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Information on EC 3.6.5.3 - protein-synthesizing GTPase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P39730

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IUBMB Comments
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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Saccharomyces cerevisiae
UNIPROT: P39730
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
elongation factor, translation initiation factor, gtpase-activating protein, eif2alpha, eif2b, elongation factor tu, eef1a, ef-1alpha, eukaryotic initiation factor 2, elongation factor g, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elongation factor (EF)
-
-
-
-
elongation factor-like 1
-
elongation factor-like 1 GTPase
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eukaryotic initiation factor 2
-
-
eukaryotic initiation factor 2A
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-
eukaryotic initiation factor 5B
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-
GTP phosphohydrolase
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-
-
-
GTPase
-
-
-
-
GTPase-activating protein
-
-
guanine triphosphatase
-
-
-
-
guanine-nucleotide-exchange factor of eIF2
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guanosine 5'-triphosphatase
-
-
-
-
guanosine triphosphatase
-
-
-
-
initiation factor (IF)
-
-
-
-
initiation factor 2
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-
mitochondrial initiation factor 2
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peptide-release or termination factor
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-
-
-
ribosomal GTPase
-
-
-
-
ribosome-dependent GTPase
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-
translation initiation factor 2
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-
translation initiation factor 2 gamma
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
hydrolysis of phosphoric ester
-
-
-
-
additional information
-
influence on translation initiation pathway and ribosomal subunit joining
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9059-32-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
-
eIF2A functions as a suppressor of Ure2p internal ribosome entry site-mediated translation in yeast cells
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heteropentamer
alphabetagammadeltaepsilon
trimer
alphabetagamma
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A208V
-
suppressor mutation to rescue growth defect associated with N135D mutation
A219T
-
suppressor mutation to rescue growth defect associated with N135D mutation, as single mutant slow-growth phenotype
A382V
-
suppressor mutation to rescue growth defect associated with N135D mutation
E569A
lethal mutation
E569D
lethal mutation, reduced binding to subunit gamma of eIF2
E569K
lethal mutation, reduced binding to subunit gamma of eIF2
E569Q
lethal mutation, reduced binding to subunit gamma of eIF2
H480I
-
impair of GTP hydrolysis and yeast cell growth
H480I/A709V
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double mutant, faster yeast cell growth
H480I/F643R
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double mutant, suppression of H480I-mutant mediated slow yeast cell growth
H480I/G642F
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double mutant, suppression of H480I-mutant mediated slow yeast cell growth
H480I/I634G
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double mutant, suppression of H480I-mutant mediated slow yeast cell growth
H480I/V637A
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double mutant, suppression of H480I-mutant mediated slow yeast cell growth
H480I/V637G
-
double mutant, suppression of H480I-mutant mediated slow yeast cell growth
L568A
cold sensitivity, defect on protein interaction
N135A
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growth defect
N135D
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slow-growth phenotype, imparied Met-tRNA binding to eIF2
N135K
-
growth defect, recessive lethal mutation
S576N
slow-growing, cold sensitivity, defect on protein interaction
T439A
T439A/F643R
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double mutant, suppression of T439A-mutant mediated slow yeast cell growth
T439A/V637G
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double mutant, suppression of T439A-mutant mediated slow yeast cell growth
T552I
slow-growing, cold sensitivity, defect on protein interaction
W699A
lethal mutation, weakens binding to subunit beta and gamma of eIF2, prevents nucleotide exchange
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
about, melting point, recombinant enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
eIF2A is an inherently unstable protein with a half-life of about 17 min
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C2 subdomain of ymIF2
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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
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
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His-tagged version of ymIF2 lacking its predicted mitochondrial presequence is expressed in Escherichia coli
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recombinant expression of His-tagged enzyme in Saccharomyces cerevisiae strain BCY123
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Garofalo, C.; Trinko, R.; Kramer, G.; Appling, D.R.; Hardesty, B.
Purification and characterization of yeast mitochondrial initiation factor 2
Arch. Biochem. Biophys.
413
243-252
2003
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Garofalo, C.; Kramer, G.; Appling, D.R.
Characterization of the C2 subdomain of yeast mitochondrial initiation factor 2
Arch. Biochem. Biophys.
439
113-120
2005
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Komar, A.A.; Gross, S.R.; Barth-Baus, D.; Strachan, R.; Hensold, J.O.; Goss Kinzy, T.; Merrick, W.C.
Novel characteristics of the biological properties of the yeast Saccharomyces cerevisiae eukaryotic initiation factor 2A
J. Biol. Chem.
280
15601-15611
2005
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Mohammad-Qureshi, S.S.; Jennings, M.D.; Pavitt, G.D.
Clues to the mechanism of action of eIF2B, the guanine-nucleotide-exchange factor for translation initiation
Biochem. Soc. Trans.
36
658-664
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P32501)
Manually annotated by BRENDA team
Acker, M.G.; Shin, B.S.; Nanda, J.S.; Saini, A.K.; Dever, T.E.; Lorsch, J.R.
Kinetic analysis of late steps of eukaryotic translation initiation
J. Mol. Biol.
385
491-506
2009
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Alone, P.V.; Cao, C.; Dever, T.E.
Translation initiation factor 2gamma mutant alters start codon selection independent of Met-tRNA binding
Mol. Cell. Biol.
28
6877-6888
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae J293
Manually annotated by BRENDA team
Shin, B.S.; Kim, J.R.; Acker, M.G.; Maher, K.N.; Lorsch, J.R.; Dever, T.E.
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
Mol. Cell. Biol.
29
808-821
2009
Saccharomyces cerevisiae, Saccharomyces cerevisiae NOY891
Manually annotated by BRENDA team
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
Biophys. Chem.
247
13-24
2019
Saccharomyces cerevisiae (P53893), Saccharomyces cerevisiae, Homo sapiens (Q7Z2Z2), Saccharomyces cerevisiae ATCC 204508 (P53893)
Manually annotated by BRENDA team