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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
S-adenosyl-L-methionine + cytidine1920 in 50S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
additional information
?
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
the 50S subunit is the preferred substrate, a modest amount of methylation is seen with free 23S rRNA and 70S ribosomes
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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the bifunctional enzyme modifies nucleotide C1409 in helix 44 of 16S rRNA and nucleotide C1920 in helix 69 of 23S rRNA
the exact position of the methyl group in the wild-type rRNAs is verified by MALDI quadrupole-TOF tandem MS analysis
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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the 50S subunit is the preferred substrate, a modest amount of methylation is seen with free 23S rRNA and 70S ribosomes
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?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
the 50S subunit is the preferred substrate, a modest amount of methylation is seen with free 23S rRNA and 70S ribosomes
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?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
the 50S subunit is the preferred substrate, a modest amount of methylation is seen with free 23S rRNA and 70S ribosomes
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?
S-adenosyl-L-methionine + cytidine1920 in 50S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 50S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 50S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
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additional information
?
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50S rRNA is used as substrate in activity assays. Mass spectrometric analyses of Campylobacter jejuni 23S rRNA
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additional information
?
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50S rRNA is used as substrate in activity assays. Mass spectrometric analyses of Campylobacter jejuni 23S rRNA
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additional information
?
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50S rRNA is used as substrate in activity assays. Mass spectrometric analyses of Campylobacter jejuni 23S rRNA
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additional information
?
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the 2'-O-methyltransferase TlyA from Mycobacterium tuberculosis methylates both nucleotide C1409 of 16S rRNA, EC 2.1.1.227, and C1920 of 23S rRNA
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additional information
?
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the purified recombinant enzyme TlyA efficiently 2'-O-methylates C1920 in vitro at a molar enzyme to substrate ratio of 1:10
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additional information
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the bifunctional enzyme exhibits the activities of EC 2.1.1.226 and EC 2.1.1.227
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additional information
?
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the bifunctional enzyme exhibits the activities of EC 2.1.1.226 and EC 2.1.1.227
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additional information
?
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the 2'-O-methyltransferase TlyA from Mycobacterium tuberculosis methylates both nucleotide C1409 of 16S rRNA, EC 2.1.1.227, and C1920 of 23S rRNA
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additional information
?
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the purified recombinant enzyme TlyA efficiently 2'-O-methylates C1920 in vitro at a molar enzyme to substrate ratio of 1:10
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additional information
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the TlyAII enzyme methylates efficiently at C1920 in 50S subunits in vitro, although weaker activity is also detected on 70S ribosome and 23S rRNA substrates
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additional information
?
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the TlyAII enzyme methylates efficiently at C1920 in 50S subunits in vitro, although weaker activity is also detected on 70S ribosome and 23S rRNA substrates
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
additional information
?
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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the 50S subunit is the preferred substrate, a modest amount of methylation is seen with free 23S rRNA and 70S ribosomes
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?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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the 50S subunit is the preferred substrate, a modest amount of methylation is seen with free 23S rRNA and 70S ribosomes
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?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
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S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
the 50S subunit is the preferred substrate, a modest amount of methylation is seen with free 23S rRNA and 70S ribosomes
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?
additional information
?
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the 2'-O-methyltransferase TlyA from Mycobacterium tuberculosis methylates both nucleotide C1409 of 16S rRNA, EC 2.1.1.227, and C1920 of 23S rRNA
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additional information
?
