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Literature summary for 2.1.1.166 extracted from

  • Hager, J.; Staker, B.L.; Jakob, U.
    Substrate binding analysis of the 23S rRNA methyltransferase RrmJ (2004), J. Bacteriol., 186, 6634-6642.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
D136N D136N mutant strain accumulates larger amounts of 30S and 50S ribosomal subunits than wild-type strains under nonstringent salt conditions, and has a significant amount of 40S ribosomal particles under stringent salt conditions Escherichia coli
D136N mutation leads to slight decrease in kcat value Escherichia coli
D20A mutation leads to slight decrease in kcat value Escherichia coli
F166A decrease in S-adenosyl-L-methionine binding affinity and/or the presence of a certain amount of an inactive yet stably folded RrmJ mutant species Escherichia coli
F37A/L39A mutant strain shows ribosome profiles that are indistinguishable from wild-type ribosome profile Escherichia coli
additional information extensive site-directed mutagenesis of the residues conserved in RrmJ and characterization of the mutant proteins both in vivo and in vitro Escherichia coli
Q67A/Y68A mutant strain shows ribosome profiles that are indistinguishable from wild-type ribosome profile Escherichia coli
R32A/R34A R32A/R34A mutant strain accumulates larger amounts of 30S and 50S ribosomal subunits than wild-type strains under nonstringent salt conditions, and has a significant amount of 40S ribosomal particles under stringent salt conditions Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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additional information changes in apparent Km-values for 50S subunit binding in RrmJ mutant proteins Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + uridine2552 in 23S rRNA Escherichia coli the enzyme is responsible for the 2'-O methylation of the universally conserved U2552 in the A loop of 23S rRNA S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
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Organism

Organism UniProt Comment Textmining
Escherichia coli A0A140N5X9
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Reaction

Reaction Comment Organism Reaction ID
S-adenosyl-L-methionine + uridine2552 in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA mechanism, 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 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + uridine2552 in 23S rRNA the enzyme is responsible for the 2'-O methylation of the universally conserved U2552 in the A loop of 23S rRNA Escherichia coli S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
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S-adenosyl-L-methionine + uridine2552 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 Escherichia coli S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
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Synonyms

Synonyms Comment Organism
23S rRNA methyltransferase
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Escherichia coli
FTSJ
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Escherichia coli
RrmJ
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Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information changes in apparent kcat-values for 50S subunit binding in RrmJ mutant proteins Escherichia coli

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
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Escherichia coli

General Information

General Information Comment Organism
metabolism absence of functional RrmJ causes the cellular accumulation of the individual ribosomal subunits at the expense of the functional 70S ribosomes Escherichia coli
physiological function the 23S rRNA modification is critical for ribosome stability Escherichia coli