3.6.5.3: protein-synthesizing GTPase
This is an abbreviated version!
For detailed information about protein-synthesizing GTPase, go to the full flat file.
Word Map on EC 3.6.5.3
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3.6.5.3
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gtpases
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eif4e
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spacer
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ras
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actin
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rapamycin
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1-alpha
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gdp
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aminoacyl-trnas
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mtor
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rrna
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perk
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clade
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fusarium
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potato
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conidia
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chop
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reticulocyte
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dextrose
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polysomes
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rna-dependent
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gtp-binding
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aminoacylated
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cap-dependent
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adp-ribosylation
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pausing
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monophyletic
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oxysporum
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wilt
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cdc42
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beta-tubulin
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stall
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autophosphorylation
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normfinder
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atf6
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rinsed
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gdp-bound
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reisolated
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neurofibromatosis
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sh2
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preinitiation
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discolor
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interferon-induced
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anticodons
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p21ras
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genorm
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diphtheria
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rnapii
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hyaline
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caspase-12
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medicine
- 3.6.5.3
- gtpases
- eif4e
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spacer
- ras
- actin
- rapamycin
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1-alpha
- gdp
- aminoacyl-trnas
- mtor
- rrna
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perk
- clade
- fusarium
- potato
- conidia
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chop
- reticulocyte
- dextrose
- polysomes
-
rna-dependent
-
gtp-binding
-
aminoacylated
-
cap-dependent
-
adp-ribosylation
-
pausing
-
monophyletic
- oxysporum
-
wilt
- cdc42
- beta-tubulin
-
stall
- autophosphorylation
-
normfinder
- atf6
-
rinsed
-
gdp-bound
-
reisolated
- neurofibromatosis
- sh2
-
preinitiation
-
discolor
-
interferon-induced
-
anticodons
-
p21ras
-
genorm
- diphtheria
- rnapii
-
hyaline
- caspase-12
- medicine
Reaction
Synonyms
50S ribosomal subunit assembly factor, aEF-1alpha, aIF2, aIF2 GTPase, aIF2-gamma, aIF2B, aIF2gamma, aIF5B, archaeal initiation factor 2, archaeal initiation factor 2C, archaeal translation initiation factor 2, BipA, BPI-inducible protein A, Bst-IF2, chloroplast elongation factor G, EC 3.6.1.48, Ec-L10, Ec-L11, Ec-L12, Eco-IF2, eEF1A, eEF2, EF 1 alpha, EF-1alpha, EF-1beta, EF-2, EF-4, EF-G, EF-G GTPase, EF-G1, EF-G1mt, EF-like GTPase, EF-Tu, EF-Tumt, EF4, EFL, Efl1, Efl1 GTPase, eIEF2, eIF 2, eIF2, eIF2A, eIF2alpha, eIF2B, eIF5, eIF5B, elongation factor, elongation factor (EF), elongation factor 1 alpha, elongation factor 1alpha, elongation factor 2, elongation factor 4, elongation factor G, elongation factor thermo unstable, elongation factor Tu, elongation factor-1alpha, elongation factor-1beta, elongation factor-2, elongation factor-like 1, elongation factor-like 1 GTPase, eukaryotic elongation factor 2, eukaryotic elongation factor one alpha, eukaryotic initiation factor 2, eukaryotic initiation factor 2A, eukaryotic initiation factor 5B, eukaryotic translation initiation factor 2, eukaryotic translation initiation factor 5B, fusA, GTP phosphohydrolase, GTPase, GTPase aIF5B, GTPase HflX, GTPase-activating protein, guanine triphosphatase, guanine-nucleotide-exchange factor of eIF2, guanosine 5'-triphosphatase, guanosine triphosphatase, HflX, HflX