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Literature summary extracted from

  • Gregory, S.T.; Demirci, H.; Belardinelli, R.; Monshupanee, T.; Gualerzi, C.; Dahlberg, A.E.; Jogl, G.
    Structural and functional studies of the Thermus thermophilus 16S rRNA methyltransferase RsmG (2009), RNA, 15, 1693-1704.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.170
-
 Thermus thermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.170 microbatch technique under oil at 4°C. Determination of the structure of RsmG (249 amino acids) in three different crystal forms: the enzyme in complex with the cofactor S-adensosyl-L-methionine, the enzyme in complex with S-adenosyl-L-homocysteine, the enzyme in complex with adenosine monophosphate and S-adenosyl-L-methionine. RsmG X-ray crystal structures at up to 1.5 A resolution. Cofactor-bound crystal structures of RsmG reveals a positively charged surface area remote from the active site that binds an adenosine monophosphate molecule Thermus thermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.170 Mg2+ the 30S subunits in their native conformation are not a proper substrate and removal of Mg2+ ions from the subunit is required to open the structure sufficiently to expose elements involved in enzyme binding Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.170 S-adenosyl-L-methionine + guanine527 in 16S rRNA Thermus thermophilus 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
-
 ?
2.1.1.170 S-adenosyl-L-methionine + guanine527 in 16S rRNA Thermus thermophilus HB8 / ATCC 27634 / DSM 579 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
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.170 Thermus thermophilus Q9LCY2
-
-
2.1.1.170 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 Q9LCY2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.170 the AdoMet cofactor is tightly bound in RsmG and copurifies with the recombinant protein Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 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 S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
-
 ?
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
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.170 16S rRNA methyltransferase RsmG
-
 Thermus thermophilus
2.1.1.170 gidB
-
 Thermus thermophilus
2.1.1.170 ribosomal RNA small subunit methyltransferase G
-
 Thermus thermophilus
2.1.1.170 rsmG
-
 Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.170 S-adenosyl-L-methionine S-adenosyl-L-methionine is bound in a canonical conformation above the beta-sheet and close to the conserved GxGxG methyltransferase signature motif (residues 88–92 between strand beta1 and helix alpha4). The AdoMet cofactor is tightly bound in RsmG and copurifies with the recombinant protein Thermus thermophilus

General Information

EC Number General Information Comment Organism
2.1.1.170 malfunction construction of an rsmG null allele by deleting the rsmG coding sequence and replacing it with htk, encoding a heat-stable kanamycin adenyltransferase. This null allele retains the very N- and C-terminal rsmG coding sequences, in-frame with the htk coding sequence, in order to maintain the rsmG–parA overlap and minimize any effects on parA expression. This allele is designated DrsmGThtk2 and the mutant containing this allele is designated HG 917. Thermus thermophilus rsmG mutants are weakly resistant to the aminoglycoside antibiotic streptomycin. Growth competition experiments indicate a physiological cost to loss of RsmG activity, consistent with the conservation of the modification site in the decoding region of the ribosome Thermus thermophilus