EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   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 |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 |
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA |
- |
? |
| 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 |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 |
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) |
Streptomyces griseus IFO13189 |
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA |
- |
? |