GTPase, IF-2, IF1, IF2, IF2 GTPase, IF2alpha, IF3, IF5B, infB, initiation factor (IF), initiation factor 2, initiation factor 3, initiation factor 5B, initiation factor aIF5B, initiation factor-2, L10, L11, L12, LepA, mitochondrial elongation factor G, mitochondrial initiation factor 2, peptide-release or termination factor, protein-synthesizing GTPase, protein-sythesizing GTPase, RF3, ribosomal GTPase, ribosome-bound initiation factor 2, ribosome-dependent GTPase, SelB, selenocysteine tRNA-specific elongation factor, signal recognition particle GTPase Ffh, SRP GTPase Ffh, Ss-aIF2, SsEF-1alpha, SsEF-2, SsGBP, SSO0269, SSO0412, SSO1050, SSO2381, SsoHflX, translation elongation factor 2, translation factor aIF2/5B, translation initiation factor, translation initiation factor 2, translation initiation factor 2 gamma, translation initiation factor 5B, translation initiation factor eIF5, translation initiation factor IF1, translation initiation factor IF2, translation termination factor eRF3, translational GTPase, translational guanosine triphosphatase, translational initiation factor 2, trGTPase, Tt-L11, ymIF2
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3.6.5.3 protein-synthesizing GTPaseAdvanced search results
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Engineering on EC 3.6.5.3 - protein-synthesizing GTPase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
P269S
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variant is expressed to a high level in Escherichia coli. The variant functions as effectively as the respective wild-type factor in ternary complex formation using Escherichia coli Phe-tRNAPhe and Cys-tRNACys. The variant is also active in A-site binding and in vitro translation assay with Escherichia coli Phe-tRNAPhe
A421(insGly)G422
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mutation causes cold-sensitivity in the organism. No GTPase activity below 10°C and reduced activity at all temperatures up to 45°C, as compared to wild-type enzyme
D138N
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mutant with decreased affinity for GDP and increased affinity for XDP
D409E
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mutation causes cold-sensitivity in the organism. No GTPase activity below 10°C and reduced activity at all temperatures up to 45°C, as compared to wild-type enzyme
E571K
F94L
site-directed mutagenesis, the mutant shows GTP hydrolysis kinetics similar to the wild-type
G83A
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mutation slows down the association of the ternary complex EF-Tu/GTP/aminoacyltRNA with the ribosome and abolishes the ribosome-induced GTPase activity of EF-Tu
G83A/G94A
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mutation slows down the association of the ternary complex EF-Tu/GTP/aminoacyltRNA with the ribosome and abolishes the ribosome-induced GTPase activity of EF-Tu
G94A
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mutation strongly impairs the conformational change of EF-Tu from the GTP-bound to the GDP-bound form and decelerates the dissociation of EF-Tu/GDP from the ribosome
H448S
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site-directed mutagenesis, a dominant-lethal substitution, the expression of the mutant causes a rapid growth arrest and a reduction in the number of viable cells by 3 or 4 orders of magnitude within 20-30 min after induction
H448S/E571K
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site-directed mutagenesis, induction of the GTPase-deficient double mutant affects neither the growth of the cells nor the viable counts demonstrating that the E571K mutation is capable of suppressing lethality of the dominant-lethal H448S substitution
H81A
H84A
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reduces the rate constant of GTP hydrolysis more than 1000000fold, the preceding steps of ternary complex binding to the ribosome, codon recognition and the GTPase activation step are affected only slightly. The catalytic role of His84 in elongation factor Tu is to stabilize the transition state of GTP hydrolysis by hydrogen bonding to the attacking water molecule or, possibly, the gamma-phosphate group of GTP
H91A
H91E
site-directed mutagenesis, the mutant shows defective ribosome associated GTP hydrolysis and inorganic phosphate release
H91Q
site-directed mutagenesis, the mutant is defective in inorganic phosphate release
H91R
site-directed mutagenesis, the mutant shows defective ribosome associated GTP hydrolysis and inorganic phosphate release
Q290L
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3-5fold more active in polymerization than wild-type Escherichia coli EF-Tu, 10fold increase in GTPase activity compared to wild-type enzyme
S221P
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variant is poorly expressed and the majority of molecules fail to fold into an active conformation. The variant functions as effectively as the respective wild-type factor in ternary complex formation using Escherichia coli Phe-tRNAPhe and Cys-tRNACys. The variant is also active in A-site binding and in vitro translation assay with Escherichia coli Phe-tRNAPhe
D138N
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mutant with decreased affinity for GDP and increased affinity for XDP
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D80N
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mutant with decreased affinity for GTP and increased GTPase activity
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E424K
