2.1.1.166: 23S rRNA (uridine2552-2'-O)-methyltransferase
This is an abbreviated version!
For detailed information about 23S rRNA (uridine2552-2'-O)-methyltransferase, go to the full flat file.
Reaction
Synonyms
23 S ribosomal RNA methyltransferase, 23S rRNA methyltransferase, FTSJ, FtsJ/RrmJ heat shock protein, FtsJ2, heat shock protein RrmJ, Mj0697, RlmE, RrmJ, Um(2552) 23S ribosomal RNA methyltransferase, Um2552 methyltransferase
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Substrates Products
Substrates Products on EC 2.1.1.166 - 23S rRNA (uridine2552-2'-O)-methyltransferase
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REACTION DIAGRAM
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
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S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
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S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
in vivo methylation of 23S rRNA by FtsJ goes to near completion
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S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
the 2'-O-ribose methylation of the universally conserved base U2552 in the A-loop of the 23 S rRNA
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S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
the enzyme is responsible for the 2'-O methylation of the universally conserved U2552 in the A loop of 23S rRNA
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S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
U2552 is an ubiquitously methylated residue
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S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
identification of the methylated nucleotide as 2'-O-methyluridine 2552, by reverse phase high performance liquid chromatography analysis, boronate affinity chromatography, and hybridization-protection experiments. In vitro, FtsJ does not efficiently methylate ribosomes purified from a strain producing FtsJ, suggesting that these ribosomes are already methylated in vivo by FtsJ. FtsJ is active on ribosomes and on the 50 S ribosomal subunit, but is inactive on free rRNA, suggesting that its natural substrate is ribosomes or a pre-ribosomal ribonucleoprotein particle
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S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
the 2'-O-ribose methylation of the universally conserved base U2552 in the A-loop of the 23 S rRNA. The active site of RrmJ appears to be formed by a catalytic triad consisting of two lysine residues, Lys-38 and Lys-164, and the negatively charged residue Asp-124. Another highly conserved residue, Glu-199, that is present in the active site of RrmJ and VP39 appears to play only a minor role in the methyltransfer reaction in vivo. A reaction mechanism for the methyltransfer activity of RrmJ is proposed
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S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
the isolated unmodified A loop serves as the minimal methylation substrate of wild-type RrmJ in vitro. 50S ribosomal subunits prepared from the rrmJ deletion strain appear to serve as substrates for RrmJ in vitro, while naked 23S rRNA or 40S ribosomal particles that are prepared from the rrmJ deletion strain are not methylated by purified RrmJ. This finding suggests that either the correct folding of the 23S rRNA or additional protein-protein interactions are necessary for the substrate recognition. A positively charged, highly conserved ridge in RrmJ appears to play a significant role in 23S rRNA binding and methylation. A structural model is provided of how the A loop of the 23S rRNA binds to RrmJ. Based on modeling studies and the structure of the 50S ribosome, a two-step model is proposed where the A loop undocks from the tightly packed 50S ribosomal subunit, allowing RrmJ to gain access to the substrate nucleotide U2552, and where U2552 undergoes base flipping, allowing the enzyme to methylate the 2'-O position of the ribose
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S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
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rrmJ gene encodes a methyltransferase that modifies the U2552 residue of 23S rRNA
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S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
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