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D286C
-
t1/2 at room temperature is 16 min, compared to 12 min for wild-type enzyme. 71% of the wild-type phosphatase activity
E257C
-
t1/2 at room temperature is 30 min, compared to 12 min for wild-type enzyme. 31% of the wild-type phosphatase activity
E261C
-
t1/2 at room temperature is 15 min, compared to 12 min for wild-type enzyme. 77% of the wild-type phosphatase activity
E268C
-
t1/2 at room temperature is 23 min, compared to 12 min for wild-type enzyme. 45% of the wild-type phosphatase activity
E275C
-
t1/2 at room temperature is 28 min, compared to 12 min for wild-type enzyme. 34% of the wild-type phosphatase activity
E276C
-
t1/2 at room temperature is 68 min, compared to 12 min for wild-type enzyme. 5% of the wild-type phosphatase activity
E282C
-
t1/2 at room temperature is 15 min, compared to 12 min for wild-type enzyme. 77% of the wild-type phosphatase activity
F43I
site-directed mutagenesis, the mutation results in a slightly reduced growth defect compared to the construct in which all interface binding site residues are mutated
G240C
-
t1/2 at room temperature is 10 min, compared to 12 min for wild-type enzyme. 123% of the wild-type phosphatase activity
G264C
-
t1/2 at room temperature is 12 min, compared to 12 min for wild-type enzyme. As active as wild-type enzyme
H153F
mutation in periplasmic arm, mutant does not show any detectable activity above background at pH 7 or pH 5.6
H176A
site-directed mutagenesis, the mutation results in the same growth defects as the construct in which all interface binding site residues are mutated
H226A
mutant can be induced at low pH
H226L
mutant cannot be induced at low pH
H226N
mutant cannot be induced at low pH
H226Q
mutant cannot be induced at low pH
H226Q/S600I
level of activity at pH 7 is very similar to that of EvgS S600I and mutant is inducible at pH 5.6
H226T
mutant cannot be induced at low pH
H226V
mutant cannot be induced at low pH
H226W
mutant cannot be induced at low pH
H243K
-
inactive mutant protein
H243N
-
inactive mutant protein
H243S
-
inactive mutant protein
H243V
-
inactive mutant protein
H243X
the His residue at position 243 of the EnvZ protein is changed by means of site-directed mutagenesis. The mutant EnvZ protein is defective in its in vitro ability not only as to EnvZ-autophosphorylation but also OmpR-phosphorylation and OmpR-dephosphorylation. This particular mutant EnvZ protein seems to exhibit null functions as to the in vivo osmoregulatory phenotype
H243Y
-
inactive mutant protein
H248A
-
mutation abrogates autophosphorylation by disrupting the phosphorylation site in the DHp domain
H248A/N356K
-
mutation abrogates autophosphorylation
H398L
-
the mutant retains itscapability to bind ATP and is competent to catalyze the transphosphorylation of an AtoS G-box (G565A) mutant protein which otherwise fails to autophosphorylate due to its inability to bind ATP
H42A
site-directed mutagenesis, the mutation results in the same growth defects as the construct in which all interface binding site residues are mutated
H63A
noninducible mutant, no protein is detected
H63Q/H106Q/H124Q
mutations in potential His triad, mutant shows the same level of induction as the wild-type EvgS
K152A
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows moderate activation by KCl-supplemented M9 medium, pH 5.5
K152E
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows strong activation by KCl-supplemented M9 medium, pH 5.5
K152F
naturally occuring mutation and site-directed mutagenesis, in the mutant, EvgS activation is observed only by complementation with pBADevgS, mutation L152F leads to the desensitization of EvgS in strain KMY1. The mutant shows no activation by KCl-supplemented M9 medium, pH 5.5. The L152F mutation is found in only two Escherichia coli strains, MC4100 and DH1
K152I
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows strong activation by KCl-supplemented M9 medium, pH 5.5
K152R
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows moderate activation by KCl-supplemented M9 medium, pH 5.5
K152Y
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows no activation by KCl-supplemented M9 medium, pH 5.5
