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Literature summary extracted from

  • Bonnerot, C.; Pintard, L.; Lutfalla, G.
    Functional redundancy of Spb1p and a snR52-dependent mechanism for the 2'-O-ribose methylation of a conserved rRNA position in yeast (2003), Mol. Cell, 12, 1309-1315.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.167 additional information a point mutation in the Ado-Met binding site of Spb1p affects cell growth but does not abolish methylation of U2918. When this mutation is combined with disruption of snR52 cell growth is severely impaired and U2918 is no longer methylated. In vitro, Spb1p is able to methylate U2918 on 60S subunits. For this methylation two mechanisms coexist: a site-specific methyltransferase (Spb1p) and a snoRNA-dependent mechanism Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.167 S-adenosyl-L-methionine + uridine2918 in 25S rRNA Saccharomyces cerevisiae the enzyme is required for proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Specifically methylates the guanosine in position 2922 of the 25S rRNA at the stage of 27S pre-rRNA maturation. Methylates also the uridine in position 2921 in the absence of methylation of this residue guided by snoRNA snR52 at the stage of 35S pre-rRNA maturation S-adenosyl-L-homocysteine + 2'-O-methyluridine2918 in 25S rRNA
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 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.167 Saccharomyces cerevisiae P25582
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.167 additional information a point mutation in the Ado-Met binding site of Spb1p affects cell growth but does not abolish methylation of U2918. When this mutation is combined with disruption of snR52 cell growth is severely impaired and U2918 is no longer methylated. In vitro, Spb1p is able to methylate U2918 on 60S subunits. For this methylation two mechanisms coexist: a site-specific methyltransferase (Spb1p) and a snoRNA-dependent mechanism Saccharomyces cerevisiae ?
-
 ?
2.1.1.167 S-adenosyl-L-methionine + uridine2918 in 25S rRNA the enzyme is required for proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Specifically methylates the guanosine in position 2922 of the 25S rRNA at the stage of 27S pre-rRNA maturation. Methylates also the uridine in position 2921 in the absence of methylation of this residue guided by snoRNA snR52 at the stage of 35S pre-rRNA maturation Saccharomyces cerevisiae S-adenosyl-L-homocysteine + 2'-O-methyluridine2918 in 25S rRNA
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 ?
2.1.1.167 S-adenosyl-L-methionine + uridine2918 in 25S rRNA no methylation of uridine2791 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + 2'-O-methyluridine2918 in 25S rRNA
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 ?

General Information

EC Number General Information Comment Organism
2.1.1.167 malfunction a point mutation in the Ado-Met binding site of Spb1p affects cell growth but does not abolish methylation of U2918. When this mutation is combined with disruption of snR52 cell growth is severely impaired and U2918 is no longer methylated. In vitro, Spb1p is able to methylate U2918 on 60S subunits. For this methylation two mechanisms coexist: a site-specific methyltransferase (Spb1p) and a snoRNA-dependent mechanism Saccharomyces cerevisiae