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Literature summary for 2.1.1.171 extracted from

  • Weitzmann, C.; Tumminia, S.J.; Boublik, M.; Ofengand, J.
    A paradigm for local conformational control of function in the ribosome: binding of ribosomal protein S19 to Escherichia coli 16S rRNA in the presence of 57 is required for methylation of m2G966 and blocks methylation of m C967 by their respective methyltransferases (1991), Nucleic Acids Res., 19, 7089-7095.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + guanine966 in 16S rRNA Escherichia coli the enzyme uses unmethylated 30S subunits as a substrate, but not free unmethylated 16S rRNA. Binding of ribosomal proteins S7, S9, and S19 to unmodified 16S rRNA individually and in all possible combinations shows that S7 plus S19 are sufficient to block methylation by the m5C967 methyltransferase, while simultaneously inducing methylation by the m2G966 methyltransferase. A purified complex containing stoichiometric amounts of proteins S7, S9, and S19 bound to 16S rRNA is isolated and shown to possess the same methylation properties as 30S subunits, that is, the ability to be methylated by the m2G966 methyltransferase but not by the m5C967 methyltransferase. Since binding of S19 requires prior binding of S7, which has no effect on methylation when bound alone, the switch in methylase specificity is attributed solely to the presence of RNA-bound S19. Single-omission reconstitution of 30S subunits deficient in S19 results in particles that could not be efficiently methylated by either enzyme. Thus while binding of S19 is both necessary and sufficient to convert 16S rRNA into a substrate of the m2G966 methyltransferase, binding of either S19 alone or some other protein or combination of proteins to the 16S rRNA can abolish activity of the m5C967 methyltransferase. Binding of S19 to 16S rRNA is known to cause local conformational changes in the 960-975 stem-loop structure surrounding the two methylated nucleotides S-adenosyl-L-homocysteine + N2-methylguanine966 in 16S rRNA
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Organism

Organism UniProt Comment Textmining
Escherichia coli P0ADX9
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + guanine966 in 16S rRNA the enzyme uses unmethylated 30S subunits as a substrate, but not free unmethylated 16S rRNA. Binding of ribosomal proteins S7, S9, and S19 to unmodified 16S rRNA individually and in all possible combinations shows that S7 plus S19 are sufficient to block methylation by the m5C967 methyltransferase, while simultaneously inducing methylation by the m2G966 methyltransferase. A purified complex containing stoichiometric amounts of proteins S7, S9, and S19 bound to 16S rRNA is isolated and shown to possess the same methylation properties as 30S subunits, that is, the ability to be methylated by the m2G966 methyltransferase but not by the m5C967 methyltransferase. Since binding of S19 requires prior binding of S7, which has no effect on methylation when bound alone, the switch in methylase specificity is attributed solely to the presence of RNA-bound S19. Single-omission reconstitution of 30S subunits deficient in S19 results in particles that could not be efficiently methylated by either enzyme. Thus while binding of S19 is both necessary and sufficient to convert 16S rRNA into a substrate of the m2G966 methyltransferase, binding of either S19 alone or some other protein or combination of proteins to the 16S rRNA can abolish activity of the m5C967 methyltransferase. Binding of S19 to 16S rRNA is known to cause local conformational changes in the 960-975 stem-loop structure surrounding the two methylated nucleotides Escherichia coli S-adenosyl-L-homocysteine + N2-methylguanine966 in 16S rRNA
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Synonyms

Synonyms Comment Organism
16S rRNA-specific methyltransferases m2GMT
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Escherichia coli
m2G966 methyltransferase
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Escherichia coli

Cofactor

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