Information on EC 3.6.5.3 - protein-synthesizing GTPase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
3.6.5.3
-
RECOMMENDED NAME
GeneOntology No.
protein-synthesizing GTPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP + H2O = GDP + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
hydrolysis of phosphoric ester
additional information
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
NIL
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
gene lepA
-
-
Manually annotated by BRENDA team
Escherichia coli DH5-alpha
strain DH5alpha
-
-
Manually annotated by BRENDA team
strain HW110, EF-Tu (wt) and EF-Tu (138N)
-
-
Manually annotated by BRENDA team
strain N4830, elongation factor EF-Tu (wt) and EF-Tu (D80N)
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
elongation factor (EF)Tu
-
-
Manually annotated by BRENDA team
Pleodorina sp.
-
-
-
Manually annotated by BRENDA team
strain 8830, elongation factor EF-Tu
-
-
Manually annotated by BRENDA team
strain 8830, elongation factor EF-Tu
-
-
Manually annotated by BRENDA team
elongation factor (EF)Tu
-
-
Manually annotated by BRENDA team
EF-3
-
-
Manually annotated by BRENDA team
strain J293
-
-
Manually annotated by BRENDA team
strain NOY891
UniProt
Manually annotated by BRENDA team
EF-3
-
-
Manually annotated by BRENDA team
elongation factor (EF)Tu
-
-
Manually annotated by BRENDA team
elongation factor (EF)Tu
-
-
Manually annotated by BRENDA team
elongation factor (EF)Tu
-
-
Manually annotated by BRENDA team
elongation factor (EF)Tu
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain JC469, JC496, JC 499, JC503
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-
Manually annotated by BRENDA team
wheat germ translation factor 2 (WgeIF-2)
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
-
universal mechanism for GTPase activation and hydrolysis in translational GTPases on the ribosome
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2',3'-O-N'-methylanthranilate-GTP + H2O
2',3'-O-N'-methylanthranilate-GDP + phosphate
show the reaction diagram
-
2',3'-O-N'-methylanthranilate, i.e. mant, is attached to GTP. EF-G binds and efficiently hydrolyzes mant-GTP in a ribosome-dependent manner
-
-
?
8-azido-GTP + H2O
8-azido-GDP + phosphate
show the reaction diagram
ATP + H2O
ADP + phosphate
show the reaction diagram
aurodox + H2O
?
show the reaction diagram
-
-
-
?
GDP + H2O
?
show the reaction diagram
GTP + H2O
?
show the reaction diagram
GTP + H2O
GDP + phosphate
show the reaction diagram
GTP gamma-(p-azido)anilide + H2O
GDP + phosphoric acid p-azidoanilin
show the reaction diagram
-
-
-
?
guanosine 5'-(thio)triphosphate + H2O
GDP + thiophosphate + 3 H+
show the reaction diagram
guanylyl imidodiphosphate + H2O
?
show the reaction diagram
ITP + H2O
IDP + phosphate
show the reaction diagram
XDP + H2O
XMP + phosphate
show the reaction diagram
XTP + H2O
XDP + phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
GDP + H2O
?
show the reaction diagram
GTP + H2O
GDP + phosphate
show the reaction diagram
guanosine 5'-(thio)triphosphate + H2O
GDP + thiophosphate + 3 H+
show the reaction diagram
guanylyl imidodiphosphate + H2O
?