K272C
-
t1/2 at room temperature is 55 min, compared to 12 min for wild-type enzyme. 10% of the wild-type phosphatase activity
L152F/S600I
level of activity at pH 7 is very similar to that of EvgS S600I and mutant is inducible at pH 5.6
L236C
-
t1/2 at room temperature is 25 min, compared to 12 min for wild-type enzyme. 40% of the wild-type phosphatase activity
L254C
-
inactive mutant enzyme, t1/2 at room temperature is 90 min, compared to 12 min for wild-type enzyme
N248A
site-directed mutagenesis, the mutation activates the enzyme
N248D
site-directed mutagenesis, the mutation activates the enzyme
N248G
site-directed mutagenesis, the mutation activates the enzyme
N271C
-
t1/2 at room temperature is 36 min, compared to 12 min for wild-type enzyme. 23% of the wild-type phosphatase activity
N278C
-
t1/2 at room temperature is 45 min, compared to 12 min for wild-type enzyme. 15% of the wild-type phosphatase activity
N356K
-
mutation abrogates autophosphorylation by disrupting the ATP-binding site in the CA domain
P522A/S600I
level of activity at pH 7 is very similar to that of EvgS S600I and mutant is inducible at pH 5.6
Q262C
-
t1/2 at room temperature is 11 min, compared to 12 min for wild-type enzyme. 111% of the wild-type phosphatase activity
Q283C
-
t1/2 at room temperature is 13 min, compared to 12 min for wild-type enzyme. 91% of the wild-type phosphatase activity
R246C
-
t1/2 at room temperature is 62 min, compared to 12 min for wild-type enzyme. 7% of the wild-type phosphatase activity
S242C
-
t1/2 at room temperature is 39 min, compared to 12 min for wild-type enzyme. 20% of the wild-type phosphatase activity
S260C
-
t1/2 at room temperature is 13 min, compared to 12 min for wild-type enzyme. 91% of the wild-type phosphatase activity
S269C
-
t1/2 at room temperature is 20 min, compared to 12 min for wild-type enzyme. 54% of the wild-type phosphatase activity
S600I
mutation in cytoplasmic PAS domain, renders EvgS constitutively active at pH 7
T235C
-
t1/2 at room temperature is 14 min, compared to 12 min for wild-type enzyme. 84% of the wild-type phosphatase activity
T247R
-
inactive mutant protein
T250C
-
t1/2 at room temperature is 23 min, compared to 12 min for wild-type enzyme. 45% of the wild-type phosphatase activity
T256C
-
t1/2 at room temperature is 27 min, compared to 12 min for wild-type enzyme. 36% of the wild-type phosphatase activity
Y265C
-
t1/2 at room temperature is 20 min, compared to 12 min for wild-type enzyme. 54% of the wild-type phosphatase activity
additional information
cheA mutations leading to defects in chemotaxis are mapped and characterized
additional information
the histidine phosphorylation sites of each TorS transmitter domain and the aspartate phosphorylation site of the TorS receiver are individually changed by site-directed mutagenesis. All three phosphorylation sites proved essential for in vivo induction of the tor structural operon and for in vitro transphosphorylation of the cognate TorR response regulator. The His to Gln change in the classical transmitter domain abolished TorS autophosphorylation, whereas TorS undergoes significant autophosphorylation when the phosphorylation site of its receiver or alternative transmitter is changed
additional information
construction of several phoR genes, with various deletions in the 5' regions, which are regulated by the trp-lac hybrid promoter. The PhoR1084 and PhoR1159 proteins that lack the 83 and 158 N-terminal amino acids, respectively, retain the positive function for the expression of phoA that codes for alkaline phosphatase, but lack the negative function. The PhoR1263 protein that lacks the 262 N-terminal amino acids is deficient in both functions
additional information
-
mutations within the linker HAMP domain block the osmosensing function of EnvZ
additional information
construction of a DELTAcusS enzyme nockout mutant in an Escherichia coli strain in which the chromosomal copy of the gene for the multicopper oxidase CueO has been deleted (DELTAcueO). CueO converts Cu(I) to Cu(II) and therefore the use of the strain with the cueO deletion allows the observation of a growth phenotype even under aerobic conditions. The chromosomal copy of cusS is deleted from this background strain to allow characterization of CusS variants expressed from a plasmid. Partial functional complementation ofthe mutant strain with lasmid-expressed wild-type enzyme. The mutations do not significantly affect the relative expression levels of CusS
