| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 2.1.1.166 | additional information | generation of Escherichia coli mutant strain BW25113 DELTArrmJ in which the rrmJ gene is substituted by the kanamycin resistance gene. Mg2+-sensitivity is detected in DELTArrmJ cells at 10.5 mM Mg2+. Analysis of a set of late-stage pre50S particles isolated from an Escherichia coli strain DELTArrmJ. Apart from the absence of L16, L35, and L36, major structural differences between these intermediates and the mature 50S subunit are clustered near the peptidyl transferase center, such as H38, H68-71, and H89-93. The ribosomal A-loop of the mature 50S subunit from DELTArrmJ strain displays large local flexibility on nucleotides next to unmethylated U2552. The DELTArrmJ 50S subunit is only 50% active and two times slower than wild-type 50S subunit in rapid subunit association. While the DELTArrmJ 70S ribosomes show no defect in peptide bond formation, peptide release, and ribosome recycling, they translocate with 20% slower rate than wild-type ribosomes in each round of elongation. These defects amplify during synthesis of the full-length proteins and cause overall defect in protein synthesis. The extremely low Mg2+ is able to cause irreversible structural distortions and activity reduction of peptidyl transferase. These 45S particles might be disrupted by low Mg2+ exposure. DELTArrmJ cells exhibit a marked accumulation of 50S fractions compared with wild-type cells at 10.5 mM Mg2+. At 0.5 mM Mg2+, a concentration sufficient to convert all 70S ribosomes into subunits, a 45S peak appears in the sedimentation profile of DELTArrmJ cells | Escherichia coli |
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.1.1.166 | S-adenosyl-L-methionine + uridine2552 in 23S rRNA | Escherichia coli | - |
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA | - |
? | |
| 2.1.1.166 | S-adenosyl-L-methionine + uridine2552 in 23S rRNA | Escherichia coli BW25113 | - |
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA | - |
? | |
| 2.1.1.166 | S-adenosyl-L-methionine + uridine2552 in 23S rRNA | Escherichia coli K12 | - |
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA | - |
? |
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 2.1.1.166 | Escherichia coli | P0C0R7 | - |
- |
| 2.1.1.166 | Escherichia coli BW25113 | P0C0R7 | - |
- |
| 2.1.1.166 | Escherichia coli K12 | P0C0R7 | - |
- |
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.1.1.166 | S-adenosyl-L-methionine + uridine2552 in 23S rRNA | - |
Escherichia coli | S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA | - |
? | |
| 2.1.1.166 | S-adenosyl-L-methionine + uridine2552 in 23S rRNA | - |
Escherichia coli BW25113 | S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA | - |
? | |
| 2.1.1.166 | S-adenosyl-L-methionine + uridine2552 in 23S rRNA | - |
Escherichia coli K12 | S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA | - |
? |
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 2.1.1.166 | FTSJ | - |
Escherichia coli |
| 2.1.1.166 | RlmE | - |
Escherichia coli |
| 2.1.1.166 | RrmJ | - |
Escherichia coli |
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 2.1.1.166 | 30 | - |
assay at | Escherichia coli |
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 2.1.1.166 | 7.5 | - |
assay at | Escherichia coli |
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 2.1.1.166 | S-adenosyl-L-methionine | - |
Escherichia coli |
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 2.1.1.166 | malfunction | absence of RrmJ activity results in severe growth defect and marked accumulation of pre50S assembly intermediates. Absence of the 2'-O-methylation of U2552, the assembly of the 50S subunit is delayed at multiple late stages. Loss of this methylation also results in compromised translation activities, particularly in the initiation and the elongation steps. Immature large subunits from the DELTArrmJ strain are highly sensitive to Mg2+ depletion. A certain level of Mg2+ is essential for the structural integrity of large ribonucleoprotein complexes, such as the ribosome. DELTArrmJ 70S ribosomes are defective in initiation and elongation of protein synthesis. Phenotype, overview | Escherichia coli |
| 2.1.1.166 | physiological function | ribosome biogenesis is a complex process, and dozens of factors are required to facilitate and regulate the subunit assembly in bacteria. The 2'-O-methylation of U2552 in 23S rRNA by methyltransferase RrmJ is a crucial step in late-stage assembly of the 50S subunit, overview | Escherichia coli |