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Literature summary for 2.1.1.230 extracted from

  • Yin, S.; Jiang, H.; Chen, D.; Murchie, A.I.
    Substrate recognition and modification by the nosiheptide resistance methyltransferase (2015), PLoS ONE, 10, e0122972.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.230

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes, with additional FLAG and HA tags, in Escherichia coli Streptomyces actuosus

Protein Variants

Protein Variants Comment Organism
R135A site-directed mutagenesis, the inactive R135A mutant homodimer binds to the RNA causing a shift in electrophoretic mobility, and the heterodimer composed of active and inactive subunits also binds the RNA efficiently. The inactive heterodimer complex binds the RNA more efficiently than the inactive mutant homodimer Streptomyces actuosus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Streptomyces actuosus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA Streptomyces actuosus
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 S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
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 ?

Organism

Organism UniProt Comment Textmining
Streptomyces actuosus P52391 nosiheptide producer
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Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography and gel filtration Streptomyces actuosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information compared the methylation activity of the Arg135Ala NHR heterodimer with the wild-type NHR homodimer and a series of 29 nt wild-type and mutant RNA substrates. The inactive heterodimer complex binds the RNA more efficiently than the inactive mutant homodimer. Construction of diverse mutant RNA substrates in which A1067 is replaced by adenine structural analogues, A1067G retains significant activity, while 7-deaza-A and 1-methyl-A substitutions at A1067 reduce the activity, overview Streptomyces actuosus ?
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 ?
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
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 Streptomyces actuosus S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
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 ?
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA as 58 nucleotide substrate for methylation, or as shortened 29 nt hairpin substrate, local base-base interactions play an important role in aligning the substrate 2'-hydroxyl group of A1067 for methyl group transfer, stoichiometry of RNA binding by the NHR dimer, overview Streptomyces actuosus S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
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 ?

Subunits

Subunits Comment Organism
dimer SDS-PAGE and gel filtration Streptomyces actuosus

Synonyms

Synonyms Comment Organism
NHR
-
 Streptomyces actuosus
NHR protein
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 Streptomyces actuosus
nosiheptide resistance methyltransferase
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 Streptomyces actuosus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Streptomyces actuosus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Streptomyces actuosus

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Streptomyces actuosus

General Information

General Information Comment Organism
additional information the NHR heterodimer requires only one functional subunit for RNA recognition and enzymatic activity. The catalytic residue is Arg135 Streptomyces actuosus
physiological function the nosiheptide producer Streptomyces actuosis prevents self-intoxication by expressing the enzyme, which methylates the 2'-hydroxyl of 23 S rRNA nucleotide adenosine 1067 within the antibiotic binding site. Methylation at A1067 blocks thiazole binding directly. This region of 23S rRNA is also the binding site for the ribosomal protein L11 Streptomyces actuosus