show the reaction diagram
ITP + H2O
IDP + phosphate
show the reaction diagram
XDP + H2O
XMP + phosphate
show the reaction diagram
XTP + H2O
XDP + phosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
enzyme IF2 does not have an identified nucleotide exchange factor
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
BaCl2
-
10 mM, about 8fold stimulation
CaCl2
-
10 mM, highest stimulation by BaCl2 (8fold), followed by SrCl2, MgCl2, MnCl2, CaCl2 and CoCl2 in a decreasing order of effectiveness
CoCl2
-
10 mM, highest stimulation by BaCl2 (8fold), followed by SrCl2, MgCl2, MnCl2, CaCl2 and CoCl2 in a decreasing order of effectiveness
MgCl2
-
10 mM, highest stimulation by BaCl2 (8fold), followed by SrCl2, MgCl2, MnCl2, CaCl2 and CoCl2 in a decreasing order of effectiveness
MnCl2
-
10 mM, highest stimulation by BaCl2 (8fold), followed by SrCl2, MgCl2, MnCl2, CaCl2 and CoCl2 in a decreasing order of effectiveness
NaCl
-
GTPase activity is measured in the presence of 3.6 M NaCl
SrCl2
-
10 mM, highest stimulation by BaCl2 (8fold), followed by SrCl2, MgCl2, MnCl2, CaCl2 and CoCl2 in a decreasing order of effectiveness
Zn2+
-
zinc-binding domain in the beta-subunit
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Adenyl-5'-yl imidodiphosphate
Anti-EF-Tu antibody
-
-
-
Anti-Ndk antibody
-
-
-
Chloramphenicol
-
-
dihydrostreptomycin
-
-
EF-G GTPase inhibitor
-
-
-
enacylotoxin IIa
Fusidic acid
GDP gamma-S
-
-
GE2270A
-
antibiotic inhibits intrinsic GTPase and that stimulated by ribosomes; thiazolyl-peptide antibiotic, inhibits both the intrinsic GTPase of elongation factor 1alpha and that stimulated by ribosomes. The M domain is the region of the enzyme most responsible for the interaction with GE2270A
GTPgammaS
-
-
guanidine hydrochloride
-
deactivation by denaturation of the protein
guanosine 5'-(beta,gamma-imido)triphosphate
-
-
guanosine 5'-tetraphosphate
-
competitive inhibition of intrinsic GTPase, inhibition of archaeal protein synthesis in vitro, even though the concentration required to get inhibition is higher than that required for the eubacterial and eukaryal systems
guanosine-5'-[(beta,gamma)-imido]triphosphate
-
i.e. GppNHp. GTPase activity in the presence of a molar concentration of NaCl is competitively inhibited
guanyl-5'-yl imidodiphosphate
guanyl-5'-yl imidotriphosphate
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-
guanyl-5'yl-imidodiphosphate
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-
hygromycin A
-
-
N-ethylmaleimide
neamine
-
-
neomycin B
-
-
NH4Cl
-
at higher concentration
P3-1-(2-nitro)phenylethylguanosine 5'-O-triphosphate
-
-
pulvomycin
purine and pyrimidine nucleotides
ribostamycin
-
-
sparsomycin
-
-
spermidine
-
2mM
streptogramin A
-
-
tetracyclin
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-
tetracycline
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mixed inhibition. The inhibition level depends on the antibiotic concentration, even though a complete inhibition is not reached even in the presence of 0.120 mM antibiotic, a concentration corresponding to about 200fold molar excess over the elongation factor
Thiostrepton
translation initiation factor IF1
-
-
-
translation initiation factor IF3
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inhibition could be overcome by increasing concentrations of divalent cations
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Urea
-
deactivation by denaturation of the protein
vanadate
viomycin
-
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-propanol
-
stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
2-propanol
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stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
50S ribosome
stimulates the enzyme
-
70S ribosome
required, stimulates the enzyme
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bluensomycin
-
-
ethanol
-
stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
ethylene glycoI
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60%, 300fold stimulation
-
gentamicin C1
-
-
gentamicin C1a
-
-
glycerol
-
stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
hygromycin
-
-
kanamycin A
-
-
kanamycin B
-
-
kirromycin
L7/12
-
functional compatibility between elongation factor G and the L7/12 protein in the ribosome governs its translational specificity; the C-terminal domian of L7/12 is responsible for EF-Tu function. Functional compatibility between elongation factor Tu and the L7/12 protein in the ribosome governs its translational specificity
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methanol
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stimulation by aliphatic alcohols in a decreasing order of effectiveness: ethylene glycol > 2-propanol > ethanol > glycerol > methanol > 1-propanol
neomycin C
-
-
paromycin
-
-
pulvomycin
-
increasing pulvomycin concentration increased the rate of the intrinsic GTPase catalysed by elongation factor 1alpha, reaching its maximum stimulation effect at 30 mM. Pulvomycin exerts its stimulatory function at all the tested temperatures (45-75C).