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random mutagenesis, the IF2-G3 domain mutant shows a reduced affinity for the 30S ribosomal subunit, the mutant shows complete loss of GTPase activity
G378C
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more stable binding within the 70S initiation complex of Bst-IF2*GDP
G420E
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random mutagenesis, the mutant shows a reduced affinity for both ribosomal subunits
S387P
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random mutagenesis, the mutant shows a reduced affinity for the 30S ribosomal subunit
A26G
D19A
site-directed mutagenesis, the mutation does not strongly modify the GDP binding properties of the two mutant enzyme, but reduces the GTP hydrolysis rate
D19A/H97A
site-directed mutagenesis, almost inactive mutant
G13A
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compared to wild-type enzyme the mutant shows a reduced rate of Phe polymerization and a reduced intrinsic GTPase activity that is stimulated by high concentrations of NaCl. Mutant enzyme shows an increased affinity for GTP and GDP. The temperature inducing a 50% denaturation of the mutant enzyme is 5°C lower than that of the wild-type enzyme
H97A
site-directed mutagenesis, the mutation does not strongly modify the GDP binding properties of the two mutant enzyme, but reduces the GTP hydrolysis rate
Y54H
the mutant of isoform EF-1beta shows wild type activity
D19A
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site-directed mutagenesis, the mutation does not strongly modify the GDP binding properties of the two mutant enzyme, but reduces the GTP hydrolysis rate
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D19A/H97A
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site-directed mutagenesis, almost inactive mutant
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H97A
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site-directed mutagenesis, the mutation does not strongly modify the GDP binding properties of the two mutant enzyme, but reduces the GTP hydrolysis rate
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D19A
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site-directed mutagenesis, the mutation does not strongly modify the GDP binding properties of the two mutant enzyme, but reduces the GTP hydrolysis rate
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H97A
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site-directed mutagenesis, the mutation does not strongly modify the GDP binding properties of the two mutant enzyme, but reduces the GTP hydrolysis rate
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D19A
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site-directed mutagenesis, the mutation does not strongly modify the GDP binding properties of the two mutant enzyme, but reduces the GTP hydrolysis rate
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D19A/H97A
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site-directed mutagenesis, almost inactive mutant
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H97A
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site-directed mutagenesis, the mutation does not strongly modify the GDP binding properties of the two mutant enzyme, but reduces the GTP hydrolysis rate
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D19A
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site-directed mutagenesis, the mutation does not strongly modify the GDP binding properties of the two mutant enzyme, but reduces the GTP hydrolysis rate
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H97A
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site-directed mutagenesis, the mutation does not strongly modify the GDP binding properties of the two mutant enzyme, but reduces the GTP hydrolysis rate
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A208V
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suppressor mutation to rescue growth defect associated with N135D mutation
A219T
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suppressor mutation to rescue growth defect associated with N135D mutation, as single mutant slow-growth phenotype
A382V
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suppressor mutation to rescue growth defect associated with N135D 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/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
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double mutant, suppression of H480I-mutant mediated slow yeast cell growth
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
A208V
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suppressor mutation to rescue growth defect associated with N135D mutation
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A382V
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suppressor mutation to rescue growth defect associated with N135D mutation
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H480I/F643R
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double mutant, suppression of H480I-mutant mediated slow yeast cell growth
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H480I/I634G
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double mutant, suppression of H480I-mutant mediated slow yeast cell growth
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A375T
additional information
E571K
