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Literature summary for 2.1.1.264 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)

Cloned (Comment) Organism
gene rlmK, expression in Escherichia coli DELTArlmKL mutant Neisseria meningitidis
gene rlmL, renamed rlmKL, encodes a fused methyltransferase responsible for forming both m7G2069 and m2G2445 Escherichia coli

Protein Variants

Protein Variants Comment Organism
D195A site-directed mutagenesis, the mutation does not affect the methylation activity Escherichia coli
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
D597A site-directed mutagenesis, the mutation does not affect the methylation activity Escherichia coli
N309A site-directed mutagenesis, the N309A mutation in the NTD impairs m2G2445 formation, but rescues m7G2069 formation Escherichia coli
N397A site-directed mutaagenesis, the N397A mutant exhibits no m2G2445 formation but rescues m7G2069 formation Escherichia coli
R530A site-directed mutagenesis, the mutation does not affect the methylation activity Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 ?
-
?
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
-
?
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
-
?
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

Organism UniProt Comment Textmining
Escherichia coli
-
gene rlmL, renamed rlmKL
-
Neisseria meningitidis Q9JYY8 gene rlmK
-
Neisseria meningitidis MC58 Q9JYY8 gene rlmK
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
?
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
-
?
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
-
?
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
-
?

Synonyms

Synonyms Comment Organism
rlmK
-
Escherichia coli
rlmK
-
Neisseria meningitidis
RlmKL
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
Escherichia coli

General Information

General Information Comment Organism
malfunction Neisseria meningitidis rlmL and rlmK homologues rescue m2G2445 and m7G2069 formation, respectively, in the Escherichia coli DELTArlmKL strain Escherichia coli
malfunction Neisseria meningitidis rlmL and rlmK homologues rescue m2G2445 and m7G2069 formation, respectively, in the Escherichia coli DELTArlmKL strain, overview Neisseria meningitidis
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