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the 2'-O-methyltransferase TlyA from Mycobacterium tuberculosis methylates both nucleotide C1409 of 16S rRNA, EC 2.1.1.227, and C1920 of 23S rRNA
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evolution
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TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, termed TlyAI, has shorter N- and C-termini and methylates only C1920. The second group, TlyAII, includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 (c.f. EC 2.1.1.227), and C1920
evolution
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TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, termed TlyAI, has shorter N- and C-termini and methylates only C1920. The second group, TlyAII, includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 (c.f. EC 2.1.1.227), and C1920
evolution
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TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, termed TlyAI, has shorter N- and C-termini and methylates only C1920. The second group, TlyAII, includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 (c.f. EC 2.1.1.227), and C1920
evolution
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TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, termed TlyAI, has shorter N- and C-termini and methylates only C1920. The second group, TlyAII, includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 (c.f. EC 2.1.1.227), and C1920
evolution
TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, termed TlyAI, has shorter N- and C-termini and methylates only C1920. The second group, TlyAII, includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 (c.f. EC 2.1.1.227), and C1920
evolution
TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, termed TlyAI, has shorter N- and C-termini and methylates only C1920. The second group, TlyAII, includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 (c.f. EC 2.1.1.227), and C1920
evolution
-
TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, termed TlyAI, has shorter N- and C-termini and methylates only C1920. The second group, TlyAII, includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 (c.f. EC 2.1.1.227), and C1920
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evolution
-
TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, termed TlyAI, has shorter N- and C-termini and methylates only C1920. The second group, TlyAII, includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 (c.f. EC 2.1.1.227), and C1920
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evolution
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TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, termed TlyAI, has shorter N- and C-termini and methylates only C1920. The second group, TlyAII, includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 (c.f. EC 2.1.1.227), and C1920
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malfunction
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disruption of the tlyA ORF can confer capreomycin resistance
malfunction
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the bifunctional enzyme modifies nucleotide C1409 in helix 44 of 16S rRNA and nucleotide C1920 in helix 69 of 23S rRNA. Loss of these rRNA methylations confers resistance to capreomycin and viomycin
malfunction
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inactivation of TlyA and loss of its activity confer resistance to capreomycin and viomycin
malfunction
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inactivation of TlyA and loss of its activity confer resistance to capreomycin and viomycin
malfunction
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inactivation of TlyA and loss of its activity confer resistance to capreomycin and viomycin
malfunction
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inactivation of TlyA and loss of its activity confer resistance to capreomycin and viomycin
malfunction
inactivation of TlyA and loss of its activity confer resistance to capreomycin and viomycin
malfunction
inactivation of TlyA and loss of its activity confer resistance to capreomycin and viomycin
malfunction
deletion of the cj0588 gene in Campylobacter jejuni or substitution with alanine of K80, D162, or K188 in the catalytic center of the enzyme cause complete loss of 2'-O-methylation activity. Campylobacter jejuni strains expressing catalytically inactive versions of Cj0588 have the same phenotype as cj0588-null mutants, and show altered tolerance to capreomycin due to perturbed ribosomal subunit association, reduced motility and impaired ability to form biofilms. These functions are reestablished when methyltransferase activity is restored
malfunction
loss-of-function mutations in rRNA methylase TlyA or point mutations in 16S rRNA, in particular the A1408G mutation. Both of these alterations result in resistance by reducing drug binding to the ribosome. Alterations of tlyA gene expression affect both antibiotic drug susceptibility and fitness cost of drug resistance. In particular, the common resistance mutation A1408G is accompanied by a physiological change that involves increased expression of the tlyA gene. This gene encodes an enzyme that methylates neighboring 16S rRNA position C1409, and as a result of increased TlyA expression the fitness cost of the A1408G mutation is significantly reduced
malfunction
