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Literature summary for 3.6.5.3 extracted from

  • Susorov, D.; Zakharov, N.; Shuvalova, E.; Ivanov, A.; Egorova, T.; Shuvalov, A.; Shatsky, I.N.; Alkalaeva, E.
    Eukaryotic translation elongation factor 2 (eEF2) catalyzes reverse translocation of the eukaryotic ribosome (2018), J. Biol. Chem., 293, 5220-5229 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.5.3

Activating Compound

Activating Compound Comment Organism Structure
GMP-PCP non-hydrolyzable or slowly hydrolyzable GTP analogues such as GMP-PCP and GMP-PNP, able to stall elongation factor on the ribosome, increase the efficiency of the reverse translocation reaction Homo sapiens
GMP-PNP non-hydrolyzable or slowly hydrolyzable GTP analogues such as GMP-PCP and GMP-PNP, able to stall elongation factor on the ribosome, increase the efficiency of the reverse translocation reaction Homo sapiens
additional information presence of nonhydrolyzable GTP analogues increases the reverse translocation at mRNA activity of eukaryotic elongation factor eEF2. Reverse translocation requires an excessive concentration of cognate deacylated tRNA Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
eEF2 in vitro translation by rabbit reticulocyte lysate Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
cycloheximide added to the POST complexes in the presence of eEF2 and deacylated tRNAHis, it blocks the -3 nt shift that supports the reverse translocation model Homo sapiens
hygromycin B the antibiotic effectively inhibits translocation of mRNA and tRNAs on the ribosome in both bacteria and eukaryotes. Hygromycin B blocks the toeprint shift induced by eEF2 and deacylated tRNA Homo sapiens
additional information ADP-ribosylation of eEF2 domain IV blocks reverse translocation activity of eEF2. ADP-ribosylation may directly interrupt the ability of eEF2 to stabilize the intermediate conformation of the tRNA ends during their movement through the SSU in the course of translocation Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
ribosome
-
 Homo sapiens 5840
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens
additional information high concentrations of Mg2+ and spermidine doe not induce spontaneous reverse translocation, as has been reported Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + H2O Homo sapiens
-
 GDP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P13639
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
-
 Homo sapiens GDP + phosphate
-
 ?
additional information elongation factor eEF2 catalyzes ribosomal reverse translocation at one mRNA triplet. This process requires a cognate tRNA in the ribosomal E-site and cannot occur spontaneously without eEF2. The efficiency of this reaction depends on the concentrations of eEF2 and cognate tRNAs and increases in the presence of nonhydrolyzable GTP analogues. Deacylated tRNAHis, cognate to the E-site codon, to the POST ribosomal complexes along with eEF2-GTP, causes a shift of the main toeprint peak by 3 nt toward the 5' end of the mRNA. POST ribosomes relocate backwards by three nucleotides in the presence of cognate deacylated tRNA and eEF2. Reverse translocation required up to a 20fold excess of eEF2 over the ribosomal complexes, whereas direct translocation is effective at a 2:1 ratio. Model of eEF2-catalyzed reverse translocation, overview Homo sapiens ?
-
-

Synonyms

Synonyms Comment Organism
eEF2
-
 Homo sapiens
eukaryotic elongation factor 2
-
 Homo sapiens
GTPase
-
 Homo sapiens
translation elongation factor 2
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

General Information

General Information Comment Organism
malfunction mutations of the conservative histidine H715 residue located at the tip of domain IV decreases the rate of mRNA translocation. ADP-ribosylation of eEF2 domain IV blocks reverse translocation activity of eEF2. ADP-ribosylation may directly interrupt the ability of eEF2 to stabilize the intermediate conformation of the tRNA ends during their movement through the SSU in the course of translocation Homo sapiens
physiological function the eukaryotic elongation factor eEF2 catalyzes ribosomal reverse translocation at one mRNA triplet. This process requires a cognate tRNA in the ribosomal E-site and cannot occur spontaneously without eEF2. The efficiency of this reaction depends on the concentrations of eEF2 and cognate tRNAs and increases in the presence of nonhydrolyzable GTP analogues. Crucial role of interactions of domain IV of eEF2 with the ribosome for the catalysis of the reverse translocation reaction. eEF2 is able to induce ribosomal translocation in forward and backward directions, highlighting the universal mechanism of tRNA-mRNA movements within the ribosome. During forward translocation, eEF2 binds to the PRE complex, capable of undergoing spontaneous conformational changes, including an intersubunit rotation of the ribosomal subunits. During reverse translocation, eEF2 binds to the POST complex, which has a conformation of unrotated ribosomal subunits because no tRNAs with hybrid acceptor ends are present therein. Reverse translocation requires an excessive concentration of cognate deacylated tRNA Homo sapiens