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site-directed mutagenesis, the mutation in the 30S binding domain IF2-G3 disrupts hydrogen bonding between subdomains G2 and G3, so that IF2 acquires a GDP-like conformation and is no longer responsive to GTP binding. The mutant has a 6.5fold reduced affinity for the 30S subunit and is completely inactive in ribosome-dependent GTP hydrolysis. The IF2 E571K mutant is active in 30S initiation complex and initiation dipeptide formation, and supports faithful mRNA translation
E571K
the IF2alpha mutant has a completely inactivated GTPase activity
H91A
site-directed mutagenesis, the mutant shows defective ribosome associated GTP hydrolysis and inorganic phosphate release
H91A
the mutant of EF-G renders the enzyme impaired in GTP hydrolysis and thereby stabilizes it on the ribosome
A26G
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converts the guanine nucleotide binding consensus sequences A-X-X-X-X-G-K-[T,S] of the elongation factor EF-2 into the corresponding G-X-X-X-X-G-K-[T,S] motif which is present in all the other GTP-binding proteins. In the mutant, the rate of poly(U)-directed poly(Phe) synthesis and the ribosome-dependent GTPase activity of A26GSsEF-2 are decreased. A26G substitution enhances the catalytic efficiency of the intrinsic SsEF-2 GTPase triggered by ethylene glycol and decreases the affinity for GDP
A26G
the mutant of isoform EF-2 shows increased wild type activity
A375T
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resistance to kirromycin, abolished streptomycin resistance of mutants of ribosomal protein S12
A375T
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resistance to kirromycin, abolished streptomycin resistance of mutants of ribosomal protein S12
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additional information
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Snowy cotyledon 1 mutant contains a mutation in a gene encoding the chloroplast elongation factor G, leading to an amino acid exchange within the predicted 70S ribosome-binding domain. The mutation results in a delay in the onset of germination. At this early developmental stage embryos still contain undifferntiated proplastids, whose proper function seems necessary for seed germination. In light-gropwn sco1 seedlings the greening of cotyledons is severely impaired, whereas the following true leaves develop normally as in wild-type plants
additional information
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used as a hybrid sytem with Thermus thermophilus ribsomal protein L11
additional information
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GTPase null mutant E424K of Bacillus stearothermophilus can replace in vivo wild-type IF2 allowing the Escherichia coli infB null mutant to grow with almost wild-type duplication times
additional information
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two EF-G cysteine mutants 58C and 196C react efficiently with 2',7'-difluorofluorescein maleimide, whereas the cysteine-free protein is unreactive
additional information
generation of C-terminal domain truncation mutants of the enzyme, truncation of the C-terminal domain does not abolish ribosome binding, the mutant enzyme is stabilized on the ribosome when the C-terminal domain is removed. Binding of wild-type EF4 and mutant variants to the ribosome in the presence of guanine nucleotides, kinetics and affinities
additional information
construction of a IF2alphaDELTA GTPase mutant with abolished GTPase activity
additional information
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construction of a IF2alphaDELTA GTPase mutant with abolished GTPase activity
additional information
intrinsic GTP hydrolysis by EF-G is unaffected by the H91 and F94 mutations. H91 mutated EF-Gs show different degrees of defect in ribosome-stimulated GTP hydrolysis. H91 mutants show larger defects in Pi release than in GTP hydrolysis
additional information
the DELTAlepA mutation is introduced via Hfr-mediated conjugation into each strain of the Keio collection, mutation DELTAlepA confers a synthetic growth defect in the absence of RsgA, a conserved GTPase known to be involved in SSU biogenesis. Mutation DELTArsgA slows the growth of Escherichia coli substantially, increasing the doubling time by 18 min. The growth defect is rescued by plasmid pRSGA, which contains the rsgA gene and its native promoter region, confirming that loss of RsgA is responsible for the phenotype. Precursor 17S rRNA accumulates in pre-30S and 30S particles in the absence of LepA, phenotype overview
additional information
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GTPase null mutant E424K of Bacillus stearothermophilus can replace in vivo wild-type IF2 allowing the Escherichia coli infB null mutant to grow with almost wild-type duplication times
additional information
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comparison of sequence with that of Sulfolobus solfataricus strain MT4 shows only one amino acid change, i.e. I15V. The difference is in the first guanine nucleotide binding consensus sequence G13HIDHGK and is responsible for a increased efficiency in protein synthesis, which is accompanied by an reduced affinity for both guanosine diphosphate (GDP) and guanosine triphosphate (GTP), and an decreased efficiency in the intrinsic GTPase activity. The exchange has only very marginal effects on the thermal properties of the enzyme
additional information
comparison of sequence with that of Sulfolobus solfataricus strain MT4 shows only one amino acid change, i.e. I15V. The difference is in the first guanine nucleotide binding consensus sequence G13HIDHGK and is responsible for a increased efficiency in protein synthesis, which is accompanied by an reduced affinity for both guanosine diphosphate (GDP) and guanosine triphosphate (GTP), and an decreased efficiency in the intrinsic GTPase activity. The exchange has only very marginal effects on the thermal properties of the enzyme