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deletion of the cj0588 gene in Campylobacter jejuni or substitution with alanine of K80, D162, or K188 in the catalytic center of the enzyme cause complete loss of 2'-O-methylation activity. Campylobacter jejuni strains expressing catalytically inactive versions of Cj0588 have the same phenotype as cj0588-null mutants, and show altered tolerance to capreomycin due to perturbed ribosomal subunit association, reduced motility and impaired ability to form biofilms. These functions are reestablished when methyltransferase activity is restored
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malfunction
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deletion of the cj0588 gene in Campylobacter jejuni or substitution with alanine of K80, D162, or K188 in the catalytic center of the enzyme cause complete loss of 2'-O-methylation activity. Campylobacter jejuni strains expressing catalytically inactive versions of Cj0588 have the same phenotype as cj0588-null mutants, and show altered tolerance to capreomycin due to perturbed ribosomal subunit association, reduced motility and impaired ability to form biofilms. These functions are reestablished when methyltransferase activity is restored
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malfunction
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inactivation of TlyA and loss of its activity confer resistance to capreomycin and viomycin
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malfunction
-
loss-of-function mutations in rRNA methylase TlyA or point mutations in 16S rRNA, in particular the A1408G mutation. Both of these alterations result in resistance by reducing drug binding to the ribosome. Alterations of tlyA gene expression affect both antibiotic drug susceptibility and fitness cost of drug resistance. In particular, the common resistance mutation A1408G is accompanied by a physiological change that involves increased expression of the tlyA gene. This gene encodes an enzyme that methylates neighboring 16S rRNA position C1409, and as a result of increased TlyA expression the fitness cost of the A1408G mutation is significantly reduced
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malfunction
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inactivation of TlyA and loss of its activity confer resistance to capreomycin and viomycin
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malfunction
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inactivation of TlyA and loss of its activity confer resistance to capreomycin and viomycin
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metabolism
antibiotic resistance mechanisms frequently confer a fitness cost, and these costs can be genetically ameliorated by intra- or extragenic second-site mutations, often without loss of resistance. Another mechanism by which the fitness cost of antibiotic resistance can be reduced is via a regulatory response where the deleterious effect of the resistance mechanism is lowered by a physiological alteration that buffers the mutational effect. In mycobacteria, resistance to the clinically used tuberactinomycin antibiotic capreomycin involves loss-of-function mutations in rRNA methylase TlyA or point mutations in 16S rRNA, in particular the A1408G mutation. Both of these alterations result in resistance by reducing drug binding to the ribosome. In mycobacteria, this nonmutational mechanism (i.e. gene regulatory) can restore fitness to genetically resistant bacteria. Incubation with capreomycin during bacterial growth resulted in a reduced post-transcriptional modification of rRNA at TlyA-dependent sites (1409 in 16S and 1920 in 23S), cf. EC 2.1.1.226
metabolism
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antibiotic resistance mechanisms frequently confer a fitness cost, and these costs can be genetically ameliorated by intra- or extragenic second-site mutations, often without loss of resistance. Another mechanism by which the fitness cost of antibiotic resistance can be reduced is via a regulatory response where the deleterious effect of the resistance mechanism is lowered by a physiological alteration that buffers the mutational effect. In mycobacteria, resistance to the clinically used tuberactinomycin antibiotic capreomycin involves loss-of-function mutations in rRNA methylase TlyA or point mutations in 16S rRNA, in particular the A1408G mutation. Both of these alterations result in resistance by reducing drug binding to the ribosome. In mycobacteria, this nonmutational mechanism (i.e. gene regulatory) can restore fitness to genetically resistant bacteria. Incubation with capreomycin during bacterial growth resulted in a reduced post-transcriptional modification of rRNA at TlyA-dependent sites (1409 in 16S and 1920 in 23S), cf. EC 2.1.1.226
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physiological function
bacterial 2'-O-methyltransferase TlyA methylates either both nucleotide C1409 of 16S rRNA and C1920 of 23S rRNA. Both ribosomal methylations increase bacterial susceptibility to ribosome targeting antibiotics capreomycin and viomycin. The enzyme also function as a hemolysin, but increased bacterial hemolytic function is not likely a consequence of TlyA-mediated methylations of the ribosome
physiological function
the enzyme TlyA is an rRNA 2'-O-methyltransferase associated with resistance to cyclic peptide antibiotics such as capreomycin. The bacterial pathogen Campylobacter jejuni possesses the TlyA homologue Cj0588, which contributes to virulence, and is a type I homologue of TlyA that 2'-O-methylates 23S rRNA nucleotide C1920. The contribution of Cj0588 to virulence is a consequence of the enzyme's ability to methylate its rRNA
