Elongation factor

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<StructureSection load='1efu' size='400' side='right' caption='Structure of EF-Tu with EF-Ts (PDB entry [[1efu]])' scene=''>
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<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'>
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__FORCETOC__
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'''Elongation factors''' (EF) facilitate translational elongation during the formation of peptide bonds in the ribosome. EF-selB is selenocysteine-specific EF. 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.
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== Function ==
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EF-Ts or EF 1-β (elongation factor thermo stable) catalyzes the release of GDP from EF-Tu. EF-G translocates the peptidyl tRNA from the A site to the P site while moving the mRNA through the ribosome. EF-SII helps RNA polymerase II to bypass blocks to elongation. EF-ELL2 enhances polyadenylation and exon skipping with the gene encoding the immunoglobulin heavy-chain complex. EF-GreA or GreB are cleavage factors allowing the resumption of elongation. EF-NusA recruits translesion DNA polymerases to gaps encountered during translation. EF-P alters the ribosome affinity to aminoacyl-tRNA. EF-1 gamma acts during the delivery of aminoacyl tRNA to the ribosome. EF-2 promotes the translocation of the nascent protein chain from the A site to the P site on the ribosome. EF-3 is unique EF in fungi hence it provides an anti-fungal drug target. EF Spt4, Spt5, Spt6 are conserved among eukaryotes. They modulate the chromatin structure. EF-CA150 is believed to play a role in coupling transcription and splicing. The elongin B and C complex is involved in the proteasomal degredation of target proteins.
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==3D structures of elongation factor==
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'''Elongation factors''' (EF) facilitate translational elongation during the formation of peptide bonds in the ribosome.<br />
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* '''EF-selB''' is selenocysteine-specific EF. See [[SelB]]<br />
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* '''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 />
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*'''EF-Ts or EF 1-β''' (elongation factor thermo stable) catalyzes the release of GDP from EF-Tu.<br />
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* '''EF-G''' translocates the peptidyl tRNA from the A site to the P site while moving the mRNA through the ribosome.<br />
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* '''EF-SII''' helps RNA polymerase II to bypass blocks to elongation.<br />
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* '''EF-ELL2''' enhances polyadenylation and exon skipping with the gene encoding the immunoglobulin heavy-chain complex.<br />
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* '''EF-GreA or GreB''' are cleavage factors allowing the resumption of elongation.<br />
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* '''EF-NusA''' recruits translesion DNA polymerases to gaps encountered during translation.<br />
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* '''EF-P''' alters the ribosome affinity to aminoacyl-tRNA.<br />
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* '''EF-1 γ''' acts during the delivery of aminoacyl tRNA to the ribosome.<br />
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* '''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 />
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* '''EF-3''' is a unique EF in fungi hence it provides an anti-fungal drug target. See [[HEAT Repeat]]<br />
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* '''EF Spt4, Spt5, Spt6''' are conserved among eukaryotes. They modulate the chromatin structure.<br />
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* '''EF-CA150''' is believed to play a role in coupling transcription and splicing.<br />
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* '''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 />
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* '''Negative EF''' (NELF) are involved in regulating the pausing of RNA Pol II polymerase transcripton<ref>PMID:38401543</ref>.<br />
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===EF-Tu===
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<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>
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[[1efm]], [[1efc]], [[1dg1]], [[2fx3]] – EcEF – ''Escherichia coli''<BR />
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==3D structures of elongation factor==
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[[1qzd]] – EcEF – Cryo EM<BR />
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[[Elongation factor 3D structures]]
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[[3u2q]] – EcEF + drug<BR />
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[[1mj1]] – EcEF + Phe-tRNA + S12 + S13 + L11 – Cryo EM<BR />
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[[1ttt]], [[1ob5]] – TaEF + Phe-tRNA + GDPNP - ''Thermus aquaticus''<BR />
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[[1b23]] - TaEF + Cys-tRNA<BR />
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[[1ls2]] – yEF + Phe-tRNA – yeast – Cryo EM<BR />
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[[3agj]] – EF + plethora protein – ''Aeropyrum pernix''
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''EF-Tu complex with antibiotics''
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</StructureSection>
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[[1ob2]] - yEF + Phe-tRNA + antibiotic<BR />