additional information
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comparison of sequence with that of Sulfolobus solfataricus strain MT4 shows only one amino acid change, i.e. V15I. The difference is in the first guanine nucleotide binding consensus sequence G13HIDHGK and is responsible for a reduced efficiency in protein synthesis, which is accompanied by an increased affinity for both guanosine diphosphate (GDP) and guanosine triphosphate (GTP), and an increased efficiency in the intrinsic GTPase activity. The exchange has only very marginal effects on the thermal properties of the enzyme
additional information
comparison of sequence with that of Sulfolobus solfataricus strain MT4 shows only one amino acid change, i.e. V15I. The difference is in the first guanine nucleotide binding consensus sequence G13HIDHGK and is responsible for a reduced efficiency in protein synthesis, which is accompanied by an increased affinity for both guanosine diphosphate (GDP) and guanosine triphosphate (GTP), and an increased efficiency in the intrinsic GTPase activity. The exchange has only very marginal effects on the thermal properties of the enzyme
additional information
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construction of truncated forms corresponding to the putative domains G+M, and domain G. Neither truncated form is able to sustain poly(Phe) synthesis but they are able to bind guanine nucleotides with an affinity much higher with respect to that of the intact factor. Kinetic data are not changed by the truncation, but both forms are less thermostable than the intact factor and both are no more sensitive to the stimulatory effect of elongation factor 1beta
additional information
the N-terminal deletion mutant displays a similar Km value as the wild-type enzyme whereas the substrate kcat is 24fold increased
additional information
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the N-terminal deletion mutant displays a similar Km value as the wild-type enzyme whereas the substrate kcat is 24fold increased
additional information
mutant gamma subunit structure determination and analysis, and comparison to the wild-type gamma subunit structure, GTP binding structures, overview
additional information
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mutant gamma subunit structure determination and analysis, and comparison to the wild-type gamma subunit structure, GTP binding structures, overview
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additional information
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mutant gamma subunit structure determination and analysis, and comparison to the wild-type gamma subunit structure, GTP binding structures, overview
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additional information
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mutant gamma subunit structure determination and analysis, and comparison to the wild-type gamma subunit structure, GTP binding structures, overview
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additional information
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mutant gamma subunit structure determination and analysis, and comparison to the wild-type gamma subunit structure, GTP binding structures, overview
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additional information
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the N-terminal deletion mutant displays a similar Km value as the wild-type enzyme whereas the substrate kcat is 24fold increased
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additional information
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inherited mutations cause fatal brain disorder: childhood ataxia with central nervous system hypomyelination, leukoencephalopathy with vanishing white matter, eIF2B-related disorders
additional information
inherited mutations cause fatal brain disorder: childhood ataxia with central nervous system hypomyelination, leukoencephalopathy with vanishing white matter, eIF2B-related disorders
additional information
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mutations in subunit beta destabilize interaction between eIF2, eIF1A, eIF3 and eIF5
additional information
mutations in subunit beta destabilize interaction between eIF2, eIF1A, eIF3 and eIF5
additional information
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mutant of elongation factor G containing the effector loop from Thermus aquaticus EF-Tu has markedly decreased GTPase activity and does not catalyze translocation. The loops are not functionally interchangeable since the factors interact with different states of the ribosome
additional information
point mutations of the common key residues that are potentially important for mediating the inter-lobe communications can substantially disrupt the couplings around the nucleotide binding regions in EF-Tu
additional information
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mutant of elongation factor G containing the effector loop from Thermus aquaticus EF-Tu has markedly decreased GTPase activity and does not catalyze translocation. The loops are not functionally interchangeable since the factors interact with different states of the ribosome
additional information
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used as a hybrid sytem with Escherichia coli ribsomal proteins L10, L11, L12