physiological function
TlyA methylase modifies the rRNA position 1409, reducing the cost of the A1408G mutation while concomitantly also reducing the antibiotic resistance level, e.g. against capreomycin and viomycin. In response to capreomycin, cells downregulate TlyA-mediated methylation of 16S and 23S rRNA resulting in decreased drug susceptibility. Increased TlyA expression reduces resistance in the A1408G mutant and concomitantly increases fitness
physiological function
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the enzyme TlyA is an rRNA 2'-O-methyltransferase associated with resistance to cyclic peptide antibiotics such as capreomycin. The bacterial pathogen Campylobacter jejuni possesses the TlyA homologue Cj0588, which contributes to virulence, and is a type I homologue of TlyA that 2'-O-methylates 23S rRNA nucleotide C1920. The contribution of Cj0588 to virulence is a consequence of the enzyme's ability to methylate its rRNA
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physiological function
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the enzyme TlyA is an rRNA 2'-O-methyltransferase associated with resistance to cyclic peptide antibiotics such as capreomycin. The bacterial pathogen Campylobacter jejuni possesses the TlyA homologue Cj0588, which contributes to virulence, and is a type I homologue of TlyA that 2'-O-methylates 23S rRNA nucleotide C1920. The contribution of Cj0588 to virulence is a consequence of the enzyme's ability to methylate its rRNA
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physiological function
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TlyA methylase modifies the rRNA position 1409, reducing the cost of the A1408G mutation while concomitantly also reducing the antibiotic resistance level, e.g. against capreomycin and viomycin. In response to capreomycin, cells downregulate TlyA-mediated methylation of 16S and 23S rRNA resulting in decreased drug susceptibility. Increased TlyA expression reduces resistance in the A1408G mutant and concomitantly increases fitness
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physiological function
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bacterial 2'-O-methyltransferase TlyA methylates either both nucleotide C1409 of 16S rRNA and C1920 of 23S rRNA. Both ribosomal methylations increase bacterial susceptibility to ribosome targeting antibiotics capreomycin and viomycin. The enzyme also function as a hemolysin, but increased bacterial hemolytic function is not likely a consequence of TlyA-mediated methylations of the ribosome
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additional information
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the cyclic peptide antibiotics capreomycin and viomycin bind on the ribosomal S70 subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA
additional information
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the cyclic peptide antibiotics capreomycin and viomycin bind on the ribosomal S70 subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA
additional information
-
the cyclic peptide antibiotics capreomycin and viomycin bind on the ribosomal S70 subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA
additional information
-
the cyclic peptide antibiotics capreomycin and viomycin bind on the ribosomal S70 subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA
additional information
the cyclic peptide antibiotics capreomycin and viomycin bind on the ribosomal S70 subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA
additional information
the cyclic peptide antibiotics capreomycin and viomycin bind on the ribosomal S70 subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA
additional information
the S4-type RNA recognition domain (residues 5-64), S-adenosyl-methionine binding domain (residues 84-153), SAM-interacting residues (residues 90-94), and four catalytic residues (K69-D154-K182-E238) are conserved in 2'-O-methyltrasferases TlyA
additional information
mechanism of Cj0588 action, overview. Homology modelling of the tertiary structure of the Cj0588 catalytic domain using Mycobacterium tuberculosis TlyA structure (PDB ID 5EOV) as a template. The HhaI methyltransferase structure (PDB ID 2HMY) is used to superimpose the AdoMet cofactor. Three-dimensional modeling of the catalytic domain of Cj0588 reveals a structure typical for 2'-O-methyltransferases with a seven-stranded beta-sheet between five alpha-helix layers and four residues K80, D162, K188 and E245 that comprise the catalytic center
additional information
-
mechanism of Cj0588 action, overview. Homology modelling of the tertiary structure of the Cj0588 catalytic domain using Mycobacterium tuberculosis TlyA structure (PDB ID 5EOV) as a template. The HhaI methyltransferase structure (PDB ID 2HMY) is used to superimpose the AdoMet cofactor. Three-dimensional modeling of the catalytic domain of Cj0588 reveals a structure typical for 2'-O-methyltransferases with a seven-stranded beta-sheet between five alpha-helix layers and four residues K80, D162, K188 and E245 that comprise the catalytic center
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additional information
-
mechanism of Cj0588 action, overview. Homology modelling of the tertiary structure of the Cj0588 catalytic domain using Mycobacterium tuberculosis TlyA structure (PDB ID 5EOV) as a template. The HhaI methyltransferase structure (PDB ID 2HMY) is used to superimpose the AdoMet cofactor. Three-dimensional modeling of the catalytic domain of Cj0588 reveals a structure typical for 2'-O-methyltransferases with a seven-stranded beta-sheet between five alpha-helix layers and four residues K80, D162, K188 and E245 that comprise the catalytic center
