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show all sequences of 2.1.1.170

Regulation of expression and catalytic activity of Escherichia coli RsmG methyltransferase

Benitez-Paez, A.; Villarroya, M.; Armengod, M.E.; RNA 18, 795-806 (2012)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
activity of rsmGp slightly increases by fourfold when cells are grown in minimal media supplemented with glycerol instead of glucose
Escherichia coli
Cloned(Commentary)
Commentary
Organism
gene rsmG is the second member in a bicistronic operon, rsmG also has its own promoter, RsmG expression might depend on the activity of an inverted repeated region, located between the rsmG promoter and ribosome binding site, which works as a weak transcriptional terminator. Expression of C-terminally His6-tagged and FLAG-tagged RsmG in Escherichia coli TOP10 cells
Escherichia coli
Engineering
Amino acid exchange
Commentary
Organism
D56A
site-directed mutagenesis of the catalytic residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
Escherichia coli
D71A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and catalytically inactive
Escherichia coli
D96A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and catalytically inactive
Escherichia coli
G73A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-sensitive and shows reduced activity compared to the wild-type enzyme
Escherichia coli
G75A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
Escherichia coli
G77A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and catalytically inactive
Escherichia coli
H53A
site-directed mutagenesis of the catalytic residue, the mutant is partly streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
Escherichia coli
K100A/R101A
site-directed mutagenesis of the RNA-binding residues, the mutant is streptomycin-resistant and catalytically inactive
Escherichia coli
K165A
site-directed mutagenesis of the RNA binding residue, the mutant is streptomycin-sensitive, but shows reduced activity compared to the wild-type enzyme
Escherichia coli
additional information
a rsmG null mutant is streptomycin-resistant
Escherichia coli
P79A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
Escherichia coli
R123A
site-directed mutagenesis of the RNA-binding residue, the mutant is streptomycin-sensitive, but shows reduced activity compared to the wild-type enzyme
Escherichia coli
R139A
site-directed mutagenesis of the catalytic residue, the mutant is streptomycin-resistant and catalytically inactive
Escherichia coli
R139K
site-directed mutagenesis of the catalytic residue, the mutant is partly streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
Escherichia coli
R197A
site-directed mutagenesis of the RNA binding residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P0A6U5
gene rsmG encoded in the mnmG-rsmG operon
-
Purification (Commentary)
Commentary
Organism
recombinant FLAG-tagged RsmG from Escherichia coli TOP10 cells by affinity chromatography
Escherichia coli
Source Tissue
Source Tissue
Commentary
Organism
Textmining
cell culture
activity of rsmGp slightly increases by fourfold when cells are grown in minimal media supplemented with glycerol instead of glucose
Escherichia coli
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Escherichia coli
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
activity of rsmGp slightly increases by fourfold when cells are grown in minimal media supplemented with glycerol instead of glucose
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
gene rsmG is the second member in a bicistronic operon, rsmG also has its own promoter, RsmG expression might depend on the activity of an inverted repeated region, located between the rsmG promoter and ribosome binding site, which works as a weak transcriptional terminator. Expression of C-terminally His6-tagged and FLAG-tagged RsmG in Escherichia coli TOP10 cells
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D56A
site-directed mutagenesis of the catalytic residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
Escherichia coli
D71A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and catalytically inactive
Escherichia coli
D96A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and catalytically inactive
Escherichia coli
G73A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-sensitive and shows reduced activity compared to the wild-type enzyme
Escherichia coli
G75A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
Escherichia coli
G77A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and catalytically inactive
Escherichia coli
H53A
site-directed mutagenesis of the catalytic residue, the mutant is partly streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
Escherichia coli
K100A/R101A
site-directed mutagenesis of the RNA-binding residues, the mutant is streptomycin-resistant and catalytically inactive
Escherichia coli
K165A
site-directed mutagenesis of the RNA binding residue, the mutant is streptomycin-sensitive, but shows reduced activity compared to the wild-type enzyme
Escherichia coli
additional information
a rsmG null mutant is streptomycin-resistant
Escherichia coli
P79A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
Escherichia coli
R123A
site-directed mutagenesis of the RNA-binding residue, the mutant is streptomycin-sensitive, but shows reduced activity compared to the wild-type enzyme
Escherichia coli
R139A
site-directed mutagenesis of the catalytic residue, the mutant is streptomycin-resistant and catalytically inactive
Escherichia coli
R139K
site-directed mutagenesis of the catalytic residue, the mutant is partly streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
Escherichia coli
R197A
site-directed mutagenesis of the RNA binding residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
Escherichia coli
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant FLAG-tagged RsmG from Escherichia coli TOP10 cells by affinity chromatography
Escherichia coli
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
cell culture
activity of rsmGp slightly increases by fourfold when cells are grown in minimal media supplemented with glycerol instead of glucose
Escherichia coli
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Escherichia coli
Expression
Organism
Commentary
Expression
Escherichia coli
RsmG levels decrease under conditions that down-regulate rRNA synthesis, but coordination between rRNA and RsmG expression does not seem to occur at the level of transcription initiation
down
Escherichia coli
slight induction of rsmGp during stationary phase is independent of the stress-inducible sigma factor RpoS
up
General Information
General Information
Commentary
Organism
malfunction
loss of the m7G527 modification confers low-level streptomycin resistance and may affect ribosomal functioning
Escherichia coli
additional information
positively charged residues on the protein surface around the active site, K100/R101, R123, K165, and R197, might play a role in the binding of the incoming 530 loop since their change to alanine impairs the modification function of RsmG
Escherichia coli
physiological function
