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Literature summary for 2.1.1.166 extracted from

  • Widerak, M.; Kern, R.; Malki, A.; Richarme, G.
    U2552 methylation at the ribosomal A-site is a negative modulator of translational accuracy (2005), Gene, 347, 109-114.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information lack of U2552 methylation, obtained in rrmJ-deficient mutants, results in a decrease in programmed +1 and -1 translational frameshifing and a decrease in readthrough of UAA and UGA stop codons. The increased translational accuracy of rrmJ-deficient strains suggests that the interaction between aminoacyl-tRNA and U2552 is important for selection of the correct tRNA at the ribosomal A site, and supports the idea that translational accuracy in vivo is optimal rather than maximal, thus pointing to the participation of recoding events in the normal cell physiology 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 U2552 is an ubiquitously methylated residue 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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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
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Escherichia coli S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
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?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA U2552 is an ubiquitously methylated residue Escherichia coli S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
-
?

Synonyms

Synonyms Comment Organism
RrmJ
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Escherichia coli
Um2552 methyltransferase
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Escherichia coli

Cofactor

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

General Information

General Information Comment Organism
malfunction lack of U2552 methylation, obtained in rrmJ-deficient mutants, results in a decrease in programmed +1 and -1 translational frameshifing and a decrease in readthrough of UAA and UGA stop codons. The increased translational accuracy of rrmJ-deficient strains suggests that the interaction between aminoacyl-tRNA and U2552 is important for selection of the correct tRNA at the ribosomal A site, and supports the idea that translational accuracy in vivo is optimal rather than maximal, thus pointing to the participation of recoding events in the normal cell physiology Escherichia coli