ribosomal subunits
ribosome
sisomicin
-
-
streptomycin
tobramycin
-
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12 - 0.2
ATP
0.00032 - 0.27
GTP
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0004 - 8.8
GTP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007 - 177
GTP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00012 - 0.0074
GDP
0.0084 - 0.0407
guanosine 5'-(beta,gamma-imido)triphosphate
0.00047
guanosine-5'-[(beta,gamma)-imido]triphosphate
-
pH 7.8, 50C, GTPase activity in the presence 3.6 M NaCl
0.0084 - 0.0407
guanyl-5'-yl imidotriphosphate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0059 - 0.0463
GE2270A
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32
-
GTPase activity of domain 1
38
-
GTPase activity of domain 1 fused to domain 2+3
61
-
GTPase activity of domain 1 fused to domain 2+3
90
-
wild-type enzyme
additional information
-
the rate of nucleotide binding to aEF-1 a increased with temperature, reaching a maximum at 95C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70 - 86
-
about 60% of maximal activity at 70C and at 86C, mutant enzyme G13A
70 - 95
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70C: about 60% of maximal activity, 95C: about 90% of maximal activity, wild-type enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.1
-
isoelectric focusing, pH-gradient 3-10
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
truncated G-form of SsEF-1alpha, determined by SDS-PAGE and Western blot
38000
-
truncated GM-form of SsEF-1alpha, determined by SDS-PAGE and Western blot
45000
-
SDS-PAGE
50000
-
SDS-PAGE
58000
-
SDS-PAGE
95000
-
gel filtration
120000
-
SDS-PAGE
150000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heteropentamer
alphabetagammadeltaepsilon
monomer
pentamer
-
-
tetramer
trimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
proteolytic modification
side-chain modification
additional information
-
differently from the wild-type enzyme the recombinant enzyme does not undergo post-translational modification of His603 into diphthamide, as indicated by its inability to be ADP-ribosylated
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, crystal structure of elongation factor Tu*Ts complex at 2.2 A resolution
-
two crystal forms of a complex between trypsin-modified elongation factor Tu-MgGDP and the antibiotic tetracycline solved by X-ray diffraction analysis to resolution of 2.8 and 2.1 A, respectively
-
hanging-drop vapour-diffusion method
-
vapour-diffusion method from ammonium sulfate either in the presence of GDP, GppHNp or without nucleotide, yielding isomorphous crystals for all three forms
-
crystal structure analysis of enzyme complexed with the GTP analogue GDPNP and with GDP at 2.0 A resolution , PDB IDs 1G7T and 1G7S, enzyme in complex with GTP/Mg2+, modeling and molecular dynamics simulations
-
crystal structure of the regulatory subunit aIF2Balpha, hanging-drop vapour diffusion method at 20C, three-dimensional structure is determined by X-ray crystallography at 2.2 A resolution
-
5 A resolution crystal structure of the ternary complex formed by archaeal aIF2 from Sulfolobus solfataricus, the GTP analog GDPNP and methionylated initiator tRNA
Q97W59 and Q980A5 and Q97Z79
analysis of crystal structures of ON and OFF aIF2 at resolution of 3.0 and 2.15 A
-
crystal structure analysis, overview
-
crystal structure of HflX from Sulfolobus solfataricus solved to 2.0 A resolution in apo- and GDP-bound forms
-
crystals of wild-type enzyme/GDP comple and mutant enzymes G235P and G235S are grown using hanging drop method at 16C
-
elongation factor 1alpha in complex with GDP, structure at 1.8 A resolution
-
elongation factor 1alpha in complex with Mg2+ (100 mM) and GDP. Elongation factor 1alpha in complex with GDP does not bind Mg2+, when the ion is present in the crystallization medium at moderate concentrations (5 mM). Crystals are grown using PEG 4000 and propan-2-ol as precipitants. Diffraction quality crystals are obtained using microbatch under oil technique at 4C and a protein concentration of 6 mg/ml
-
Fourier transform infrared spectroscopic study. Substitution of the GDP bound with guanyl-5'-yl imido diphosphate induces a slight increase in the alpha helix and beta sheet content. The alpha helix content of the enzyme-GDP complex increases upon addition of salts, and the highest effect is produced by 5 M NaCl. Thermal stability of the enzyme-GDP complex is significantly reduced when the GDP is replaced with guanyl-5'-yl imido diphosphate or in the presence of NaBr or NH4Cl
-
full-sized alphabetagamma heterotrimeric aIF2 in the nucleotide-free form, and aIF2alphagamma dimer, X-ray diffraction structure determination and analysis at 2.8 A resolution
-
crystal structure of the Mg2+-GDP complex of the Ffh NG-domain refined at 2.1 resolution
-
EF-Tu bound to aminoacyl-tRNA of the 70s ribosome and a GTP analogue, X-ray diffraction structure determination and analysis at 3.1 A resolution
-
