This enzyme comprises a family of proteins involved in prokaryotic as well as eukaryotic protein synthesis. In the initiation factor complex, it is IF-2b (98 kDa) that binds GTP and subsequently hydrolyses it in prokaryotes. In eukaryotes, it is eIF-2 (150 kDa) that binds GTP. In the elongation phase, the GTP-hydrolysing proteins are the EF-Tu polypeptide of the prokaryotic transfer factor (43 kDa), the eukaryotic elongation factor EF-1alpha (53 kDa), the prokaryotic EF-G (77 kDa), the eukaryotic EF-2 (70-110 kDa) and the signal recognition particle that play a role in endoplasmic reticulum protein synthesis (325 kDa). EF-Tu and EF-1alpha catalyse binding of aminoacyl-tRNA to the ribosomal A-site, while EF-G and EF-2 catalyse the translocation of peptidyl-tRNA from the A-site to the P-site. GTPase activity is also involved in polypeptide release from the ribosome with the aid of the pRFs and eRFs.
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SYSTEMATIC NAME
IUBMB Comments
GTP phosphohydrolase (mRNA-translation-assisting)
This enzyme comprises a family of proteins involved in prokaryotic as well as eukaryotic protein synthesis. In the initiation factor complex, it is IF-2b (98 kDa) that binds GTP and subsequently hydrolyses it in prokaryotes. In eukaryotes, it is eIF-2 (150 kDa) that binds GTP. In the elongation phase, the GTP-hydrolysing proteins are the EF-Tu polypeptide of the prokaryotic transfer factor (43 kDa), the eukaryotic elongation factor EF-1alpha (53 kDa), the prokaryotic EF-G (77 kDa), the eukaryotic EF-2 (70-110 kDa) and the signal recognition particle that play a role in endoplasmic reticulum protein synthesis (325 kDa). EF-Tu and EF-1alpha catalyse binding of aminoacyl-tRNA to the ribosomal A-site, while EF-G and EF-2 catalyse the translocation of peptidyl-tRNA from the A-site to the P-site. GTPase activity is also involved in polypeptide release from the ribosome with the aid of the pRFs and eRFs.
the enzyme has the same domain structure and biochemical properties of a typical IF2 species as found in bacteria or mammalian mitochondria, but with enhanced ability to bind unformylated initiator met-tRNA
one of the final maturation steps of the large ribosomal subunit requires the joint action of the elongation factor-like 1 (Efl1) GTPase and the Shwachman-Diamond syndrome protein (SDO1, UniProt ID Q07953) to release the eukaryotic translation initiation factor 6 (Tif6) and allow the assembly of mature ribosomes. EFL1 function is driven by conformational changes
calorimetric energetic basis describing the recognition of Efl1 to GT(D)P, Sdo1 and their intercommunication in solution, overview. The structure based analysis of the binding signatures indicates that Efl1 has a large structural flexibility
calorimetric energetic basis describing the recognition of Efl1 to GT(D)P, Sdo1 and their intercommunication in solution, overview. The structure based analysis of the binding signatures indicates that Efl1 has a large structural flexibility
inherited mutations cause fatal brain disorder: childhood ataxia with central nervous system hypomyelination, leukoencephalopathy with vanishing white matter, eIF2B-related disorders
inherited mutations cause fatal brain disorder: childhood ataxia with central nervous system hypomyelination, leukoencephalopathy with vanishing white matter, eIF2B-related disorders
recombinant His-tagged enzyme from Saccharomyces cerevisiae strain BCY123 by nickel affinity chromatography, tag cleavage by TEV protease, and another step of nickel affinity chromatography, followed by gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
full-length enzyme or C2 subdomain of ymIF2 expressed in Escherichia coli. The full-length ymIF2 can substitute for Escherichia coli IF2 in the formation of a functional initiation complex on 70S Escherichia coli ribosomes capable of forming the first peptide bond
rRNA suppressor of a eukaryotic translation initiation factor 5B/initiation factor 2 mutant reveals a binding site for translational GTPases on the small ribosomal subunit
Luviano, A.; Cruz-Castaneda, R.; Sanchez-Puig, N.; Garcia-Hernandez, E.
Cooperative energetic effects elicited by the yeast Shwachman-Diamond syndrome protein (Sdo1) and guanine nucleotides modulate the complex conformational landscape of the elongation factor-like 1 (Efl1) GTPase