RsmG is an S-adenosyl-L-methionine-dependent methyltransferase responsible for the synthesis of m7G527 in the 530 loop of bacterial 16S rRNA. This loop is universally conserved, plays a key role in ribosomal accuracy, and is a target for streptomycin binding, mechanisms controlling RsmG expression and activity, overview. Gene rsmG as part of a bicistronic operon also has its own promoter, which appears, in actively growing cells, as a control device to offset both the relatively low stability of RsmG and inhibition of the operon promoter. Critical importance of some residues located in the active site of Escherichia coli RsmG for the m7G modification process, the residues play a role in rRNA binding and catalysis
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
malfunction
loss of the m7G527 modification confers low-level streptomycin resistance and may affect ribosomal functioning
Escherichia coli
additional information
positively charged residues on the protein surface around the active site, K100/R101, R123, K165, and R197, might play a role in the binding of the incoming 530 loop since their change to alanine impairs the modification function of RsmG
Escherichia coli
physiological function
RsmG is an S-adenosyl-L-methionine-dependent methyltransferase responsible for the synthesis of m7G527 in the 530 loop of bacterial 16S rRNA. This loop is universally conserved, plays a key role in ribosomal accuracy, and is a target for streptomycin binding, mechanisms controlling RsmG expression and activity, overview. Gene rsmG as part of a bicistronic operon also has its own promoter, which appears, in actively growing cells, as a control device to offset both the relatively low stability of RsmG and inhibition of the operon promoter. Critical importance of some residues located in the active site of Escherichia coli RsmG for the m7G modification process, the residues play a role in rRNA binding and catalysis
Escherichia coli
Expression (protein specific)
Organism
Commentary
Expression
Escherichia coli
RsmG levels decrease under conditions that down-regulate rRNA synthesis, but coordination between rRNA and RsmG expression does not seem to occur at the level of transcription initiation
down
Escherichia coli
slight induction of rsmGp during stationary phase is independent of the stress-inducible sigma factor RpoS
up
Other publictions for EC 2.1.1.170
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
733472
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Impairing methylations at ribo ...
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41-49
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1
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2
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721042
Benitez-Paez
Regulation of expression and c ...
Escherichia coli
RNA
18
795-806
2012
1
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1
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15
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2
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1
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1
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1
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1
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1
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1
1
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15
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1
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1
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1
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2
3
3
2
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704222
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Activation of secondary metabo ...
Streptomyces griseus, Streptomyces griseus IFO13189
J. Antibiot.
62
669-673
2009
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2
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1
1
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706725
Gregory
Structural and functional stud ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
RNA
15
1693-1704
2009
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1
1
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1
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2
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5
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1
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4
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1
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1
1
1
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1
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2
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1
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4
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1
1
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704272
Nishimura
Mutations in rsmG, encoding a ...
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
J. Bacteriol.
189
3876-3883
2007
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-
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6
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1
1
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704273
Nishimura
Identification of the RsmG met ...
Bacillus subtilis 168, Bacillus subtilis
J. Bacteriol.
189
6068-6073
2007
-
-
-
-
-
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-
-
-
-
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2
-
90
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4
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2
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4
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1
1
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705767
Okamoto
Loss of a conserved 7-methylgu ...
Escherichia coli, Escherichia coli BW25113
Mol. Microbiol.
63
1096-1106
2007
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-
1
-
1
-
-
-
-
-
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-
28
-
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1
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2
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1
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1
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1
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1
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2
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1
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1
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1
1
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706646
Romanowski
Crystal structure of the Esche ...
Escherichia coli
Proteins
47
563-567
2002
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1
1
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2
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2
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1
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1
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1
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