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Literature summary for 2.1.1.226 extracted from

  • Salamaszynska-Guz, A.; Rose, S.; Lykkebo, C.; Taciak, B.; Bacal, P.; Uspienski, T.; Douthwaite, S.
    Biofilm formation and motility are promoted by Cj0588-directed methylation of rRNA in Campylobacter jejuni (2018), Front. Cell. Infect. Microbiol., 7, 533 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.226

Cloned(Commentary)

Cloned (Comment) Organism
gene tlyA, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Campylobacter jejuni subsp. jejuni

Protein Variants

Protein Variants Comment Organism
D162A site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type Campylobacter jejuni subsp. jejuni
K188A site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type Campylobacter jejuni subsp. jejuni
K80A site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type Campylobacter jejuni subsp. jejuni
additional information generation of an inactive Cj0588 deletion mutant. The Campylobacter jejuni 4051cj0588 null-mutant is complemented in trans with plasmid-encoded versions of the cj0588 gene. Inactivation of Cj0588 hinders Campylobacter jejuni motility and impairs biofilm formation, phenotype, overview Campylobacter jejuni subsp. jejuni

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic analysis Campylobacter jejuni subsp. jejuni

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA Campylobacter jejuni subsp. jejuni
-
 S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
 ?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA Campylobacter jejuni subsp. jejuni NCTC 11168
-
 S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
 ?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA Campylobacter jejuni subsp. jejuni ATCC 700819
-
 S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
 ?

Organism

Organism UniProt Comment Textmining
Campylobacter jejuni subsp. jejuni Q0PAS9 serotype O:2
-
Campylobacter jejuni subsp. jejuni ATCC 700819 Q0PAS9 serotype O:2
-
Campylobacter jejuni subsp. jejuni NCTC 11168 Q0PAS9 serotype O:2
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Campylobacter jejuni subsp. jejuni

Source Tissue

Source Tissue Comment Organism Textmining
additional information polysome profiles Campylobacter jejuni subsp. jejuni
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 50S rRNA is used as substrate in activity assays. Mass spectrometric analyses of Campylobacter jejuni 23S rRNA Campylobacter jejuni subsp. jejuni ?
-
-
additional information 50S rRNA is used as substrate in activity assays. Mass spectrometric analyses of Campylobacter jejuni 23S rRNA Campylobacter jejuni subsp. jejuni NCTC 11168 ?
-
-
additional information 50S rRNA is used as substrate in activity assays. Mass spectrometric analyses of Campylobacter jejuni 23S rRNA Campylobacter jejuni subsp. jejuni ATCC 700819 ?
-
-
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
-
 Campylobacter jejuni subsp. jejuni S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
 ?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
-
 Campylobacter jejuni subsp. jejuni NCTC 11168 S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
 ?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
-
 Campylobacter jejuni subsp. jejuni ATCC 700819 S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
 ?

Synonyms

Synonyms Comment Organism
Cj0588
-
 Campylobacter jejuni subsp. jejuni
rRNA 2'-O-methyltransferase
-
 Campylobacter jejuni subsp. jejuni
TlyA
-
 Campylobacter jejuni subsp. jejuni

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Campylobacter jejuni subsp. jejuni

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Campylobacter jejuni subsp. jejuni

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Campylobacter jejuni subsp. jejuni

General Information

General Information Comment Organism
malfunction deletion of the cj0588 gene in Campylobacter jejuni or substitution with alanine of K80, D162, or K188 in the catalytic center of the enzyme cause complete loss of 2'-O-methylation activity. Campylobacter jejuni strains expressing catalytically inactive versions of Cj0588 have the same phenotype as cj0588-null mutants, and show altered tolerance to capreomycin due to perturbed ribosomal subunit association, reduced motility and impaired ability to form biofilms. These functions are reestablished when methyltransferase activity is restored Campylobacter jejuni subsp. jejuni
additional information mechanism of Cj0588 action, overview. Homology modelling of the tertiary structure of the Cj0588 catalytic domain using Mycobacterium tuberculosis TlyA structure (PDB ID 5EOV) as a template. The HhaI methyltransferase structure (PDB ID 2HMY) is used to superimpose the AdoMet cofactor. Three-dimensional modeling of the catalytic domain of Cj0588 reveals a structure typical for 2'-O-methyltransferases with a seven-stranded beta-sheet between five alpha-helix layers and four residues K80, D162, K188 and E245 that comprise the catalytic center Campylobacter jejuni subsp. jejuni
physiological function the enzyme TlyA is an rRNA 2'-O-methyltransferase associated with resistance to cyclic peptide antibiotics such as capreomycin. The bacterial pathogen Campylobacter jejuni possesses the TlyA homologue Cj0588, which contributes to virulence, and is a type I homologue of TlyA that 2'-O-methylates 23S rRNA nucleotide C1920. The contribution of Cj0588 to virulence is a consequence of the enzyme's ability to methylate its rRNA Campylobacter jejuni subsp. jejuni