| Full name: |
Ribosomal RNA small subunit methyltransferase G |
| Synonym: |
GidB, TTHA1971 |
| GI: |
62298017 |
| Orf: |
|
| COG: |
COG0357 |
| UniProt: |
Q9LCY2 |
| Structures: |
|
3G8B |
3G88 |
3G89 |
3G8A |
|
| Complex: |
|
| Enzyme type: |
methyltransferase |
| Position of modification - modification: |
s:510(527) - m7G
|
Comments:
RsmG catalyzes N7-methylation of G527, the universally conserved loop of hairpin 18 in domain I of 16S rRNA in bacteria. In contrast to E. coli RsmG, which has been reported to recognize only intact 30S subunits, T. thermophilus RsmG shows no in vitro methylation activity against native 30S subunits, only low activity with 30S subunits at low magnesium concentration, and maximum activity with deproteinized 16S rRNA. Therefore T. thermophilus probably works on early assembly intermediate of ribosome biogenesis. Also, as other bacteria, the T. thermophilus rsmG mutants acquires resistance to aminoglycoside antibiotic streptomycin. AdoMet is the methyl group donor.
Protein sequence:
MFHGKHPGGLSERGRALLLEGGKALGLDLKPHLEAFSRLYALLQEASGKVNLTALRGEEEVVVKHFLDSL
TLLRLPLWQGPLRVLDLGTGAGFPGLPLKIVRPELELVLVDATRKKVAFVERAIEVLGLKGARALWGRAE
VLAREAGHREAYARAVARAVAPLCVLSELLLPFLEVGGAAVAMKGPRVEEELAPLPPALERLGGRLGEVL
ALQLPLSGEARHLVVLEKTAPTPPAYPRRPGVPERHPLC
Enzymatic activities:
| Reaction
| Substrate
| Type
| Position
|
|
G:m7G
|
rRNA (r) |
SSU/16S/prokaryotic cytosol |
511 |
Publications:
| Title |
Authors |
Journal |
Details |
PubMed Id |
DOI |
| Structural and functional studies of the Thermus thermophilus 16S rRNA methyltransferase RsmG. |
Gregory ST, Demirci H, Belardinelli R, Monshupanee T, Gualerzi C, Dahlberg AE, Jogl G |
RNA |
[details]
|
19622680
|
-
|