EC Number   |
Substrates |
Products |
Reversibility |
|---|
   2.1.1.170 | more |
the pseudoknot mutant (PKMut) G505A/C507U for 5'-domain RNA is obtained by site-directed mutagenesis. All 5'-domain RNA constructs are extended at the 3'-end to base pair with a fluorophore-labelled complementary DNA oligomer and in vitro transcribed |
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| 2.1.1.170 | more |
RsmG enzyme binds to Escherichia coli small subunit precursor rRNAs. Ability of RsmG to bind various premature small subunit ribosomal RNAs with contrasting affinities, overview. Protein RsmG binds with approximately 15times higher affinity to premature 16S rRNA with the full leader sequence compared to that of mature 16S rRNA. Various r-proteins which bind to the 5'-domain influence RsmG binding. The binding cooperativity between RsmG and r-proteins is sensitive to the maturation status of premature small subunit rRNA. But neither the maturation of 16S rRNA nor the presence of various r-proteins significantly influence the methylation activity of RsmG |
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| 2.1.1.170 | S-adenosyl-L-methionine + guanine527 in 16S rRNA |
methylations concentrated in the decoding site of the 30S ribosomal subunit may act to fine tune codon recognition in a manner similar to tRNA modifications. The intact 30S subunit is very unlikely to be the natural substrate for Thermus thermophilus RsmG in vivo. This interpretation is consistent with the position of G527 in the intact 30S subunit, where it is buried and would be inaccessible for methylation without substantial unfolding of the local subunit structure. Deproteinized 16S rRNA is the most active substrate in vitro. In vivo, several ribosomal proteins probably begin binding to the nascent 16S rRNA transcript prior to its completion, making an early assembly intermediate a plausible candidate for the biological substrate of RsmG |
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA |
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| 2.1.1.170 | S-adenosyl-L-methionine + guanine527 in 16S rRNA |
the methyltransferase RsmG methylates the N7 position of nucleotide G535 in 16S rRNA of Bacillus subtilis (corresponding to G527 in Escherichia coli). Nucleotide G527 is situated within a hairpin loop (the socalled 530 loop) that is one of the most highly conserved features of 16S rRNA |
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA |
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| 2.1.1.170 | S-adenosyl-L-methionine + guanine527 in 16S rRNA |
the most active substrate for Thermus thermophilus RsmG in vitro is deproteinized 16S rRNA. 30S subunits in their native conformation are not a proper substrate, removal of Mg2+ ions from the subunit is required to open the structure sufficiently to expose elements involved in enzyme binding. Identification of methylated nucleotide |
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA |
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? |
| 2.1.1.170 | S-adenosyl-L-methionine + guanine527 in 16S rRNA |
the methyltransferase RsmG methylates the N7 position of nucleotide G535 in 16S rRNA of Bacillus subtilis (corresponding to G527 in Escherichia coli) |
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA |
- |
? |
| 2.1.1.170 | S-adenosyl-L-methionine + guanine527 in 16S rRNA |
the methyltransferase RsmG methylates the N7 position of nucleotide G535 in 16S rRNA of Bacillus subtilis (corresponding to G527 in Escherichia coli), identification of the exact target site of RsmG methylation |
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA |
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? |
| 2.1.1.170 | S-adenosyl-L-methionine + guanine527 in 16S rRNA |
GidB is a m7G methyltransferase specific for 16S rRNA, identification of methylated nucleotide |
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA |
- |
? |
| 2.1.1.170 | S-adenosyl-L-methionine + guanine527 in 16S rRNA |
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S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA |
- |
? |
| 2.1.1.170 | S-adenosyl-L-methionine + guanine527 in 16S rRNA |
RsmG binds to 30S 5'-domain and methylates N7 of G527 that is located at the highly conserved 530 loop of 16S helix 18. Substrates rRNAs and are 5'-leader rRNA fragments |
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA |
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