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== References ==
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[[4abr]] - TtEF + antibiotic in 30S ribosome<BR />
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<references/>
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[[1ha3]] - TtEF + antibiotic + GDP<BR />
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[[2c77]], [[2c78]] - TtEF + antibiotic + GTP analog<br />
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[[3fic]], [[3fic]] – TtEF + antibiotic in 70S ribosome – Cryo EM<BR />
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[[2bvn]] - EcEF + GDP<BR />NP + antibiotic<BR />
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[[1d8t]], [[2hcj]], [[2hdn]], [[3u6b]], [[3u6k]] – EcEF + antibiotic
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''EF-Tu complex with nucleotide''
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[[Category:Topic Page]]
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[[1efu]] – EcEF + GDP<BR />
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[[1exm]] – TtEF + GTP analog<br />
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[[1eft]] – TaEF + GNP – ''Thermus aquaticus''<BR />
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[[1tui]] – TaEF + GDP<BR />
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[[1d2e]] – bEF + GDP – bovine<BR />
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[[1jny]], [[1skq]] – SsEF + GDP – ''Sulfolobus solfataricus''
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''EF-Tu with EF-Ts''
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[[1efu]] – EcEF + EcEF-Ts<BR />
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[[1aip]] - TtEF + TtEF-Ts - ''Thermus thermophilus''<BR />
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[[1xb2]] – bEF + EF-Ts - bovine<BR />
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[[1f60]] – yEF + EF-Ts C terminal<BR />
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[[1g7c]] - yEF + EF-Ts C terminal + GDPNP<BR />
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[[1ije]], [[1ijf]] - yEF + EF-Ts C terminal + GDP<BR />
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[[2b7b]] - yEF + EF-Ts C terminal (mutant) + GDP<BR />
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[[2b7c]] - yEF + EF-Ts C terminal (mutant)
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''EF-Tu in the ribosome''
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[[3eq3]], [[3eq4]] – EcEF in 80S ribosome – Cryo EM<BR />
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[[3izv]], [[3izw]] - EcEF in 30S ribosome – Cryo EM<BR />
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[[1zc8]], [[3dwu]] – TtEF in 70S ribosome – Cryo EM<BR />
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[[2wrn]], [[2wrq]], [[2xqd]], [[2y0u]], [[2y0w]], [[2y0y]], [[2y10]], [[2y12]], [[2y14]], [[2y16]], [[2y18]] - TtEF in 70S ribosome
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===EF-SII===
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[[1tfi]] – hEF – human – NMR<BR />
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[[3ndq]] - hEF domain II<BR />
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[[1enw]] – yEF domain II – NMR<BR />
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[[1eo0]] - yEF domain I – NMR<BR />
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[[2xex]] – SaEF – ''Staphylococcus aureus''<BR />
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[[1pqv]], [[1y1v]] – yEF + RNA polymerase II<BR />
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[[1y1y]], [[3gtm]] – yEF + RNA polymerase II + RNA<BR />
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[[1wjt]] – mEF N terminal – mouse – NMR<BR />
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===EF-ELL2===
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[[2e5n]] – hEF N2 domain - NMR<BR />
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===EF-G===
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[[1efg]], [[1elo]], [[1ktv]], [[1wdt]], [[2dy1]] – TtEF<BR />
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[[1pn6]], [[3izp]] – TtEF – Cryo EM<BR />
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[[1fnm]], [[2bm0]], [[2bm1]] – TtEF (mutant) <BR />
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[[2xex]] – SaEF<BR />
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[[3zz0]], [[3zzt]], [[3zzu]] – SaEF (mutant) <BR />
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[[2bv3]] - TtEF (mutant) + GTP analog<br />
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[[2j7k]] - TtEF (mutant) + GDP analog<br />
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[[2om7]], [[2wri]], [[2wrk]] – TtEF in 70S ribosome – Cryo EM<BR />
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[[2xsy]], [[2xuy]] - TtEF in 70S ribosome<BR />
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[[1dar]], [[2efg]] – TtEF + GDP<BR />
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[[1jqm]], [[1jqs]] – EcEF + L11 – Cryo EM<BR />
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[[1zn0]], [[2rdo]], [[3j0e]], [[3j18]] – EcEF in 30S ribosome – Cryo-EM<BR />
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===EF-GreA/GreB===
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[[2pn0]] – EF – ''Nitrosomonas europaea''<BR />
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[[2p4v]] – EcEF-GreB
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===EF-NusA===
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[[1wcl]], [[1wcn]] – EcEF C terminal – NMR<BR />
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[[2kwp]] - EcEF N terminal – NMR<BR />
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[[2jzb]] – EcEF + RNA polymerase subunit α - NMR<BR />
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===EF-P===