purified recombinant apo-enzyme IF2 and its complex with GDP, vapor diffusion, mixing of 25 mg/ml protein in 30 mM HEPES-KOH, pH 7.5, 10 mM MgCl2, 30 mM NH4Cl, 1 mM EDTA NaOH, and 1 mM 2-mercaptoethanol in a 4:1 ratio with a well solution contaning 0.1 M calcium acetate, 0.04 M Na-cacodylate, pH 5.4, 8% w/v PEG 8000, 10-30 mM glycl-glycine, and 10-30 mM taurine, 2 weeks, X-ray diffraction structure determination and analysis aat 3.09 A resolution
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purified recombinant apoenzyme protein core and enzyme in complex with GTP or GDP, sitting-drop vapour diffusion method, mixing of protein in 20 mM HEPES, pH 7.5, 50 mM KCl, 20 mM MgCl2, 1 mM DTT, with 2.5% glycerol and with reservoir solution containing 20% PEG 3350 and 0.2 M ammonium nitrate, to a final volume of 0.008 ml, 21C, 1-3 weeks, X-ray diffraction structure determination and analysis
-
structure of the mutant enzyme T84A in complex with the non-hydrolysable GTP analogue GDPNP
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 100
-
EF-1alpha denaturation profile at pH 4.0, the protonation state of the numerous Asp and Glu residues plays a critical role for the thermally denatured state of the enzyme, reversibility of the inter-conversion between the two denatured forms, overview
87 - 96
-
half-inactivation time 99 min at 87C, half-inactivation time 3.5 min at 96C
87
-
half-denaturation of mutant enzyme G13A
91
-
10 min, 50% inactivation of GDP binding ability, mutant enzyme G13A
92
-
half-denaturation of wild-type enzyme
93.6
-
temperature for half denaturation of D60A mutant
94
-
10 min, 50% inactivation of GDP binding ability, wild-type enzyme
95
-
10 min, 50% inactivation
95.1
-
temperature for half denaturation
96
-
binding of guanosine 5'-tetraphosphate to SsEF-1alpha renders the elongation factor more resistant to heat treatment. The denaturation profile of the elongation factor in the presence of guanosine tetraphosphate is shifted towards higher temperatures with a denaturation midpoint (96.4C) about 2C higher with respect to that observed for the elongation factor bound to GDP
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
conformational change of the elongation factor takes place upon interaction with the antibiotic. Protection against chemical denaturation of SsEF-1alpha is observed in the presence of pulvomycin
-
EF-Tu(138N) not functional in vivo
-
eIF2A is an inherently unstable protein with a half-life of about 17 min
-
mutants lethal to E. coli
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Glycerol
guanidine-HCl
-
50% inactivation of GTPase activity at 3.0 M guanidine-HCl in presence 3.6 M NaCl and absence of pulvomycin. 50% inactivation of GTPase activity at 3.6 M guanidine-HCl in presence 3.6 M NaCl and presence of pulvomycin
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 20 mM Tris/HCl, pH 7.8, 50 mM KCl, 10 mM MgCl2, 50% v/v glycerol
-
-20C, stable for several months
-
-20C, Tris/HCl buffer, pH 7.8, 10 mM MgCl2, 50 mM KCl, 50% v/v glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE Sephadex A-50 column
-
purified as a complex with GDP
-
recombinant C2 subdomain of ymIF2
-
recombinant EF-G mutants 58C and 196C
-
recombinant enzyme from Escherichia coli by heat treatment at 65C for 20 min, ultracentrifugation, hydrophobic interaction chromatography, gel filtration, and ultrafiltration
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chhrmatography and gel filtration
recombinant wild-type and selenomethionine-labelled enzymes from Escherichia coli by hydrophobic interaction chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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; 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 gene encoding SsEF-1alpha from the strain MT3 is cloned, sequenced and expressed in Escherichia coli, the vectors pGEM-3Z and pET22 are used
expression in Escherichia coli
expression in Escherichia coli BL21
expression in Escherichia coli using the pT7-7 expression vector
-
expression in Escherichia coli; the SsEF-1alpha gene is cloned into the pT7-7 vector for expression in Escherichia coli BL21DE3 cells, in addition two truncated forms of SsEF-1alpha are constructed, encoding the domain G and the domains G+M
-
for expression in Escherichia coli cells
-
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
-
gene lepA, recombinant overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
high level expression of mutant enzyme P269S in Escherichia coli
-
His-tagged version of ymIF2 lacking its predicted mitochondrial presequence is expressed in Escherichia coli
-
mutant enzyme Q290L, expression in Escherichia coli
-
overexpression of all three subunits of human eIEF2 independently, and together in Sf9 cells using pFast Bac HT vector of baculovirus expression system. the expression of all subunits increases in infection time up to 72 h. Expression of the mutant forms S51A, S51D and S48A
-
recombinant expression in Escherichia coli strain BL21(DE3)
-
recombinant expression of EF-G mutants 58C and 196C
-
recombinant expression of nontagged wild-type full-length enzyme in Escherichia coli strain BL21(DE3) and of selenomethionine-labelled enzyme in Escherichia coli strain B834 (DE3)
-
recombinant SsEF-1alpha and its nucleotide-free form are prepared by using an Escherichia coli expression system
-