additional information
-
construction of a DELTAcusS enzyme nockout mutant in an Escherichia coli strain in which the chromosomal copy of the gene for the multicopper oxidase CueO has been deleted (DELTAcueO). CueO converts Cu(I) to Cu(II) and therefore the use of the strain with the cueO deletion allows the observation of a growth phenotype even under aerobic conditions. The chromosomal copy of cusS is deleted from this background strain to allow characterization of CusS variants expressed from a plasmid. Partial functional complementation ofthe mutant strain with lasmid-expressed wild-type enzyme. The mutations do not significantly affect the relative expression levels of CusS
additional information
construction of a functional chimeric protein, equivalent to the full cytosolic part of EnvZ, encompassing the entire catalytic part of the Escherichia coli EnvZ histidine kinase, fused to the HAMP domain of the Archaeoglobus fulgidus Af1503 receptor, generation of a second chimeric mutant version with additional A291F exchange
additional information
-
construction of a functional chimeric protein, equivalent to the full cytosolic part of EnvZ, encompassing the entire catalytic part of the Escherichia coli EnvZ histidine kinase, fused to the HAMP domain of the Archaeoglobus fulgidus Af1503 receptor, generation of a second chimeric mutant version with additional A291F exchange
additional information
construction of EvgS-PhoQ chimeras and activation of these chimera sensors, overview. The EvgS sensor domain is fused to the cytoplasmic region of PhoQ to examine whether it still responded to the signals. In chimera PvgS-A, the region from the N terminus to the transmembrane region of EvgS (residues 1 to 558 of EvgS) is fused to the cytoplasmic region of PhoQ (residues 215 to 486 of PhoQ) comprising the HAMP, HisKA, and HATPase_c domains, and in chimera PvgS-B, the region from the N terminus to the linker domain of EvgS (residues 1 to 710 of EvgS) is fused to the HisKA and HATPase_c domains of PhoQ (residues 267 to 486 of PhoQ)
additional information
-
construction of EvgS-PhoQ chimeras and activation of these chimera sensors, overview. The EvgS sensor domain is fused to the cytoplasmic region of PhoQ to examine whether it still responded to the signals. In chimera PvgS-A, the region from the N terminus to the transmembrane region of EvgS (residues 1 to 558 of EvgS) is fused to the cytoplasmic region of PhoQ (residues 215 to 486 of PhoQ) comprising the HAMP, HisKA, and HATPase_c domains, and in chimera PvgS-B, the region from the N terminus to the linker domain of EvgS (residues 1 to 710 of EvgS) is fused to the HisKA and HATPase_c domains of PhoQ (residues 267 to 486 of PhoQ)
additional information
-
engineering of covalent dimers of the cytoplasmic domains of CpxA which provide a robust experimental system for investigating cooperativity in histidine kinase autophosphorylation
additional information
His226 is required for induction and is structurally colocated with Pro522 at the top of the predicted transmembrane helix. The constitutive mutations in the PAS domain can be further activated by low external pH. Expression of the cytoplasmic part of the protein alone also gives constitutive activation, which is lost if the constitutive PAS mutations are present. The cytoplasmic part shows pH-dependent dimer formation in vitro
additional information
-
His226 is required for induction and is structurally colocated with Pro522 at the top of the predicted transmembrane helix. The constitutive mutations in the PAS domain can be further activated by low external pH. Expression of the cytoplasmic part of the protein alone also gives constitutive activation, which is lost if the constitutive PAS mutations are present. The cytoplasmic part shows pH-dependent dimer formation in vitro
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