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[[1ueb]] – TtEF<BR />
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[[3huw]], [[3huy]] – TtEF in 70S ribosome<BR />
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[[3oyy]] – EF – ''Pseudomonas aeruginosa''<BR />
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[[3a5z]] – EcEF + lysyl-tRNA synthetase
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===EF-Ts===
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[[1tfe]] – TtEF<BR />
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[[1b64]] – hEF guanine exchange factor domain – NMR<BR />
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[[2cp9]] – UBA domain – NMR<BR />
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[[1gh8]] – EF – ''Methanobacterium thermoautotrophicum'' – NMR<BR />
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[[2yy3]] – EF – ''Pyrococcus horikoshii''<BR />
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[[2uz8]] – hEF (mutant)
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===EF-1G===
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[[1nhy]] – yEF N terminal
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[[1pbu]] – hEF C terminal (mutant) - NMR<BR />
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===EF-2===
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[[1n0v]] – yEF<BR />
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[[1u2r]] – yEF + GDP<BR />
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[[1n0u]], [[2e1r]], [[2npf]] – yEF + antifungal drug<BR />
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[[1zm2]], [[1zm3]], [[1zm4]], [[1zm9]], [[3b78]], [[3b82]], [[3b8h]], [[2zit]] – yEF + exotoxin<BR />
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[[1s1h]] - yEF + antifungal drug in 40S ribosome – Cryo EM<BR />
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[[2p8w]], [[2p8x]], [[3dny]] - yEF in 80S ribosome – Cryo EM<BR />
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[[2p8y]], [[2p8z]] - yEF+ antifungal drug in 80S ribosome – Cryo EM<BR />
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===EF-3===
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[[2ix3]] – yEF<BR />
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[[2iwh]] – yEF + ADPNP<BR />
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[[2iw3]] – yEF + ADP<BR />
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[[2ix8]] – yEF in 80S ribosome – Cryo EM<BR />
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===EF-SelB===
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[[1lva]] – MtEF C terminal – ''Moorella thermoacetica''<BR />
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[[2v9v]] – MtEF winged helix domain<BR />
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[[1wsu]], [[2uwm]] – MtEF + RNA<BR />
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[[2ply]] – MtEF (mutant) + RNA<BR />
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[[1wb2]] – MmEF – ''Methanococcus maripaludis''<BR />
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[[1wb3]] – MmEF + GTP analog<br />
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[[4ac9]] – MmEF + GDP<BR />
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[[2pjp]] – EcEF + RNA
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===EF-Spt5===
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[[2do3]], [[2e6z]], [[2e70]] – hEF KOW motif – NMR<BR />
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[[2exu]] – yEF<BR />
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[[3h7h]] – hEF + hEF-Spt4
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===EF-Spt6===
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[[3gxw]], [[3gxx]], [[3pjp]] – EF SH2 domain – ''Candida glabrata''<BR />
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[[3psf]], [[3psi]] – yEF core domain<BR />
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[[3psj]], [[3psk]] – yEF SH2 domain<BR />
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[[2l3t]] - yEF SH2 domain]] - NMR<BR />
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[[3oak]] – yEF + transcription factor IWS1
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===EF-CA150===
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[[2dod]], [[2doe]], [[2dof]], [[2e71]], [[2kiq]], [[2kis]] – hEF FF domain – NMR<BR />
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[[3hfh]] – hEF FF domain<BR />
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[[2ysi]]– mEF WW domain - NMR<BR />
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===Elongin BC complex===
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[[1lqb]] – hEloBC + von-Hippel Lindau disease tumor suppressor + hypoxia inducible factor 1 α<BR />
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[[3zrc]], [[3ztc]], [[3ztd]], [[3zun]] - hEloBC + von-Hippel Lindau disease tumor suppressor + inhibitor<BR />
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[[3zrf]] - hEloBC + von-Hippel Lindau disease tumor suppressor<BR />
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[[2c9w]], [[2izv]], [[2jz3]] – hEloBC + suppressor of cytokine signaling<BR />
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[[3dcg]] – hEloBC + virion infectivity factor<BR />
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[[2xai]] - hEloBC + ankyrin repeat<BR />
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[[2fnj]] - mEloBC + GUSTAVUS
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</StructureSection>
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Current revision

Structure of EF-Tu (cyan and magenta) with EF-Ts (green and yellow) (PDB entry 1efu)

Drag the structure with the mouse to rotate

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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