Eukaryotic translation elongation (Homo sapiens)
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Description
The translation elongation cycle adds one amino acid at a time to a growing polypeptide according to the sequence of codons found in the mRNA. The next available codon on the mRNA is exposed in the aminoacyl-tRNA (aa-tRNA) binding site (A site) on the 30S subunit.
A: Ternary complexes of aa -tRNA:eEF1A:GTP enter the ribosome and enable the anticodon of the tRNA to make a codon/anticodon interaction with the A-site codon of the mRNA. B: Upon cognate recognition, the eEF1A:GTP is brought into the GTPase activating center of the ribosome, GTP is hydrolyzed and eEF1A:GDP leaves the ribosome. C: The peptidyl transferase center of ribosome catalyses the formation of a peptide bond between the incoming amino acid and the peptide found in the peptidyl-tRNA binding site (P site). D: In the pre-translocation state of the ribosome, the eEF2:GTP enters the ribosome, physically translocating the peptidyl-tRNA out of the A site to P site and leaves the ribosome eEF2:GDP. This action of eEF2:GTP accounts for the precise movement of the mRNA by 3 nucleotides.Consequently, deacylated tRNA is shifted to the E site. A ribosome associated ATPase activity is proposed to stimulate the release of deacylated tRNA from the E site subsequent to translocation (Elskaya et al., 1991). In this post-translocation state, the ribosome is now ready to receive a new ternary complex.
This process is illustrated below with: an amino acyl-tRNA with an amino acid, a peptidyl-tRNA with a growing peptide, a deacylated tRNA with an -OH, and a ribosome with A,P and E sites to accommodate these three forms of tRNA.
A: Ternary complexes of aa -tRNA:eEF1A:GTP enter the ribosome and enable the anticodon of the tRNA to make a codon/anticodon interaction with the A-site codon of the mRNA. B: Upon cognate recognition, the eEF1A:GTP is brought into the GTPase activating center of the ribosome, GTP is hydrolyzed and eEF1A:GDP leaves the ribosome. C: The peptidyl transferase center of ribosome catalyses the formation of a peptide bond between the incoming amino acid and the peptide found in the peptidyl-tRNA binding site (P site). D: In the pre-translocation state of the ribosome, the eEF2:GTP enters the ribosome, physically translocating the peptidyl-tRNA out of the A site to P site and leaves the ribosome eEF2:GDP. This action of eEF2:GTP accounts for the precise movement of the mRNA by 3 nucleotides.Consequently, deacylated tRNA is shifted to the E site. A ribosome associated ATPase activity is proposed to stimulate the release of deacylated tRNA from the E site subsequent to translocation (Elskaya et al., 1991). In this post-translocation state, the ribosome is now ready to receive a new ternary complex.
This process is illustrated below with: an amino acyl-tRNA with an amino acid, a peptidyl-tRNA with a growing peptide, a deacylated tRNA with an -OH, and a ribosome with A,P and E sites to accommodate these three forms of tRNA.
Quality Tags
Ontology Terms
Bibliography
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- Carvalho MD, Carvalho JF, Merrick WC.; ''Biological characterization of various forms of elongation factor 1 from rabbit reticulocytes.''; PubMed Europe PMC Scholia
- Pérez JM, Siegal G, Kriek J, Hård K, Dijk J, Canters GW, Möller W.; ''The solution structure of the guanine nucleotide exchange domain of human elongation factor 1beta reveals a striking resemblance to that of EF-Ts from Escherichia coli.''; PubMed Europe PMC Scholia
- Van Ness BG, Howard JB, Bodley JW.; ''ADP-ribosylation of elongation factor 2 by diphtheria toxin. Isolation and properties of the novel ribosyl-amino acid and its hydrolysis products.''; PubMed Europe PMC Scholia
- Veremieva M, Khoruzhenko A, Zaicev S, Negrutskii B, El'skaya A.; ''Unbalanced expression of the translation complex eEF1 subunits in human cardioesophageal carcinoma.''; PubMed Europe PMC Scholia
- Guillot D, Penin F, Di Pietro A, Sontag B, Lavergne JP, Reboud JP.; ''GTP binding to elongation factor eEF-2 unmasks a tryptophan residue required for biological activity.''; PubMed Europe PMC Scholia
- Van Ness BG, Howard JB, Bodley JW.; ''ADP-ribosylation of elongation factor 2 by diphtheria toxin. NMR spectra and proposed structures of ribosyl-diphthamide and its hydrolysis products.''; PubMed Europe PMC Scholia
- Kapp LD, Lorsch JR.; ''The molecular mechanics of eukaryotic translation.''; PubMed Europe PMC Scholia
History
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External references
DataNodes
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Name | Type | Database reference | Comment |
---|---|---|---|
80S Ribosome:mRNA:
peptidyl-tRNA with elongating peptide | Complex | REACT_4835 (Reactome) | |
80S ribosome | Complex | REACT_4330 (Reactome) | |
80S:Met-tRNAi:
mRNA | Complex | REACT_4537 (Reactome) | |
80S:Met-tRNAi:
mRNA:aminoacyl- tRNA | Complex | REACT_3365 (Reactome) | |
80S:aminoacyl tRNA:
mRNA:eEF1A:GTP | Complex | REACT_5558 (Reactome) | |
Aminoacyl-tRNA | Metabolite | REACT_4792 (Reactome) | |
Elongation complex
with growing peptide chain | Complex | REACT_5024 (Reactome) | |
GTP | Metabolite | 15996 (ChEBI) | |
Orthophosphate | Metabolite | 18367 (ChEBI) | |
eEF1A | Protein | P68104 (UniProt) | |
eEF1A:GDP | Complex | REACT_5872 (Reactome) | |
eEF1A:GTP | Complex | REACT_3513 (Reactome) | |
eEF1A:GTP:
aminoacyl-tRNA complex | Complex | REACT_3062 (Reactome) | |
eEF1B alpha | Protein | P24534 (UniProt) | |
eEF1B beta | Protein | P29692 (UniProt) | |
eEF1B complex | Complex | REACT_3047 (Reactome) | |
eEF1B gamma | Protein | P26641 (UniProt) | |
eEF1B:GDP
exchange complex | Complex | REACT_3385 (Reactome) | |
eEF2 | Protein | P13639 (UniProt) | |
eEF2:GDP | Complex | REACT_5865 (Reactome) | |
eEF2:GTP | Complex | REACT_2807 (Reactome) |
Annotated Interactions
No annotated interactions