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additional information
-
the cyclic peptide antibiotics capreomycin and viomycin bind on the ribosomal S70 subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA
-
additional information
-
the S4-type RNA recognition domain (residues 5-64), S-adenosyl-methionine binding domain (residues 84-153), SAM-interacting residues (residues 90-94), and four catalytic residues (K69-D154-K182-E238) are conserved in 2'-O-methyltrasferases TlyA
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additional information
-
the cyclic peptide antibiotics capreomycin and viomycin bind on the ribosomal S70 subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA
-
additional information
-
the cyclic peptide antibiotics capreomycin and viomycin bind on the ribosomal S70 subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D162A
site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type
K188A
site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type
K80A
site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type
D162A
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site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type
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K188A
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site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type
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K80A
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site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type
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D162A
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site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type
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K188A
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site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type
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K80A
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site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type
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additional information
generation of an inactive Cj0588 deletion mutant. The Campylobacter jejuni 4051cj0588 null-mutant is complemented in trans with plasmid-encoded versions of the cj0588 gene. Inactivation of Cj0588 hinders Campylobacter jejuni motility and impairs biofilm formation, phenotype, overview
additional information
-
generation of an inactive Cj0588 deletion mutant. The Campylobacter jejuni 4051cj0588 null-mutant is complemented in trans with plasmid-encoded versions of the cj0588 gene. Inactivation of Cj0588 hinders Campylobacter jejuni motility and impairs biofilm formation, phenotype, overview
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additional information
-
generation of an inactive Cj0588 deletion mutant. The Campylobacter jejuni 4051cj0588 null-mutant is complemented in trans with plasmid-encoded versions of the cj0588 gene. Inactivation of Cj0588 hinders Campylobacter jejuni motility and impairs biofilm formation, phenotype, overview
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additional information
generation of a tlyA deletion mutant
additional information
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generation of a tlyA deletion mutant
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Maus, C.E.; Plikaytis, B.B.; Shinnick, T.M.
Mutation of tlyA confers capreomycin resistance in Mycobacterium tuberculosis
Antimicrob. Agents Chemother.
49
571-577
2005
Mycobacterium tuberculosis
brenda
Johansen, S.K.; Maus, C.E.; Plikaytis, B.B.; Douthwaite, S.
Capreomycin binds across the ribosomal subunit interface using tlyA-encoded 2'-O-methylations in 16S and 23S rRNAs
Mol. Cell
23
173-182
2006
Mycobacterium tuberculosis
brenda
Monshupanee, T.; Johansen, S.K.; Dahlberg, A.E.; Douthwaite, S.
Capreomycin susceptibility is increased by TlyA-directed 2-O-methylation on both ribosomal subunits
Mol. Microbiol.
85
1194-1203
2012
Brachyspira hyodysenteriae (Q06803), Geobacillus stearothermophilus, Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, Mycolicibacterium smegmatis (A0QYR0), Mycolicibacterium smegmatis mc(2)155 (A0QYR0), no activity in Escherichia coli, Streptomyces coelicolor, Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Monshupanee, T.
Increased bacterial hemolytic activity is conferred by expression of TlyA methyltransferase but not by its 2'-O-methylation of the ribosome
Curr. Microbiol.
67
61-68
2013
Mycobacterium tuberculosis (P9WJ63), Mycobacterium tuberculosis H37Rv (P9WJ63)
brenda
Salamaszynska-Guz, A.; Rose, S.; Lykkebo, C.; Taciak, B.; Bacal, P.; Uspienski, T.; Douthwaite, S.
Biofilm formation and motility are promoted by Cj0588-directed methylation of rRNA in Campylobacter jejuni
Front. Cell. Infect. Microbiol.
7
533
2018
Campylobacter jejuni subsp. jejuni (Q0PAS9), Campylobacter jejuni subsp. jejuni NCTC 11168 (Q0PAS9), Campylobacter jejuni subsp. jejuni ATCC 700819 (Q0PAS9)
brenda
Freihofer, P.; Akbergenov, R.; Teo, Y.; Juskeviciene, R.; Andersson, D.; Boettger, E.
Nonmutational compensation of the fitness cost of antibiotic resistance in mycobacteria by overexpression of tlyA rRNA methylase
RNA
22
1836-1843
2016
Mycobacterium tuberculosis (P9WJ63), Mycobacterium tuberculosis H37Rv (P9WJ63)
brenda