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Literature summary extracted from

  • Kimura, S.; Ikeuchi, Y.; Kitahara, K.; Sakaguchi, Y.; Suzuki, T.; Suzuki, T.
    Base methylations in the double-stranded RNA by a fused methyltransferase bearing unwinding activity (2012), Nucleic Acids Res., 40, 4071-4085.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.173 gene rlmKL, DNA and amino acid sequence determination and analysis, gene rlmL/ycbY has been renamed rlmKL Escherichia coli
2.1.1.264 gene rlmK, expression in Escherichia coli DELTArlmKL mutant Neisseria meningitidis
2.1.1.264 gene rlmL, renamed rlmKL, encodes a fused methyltransferase responsible for forming both m7G2069 and m2G2445 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.173 additional information generation of several base-flipping mutant enzymes lacking m2G2445 formation activity, overview Escherichia coli
2.1.1.264 D195A site-directed mutagenesis, the mutation does not affect the methylation activity Escherichia coli
2.1.1.264 D568A site-directed mutagenesis, the D568A mutation in the C-terminal domain does not rescue m7G2069 formation, but m2G2445 is efficiently formed in this mutant Escherichia coli
2.1.1.264 D597A site-directed mutagenesis, the mutation does not affect the methylation activity Escherichia coli
2.1.1.264 N309A site-directed mutagenesis, the N309A mutation in the NTD impairs m2G2445 formation, but rescues m7G2069 formation Escherichia coli
2.1.1.264 N397A site-directed mutaagenesis, the N397A mutant exhibits no m2G2445 formation but rescues m7G2069 formation Escherichia coli
2.1.1.264 R530A site-directed mutagenesis, the mutation does not affect the methylation activity Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.173 Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.173 S-adenosyl-L-methionine + guanine2069 in 23S rRNA Escherichia coli
-
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
?
2.1.1.173 S-adenosyl-L-methionine + guanine2445 in 23S rRNA Escherichia coli
-
S-adenosyl-L-homocysteine + N2-methylguanine2445 in 23S rRNA
-
?
2.1.1.264 additional information Escherichia coli the enzyme also catalyzes the N2-methylation of guanine2445 in 23S rRNA, RlmL activity, reaction of EC 2.1.1.173 ?
-
?
2.1.1.264 S-adenosyl-L-methionine + guanine2069 in 23S rRNA Escherichia coli RlmK activity in helix 74 of Escherichia coli 23S rRNA S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
?
2.1.1.264 S-adenosyl-L-methionine + guanine2069 in 23S rRNA Neisseria meningitidis RlmK activity in helix 74 of Escherichia coli 23S rRNA S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
?
2.1.1.264 S-adenosyl-L-methionine + guanine2069 in 23S rRNA Neisseria meningitidis MC58 RlmK activity in helix 74 of Escherichia coli 23S rRNA S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.173 Escherichia coli
-
gene rlmL/ycbY has been renamed rlmKL
-
2.1.1.264 Escherichia coli
-
gene rlmL, renamed rlmKL
-
2.1.1.264 Neisseria meningitidis Q9JYY8 gene rlmK
-
2.1.1.264 Neisseria meningitidis MC58 Q9JYY8 gene rlmK
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.173 additional information helix 80 and the 12 nt ss region are critical sites necessary for m2G2445 and m7G2069 formation. Transcript 7, which lacks helix 80 and the 12 nt single-strand region, is not methylated at either position Escherichia coli ?
-
?
2.1.1.173 S-adenosyl-L-methionine + guanine2069 in 23S rRNA
-
Escherichia coli S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
?
2.1.1.173 S-adenosyl-L-methionine + guanine2445 in 23S rRNA
-
Escherichia coli S-adenosyl-L-homocysteine + N2-methylguanine2445 in 23S rRNA
-
?
2.1.1.173 S-adenosyl-L-methionine + guanine2445 in 23S rRNA duplex formation of H74 is not required for the m2G2445 formation. The 29-mer single-stranded transcript 6, which consists of residues C2422 to A2450, can form m2G2445 efficiently Escherichia coli S-adenosyl-L-homocysteine + N2-methylguanine2445 in 23S rRNA
-
?
2.1.1.264 additional information the enzyme also catalyzes the N2-methylation of guanine2445 in 23S rRNA, RlmL activity, reaction of EC 2.1.1.173 Escherichia coli ?
-
?
2.1.1.264 S-adenosyl-L-methionine + guanine2069 in 23S rRNA RlmK activity in helix 74 of Escherichia coli 23S rRNA Escherichia coli S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
?
2.1.1.264 S-adenosyl-L-methionine + guanine2069 in 23S rRNA RlmK activity in helix 74 of Escherichia coli 23S rRNA Neisseria meningitidis S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
?
2.1.1.264 S-adenosyl-L-methionine + guanine2069 in 23S rRNA RlmK activity in helix 74 of Escherichia coli 23S rRNA Neisseria meningitidis MC58 S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
?

Subunits

EC Number Subunits Comment Organism
2.1.1.173 More RlmKL is a fused methyltransferase consisting of an N-terminal RlmL domain and a C-terminal RlmK domain Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.1.1.173 m2G2445 methyltransferase
-
Escherichia coli
2.1.1.173 RlmKL
-
Escherichia coli
2.1.1.173 RlmL
-
Escherichia coli
2.1.1.264 rlmK
-
Escherichia coli
2.1.1.264 rlmK
-
Neisseria meningitidis
2.1.1.264 RlmKL
-
Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.173 37
-
assay at Escherichia coli
2.1.1.264 37
-
assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.173 7.5
-
assay at Escherichia coli
2.1.1.264 7.5
-
assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.173 S-adenosyl-L-methionine
-
Escherichia coli
2.1.1.264 S-adenosyl-L-methionine
-
Escherichia coli

General Information

EC Number General Information Comment Organism
2.1.1.173 malfunction deletion of rlmL/ycbY results in a slight growth reduction phenotype Escherichia coli
2.1.1.173 additional information RlmKL is involved in the efficient assembly of 50S subunit in a mutant strain lacking an RNA helicase deaD Escherichia coli
2.1.1.173 physiological function cooperative methylation of helix 74 by RlmKL plays a key role in the efficient assembly of the 50S subunit, RlmKL enzyme is an example of a methyltransferase catalyzing two mechanistically different types of RNA modification. RlmKL has an unwinding activity of Helix 74, facilitating cooperative methylations of m7G2069 and m2G2445 during biogenesis of 50S subunit. Methyltransferase RlmL, encoded by rlmL/ycbY, catalyzes S-adenosyl-L-methionine-dependent m2G2445 formation Escherichia coli
2.1.1.264 malfunction Neisseria meningitidis rlmL and rlmK homologues rescue m2G2445 and m7G2069 formation, respectively, in the Escherichia coli DELTArlmKL strain Escherichia coli
2.1.1.264 malfunction Neisseria meningitidis rlmL and rlmK homologues rescue m2G2445 and m7G2069 formation, respectively, in the Escherichia coli DELTArlmKL strain, overview Neisseria meningitidis
2.1.1.264 physiological function rlmKL encodes a fused methyltransferase responsible for forming both m7G2069 and m2G2445, the N-terminal RlmL activity for m2G2445 formation is significantly enhanced by the C-terminal RlmK. RlmKL has an unwinding activity of Helix 74, facilitating cooperative methylations of m7G2069 and m2G2445 during biogenesis of 50S subunit. For unwinding single-stranded RNA is a good substrate for RlmKL, substrate speccificity, overview. RlmKL is involved in the efficient assembly of 50S subunit in a mutant strain lacking an RNA helicase deaD Escherichia coli