2.1.1.230: 23S rRNA (adenosine1067-2'-O)-methyltransferase
This is an abbreviated version!
For detailed information about 23S rRNA (adenosine1067-2'-O)-methyltransferase, go to the full flat file.
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Reaction
Synonyms
EC 2.1.1.66, NHR, NHR protein, nosiheptide resistance methyltransferase, nosiheptide-resistance methyltransferase, thiostrepton resistance methyltransferase, thiostrepton-resistance methylase, thiostrepton-resistance methyltransferase, TSR
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Substrates Products
Substrates Products on EC 2.1.1.230 - 23S rRNA (adenosine1067-2'-O)-methyltransferase
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REACTION DIAGRAM
S-adenosyl-L-methionine + adenosine in an RNA fragment containing nucleotides 1029-1122 of the 23S ribosomal RNA from Escherichia coli
S-adenosyl-L-homocysteine + 2'-O-methyladenosine in an RNA fragment containing nucleotides 1029-1122 of the 23S ribosomal RNA from Escherichia coli
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S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
S-adenosyl-L-methionine + adenosine1067 in Escherichia coli 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in Escherichia coli 23S rRNA
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S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
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S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
as 58 nucleotide substrate for methylation, or as shortened 29 nt hairpin substrate, local base-base interactions play an important role in aligning the substrate 2'-hydroxyl group of A1067 for methyl group transfer, stoichiometry of RNA binding by the NHR dimer, overview
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S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
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S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
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Streptomyces azureus is the producer of the peptide antibiotic thiostrepton. Thiostrepton inhibits protein synthesis by binding to the complex of 23S rRNA and protein L-11 which blocks processes associated with the GTP-hydrolysis center of the ribosome including the binding of guanine nucleotides, elongation factor proteins and tRNA. 23S rRNA (adenosine1067-2'-O)-methyltransferase confers resistance to tthiostrepton
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S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
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the enzyme is involved in resistance to thiostrepton
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S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
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the methylase enzyme, responsible for autoimmunity in the thiostrepton producer Streptomyces azureus, renders ribosomes completely resistant to thiostrepton
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S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
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RNA sequence variants of the RNA fragment with mutations in nucleotides 1051-1108 are tested as substrates for the methylase. Methylation is dependent on the secondary structure of the hairpin including nucleotide A1067 and the exact sequence U(1066)-A(1067)-G(1068)-A(1O69)-A(1070) of the single strand
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S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
enzyme Tsr uses the co-substrate AdoMet to methylate the 23 S rRNA, presumably prior to the assembly of the 50 S subunit as the L11 and proposed Tsr binding surfaces are overlapping
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S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
58-nt RNA substrate secondary structure, and key longrange interactions within the 58-nt domain tertiary fold, overview
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compared the methylation activity of the Arg135Ala NHR heterodimer with the wild-type NHR homodimer and a series of 29 nt wild-type and mutant RNA substrates. The inactive heterodimer complex binds the RNA more efficiently than the inactive mutant homodimer. Construction of diverse mutant RNA substrates in which A1067 is replaced by adenine structural analogues, A1067G retains significant activity, while 7-deaza-A and 1-methyl-A substitutions at A1067 reduce the activity, overview
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additional information
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compared the methylation activity of the Arg135Ala NHR heterodimer with the wild-type NHR homodimer and a series of 29 nt wild-type and mutant RNA substrates. The inactive heterodimer complex binds the RNA more efficiently than the inactive mutant homodimer. Construction of diverse mutant RNA substrates in which A1067 is replaced by adenine structural analogues, A1067G retains significant activity, while 7-deaza-A and 1-methyl-A substitutions at A1067 reduce the activity, overview
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