Elongation factor

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

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1 Function
2 3D structures of elongation factor

Function

Elongation factors (EF) facilitate translational elongation during the formation of peptide bonds in the ribosome.

EF-selB is selenocysteine-specific EF. See SelB
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^[1].
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 γ 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^[2].
EF-3 is a unique EF in fungi hence it provides an anti-fungal drug target. See HEAT Repeat
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.
Elongin complex or SIII activates elongation by RNA polymerase II by suppressing transient pausing of the enzyme^[3]. 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.
Negative EF (NELF) are involved in regulating the pausing of RNA Pol II polymerase transcripton^[4].

, or, more exactly (PDB entry 1efu).^[5]

3D structures of elongation factor

Elongation factor 3D structures

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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

Retrieved from "http://52.214.119.220/wiki/index.php/Elongation_factor"

Category: Topic Page

@@ Line 1: / Line 1: @@
-<StructureSection load='1efu' size='400' side='right' caption='Structure of EF-Tu (grey and pink) with EF-Ts (green and yellow) (PDB entry [[1efu]])' scene=''>
+<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__
-'''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.
+== Function ==
-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.
-==3D structures of elongation factor==
+'''Elongation factors''' (EF) facilitate translational elongation during the formation of peptide bonds in the ribosome.<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-Ts or EF 1-β''' (elongation factor thermo stable) catalyzes the release of GDP from EF-Tu.<br />
+* '''EF-G''' translocates the peptidyl tRNA from the A site to the P site while moving the mRNA through the ribosome.<br />
+* '''EF-SII''' helps RNA polymerase II to bypass blocks to elongation.<br />
+* '''EF-ELL2''' enhances polyadenylation and exon skipping with the gene encoding the immunoglobulin heavy-chain complex.<br />
+* '''EF-GreA or GreB''' are cleavage factors allowing the resumption of elongation.<br />
+* '''EF-NusA''' recruits translesion DNA polymerases to gaps encountered during translation.<br />
+* '''EF-P''' alters the ribosome affinity to aminoacyl-tRNA.<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-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-CA150''' is believed to play a role in coupling transcription and splicing.<br />
+*  '''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 />
-===EF-Tu===
+<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>
-[[1efm]], [[1efc]], [[1dg1]], [[2fx3]] – EcEF – ''Escherichia coli''<BR />
+==3D structures of elongation factor==
-[[1qzd]] – EcEF – Cryo EM<BR />
+[[Elongation factor 3D structures]]
-[[3u2q]] – EcEF + drug<BR />
-[[1mj1]] – EcEF + Phe-tRNA + S12 + S13 + L11 – 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 />
-[[3agj]] – EF + plethora protein – ''Aeropyrum pernix''
-''EF-Tu complex with antibiotics''
+</StructureSection>
-[[1ob2]] - yEF + Phe-tRNA + antibiotic<BR />
+== References ==
-[[4abr]] - TtEF + antibiotic in 30S ribosome<BR />
+<references/>
-[[1ha3]] - TtEF + antibiotic + GDP<BR />
-[[2c77]], [[2c78]] - TtEF + antibiotic + GTP analog<br />
-[[3fic]], [[3fic]] – TtEF + antibiotic in 70S ribosome – Cryo EM<BR />
-[[2bvn]] - EcEF + GDP<BR />NP + antibiotic<BR />
-[[1d8t]], [[2hcj]], [[2hdn]], [[3u6b]], [[3u6k]] – 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''
-''EF-Tu with EF-Ts''
-[[1efu]] – EcEF + EcEF-Ts<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 />
-[[3izv]], [[3izw]] -  EcEF in 30S ribosome – Cryo EM<BR />
-[[1zc8]], [[3dwu]] – TtEF in 70S ribosome – Cryo EM<BR />
-[[2wrn]], [[2wrq]], [[2xqd]], [[2y0u]], [[2y0w]], [[2y0y]], [[2y10]], [[2y12]], [[2y14]], [[2y16]], [[2y18]] - 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 />
-===EF-ELL2===
-[[2e5n]] – hEF N2 domain - NMR<BR />
-===EF-G===
-[[1efg]], [[1elo]], [[1ktv]], [[1wdt]], [[2dy1]] – TtEF<BR />
-[[1pn6]], [[3izp]] – TtEF – Cryo EM<BR />
-[[1fnm]], [[2bm0]], [[2bm1]] – TtEF (mutant) <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 />
-[[2xsy]], [[2xuy]] - TtEF in 70S ribosome<BR />
-[[1dar]], [[2efg]] – TtEF + GDP<BR />
-[[1jqm]], [[1jqs]] – EcEF + L11 – Cryo EM<BR />
-[[1zn0]], [[2rdo]], [[3j0e]], [[3j18]] – EcEF in 30S ribosome – Cryo-EM<BR />
-===EF-GreA/GreB===
-[[2pn0]] – EF – ''Nitrosomonas europaea''<BR />
-[[2p4v]] – EcEF-GreB
-===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 />
-[[3huw]], [[3huy]] – TtEF in 70S ribosome<BR />
-[[3oyy]] – EF – ''Pseudomonas aeruginosa''<BR />
-[[3a5z]] – EcEF + lysyl-tRNA synthetase
-===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]] – EF – ''Pyrococcus horikoshii''<BR />
-[[2uz8]] – hEF (mutant)
-===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]] - yEF + antifungal drug 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-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]] – MmEF – ''Methanococcus maripaludis''<BR />
-[[1wb3]] – MmEF + GTP analog<br />
-[[4ac9]] – 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]] – 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 repeat<BR />
-[[2fnj]] - mEloBC + GUSTAVUS
-</StructureSection>
 [[Category:Topic Page]]

Elongation factor

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Contents

Function

3D structures of elongation factor

References

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