor conformations regulate RNA polymerase II promoter-proximal pausing. Mol Cell. 2024 Apr 4;84(7):1243-1256.e5. PMID:38401543 doi:10.1016/j.molcel.2024.01.023
- ↑ Kawashima T, Berthet-Colominas C, Wulff M, Cusack S, Leberman R. The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution. Nature. 1996 Feb 8;379(6565):511-8. PMID:8596629 doi:http://dx.doi.org/10.1038/379511a0