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Information on EC 2.1.1.166 - 23S rRNA (uridine2552-2'-O)-methyltransferase
for references in articles please use BRENDA:EC2.1.1.166
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.166 23S rRNA (uridine2552-2'-O)-methyltransferase
IUBMB Comments
The enzyme catalyses the 2′-O-methylation of the universally conserved U2552 in the A loop of 23S rRNA .
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
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uridine2552 in 23S rRNA
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2'-O-methyluridine2552 in 23S rRNA
Synonyms
ftsj2, mj0697, heat shock protein rrmj, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FTSJ
RlmE
RrmJ
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + uridine2552 in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
S-adenosyl-L-methionine + uridine2552 in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
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S-adenosyl-L-methionine + uridine2552 in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
mechanism, based on modeling studies and the structure of the 50S ribosome, a two-step model is proposed where the A loop undocks from the tightly packed 50S ribosomal subunit, allowing RrmJ to gain access to the substrate nucleotide U2552, and where U2552 undergoes base flipping, allowing the enzyme to methylate the 2'-O position of the ribose
A0A140N5X9
S-adenosyl-L-methionine + uridine2552 in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
a reaction mechanism for the methyltransfer activity of RrmJ is proposed
A0A140N5X9
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:23S rRNA (uridine2552-2'-O)-methyltransferase
The enzyme catalyses the 2'-O-methylation of the universally conserved U2552 in the A loop of 23S rRNA [3].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
A0A140N5X9
Substrates: U2552 is an ubiquitously methylated residue
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
A0A140N5X9
Substrates: the enzyme is responsible for the 2'-O methylation of the universally conserved U2552 in the A loop of 23S rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
A0A140N5X9
Substrates: the 2'-O-ribose methylation of the universally conserved base U2552 in the A-loop of the 23 S rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
A0A140N5X9
Substrates: in vivo methylation of 23S rRNA by FtsJ goes to near completion
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
A0A140N5X9
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
A0A140N5X9
Substrates: the isolated unmodified A loop serves as the minimal methylation substrate of wild-type RrmJ in vitro. 50S ribosomal subunits prepared from the rrmJ deletion strain appear to serve as substrates for RrmJ in vitro, while naked 23S rRNA or 40S ribosomal particles that are prepared from the rrmJ deletion strain are not methylated by purified RrmJ. This finding suggests that either the correct folding of the 23S rRNA or additional protein-protein interactions are necessary for the substrate recognition. A positively charged, highly conserved ridge in RrmJ appears to play a significant role in 23S rRNA binding and methylation. A structural model is provided of how the A loop of the 23S rRNA binds to RrmJ. Based on modeling studies and the structure of the 50S ribosome, a two-step model is proposed where the A loop undocks from the tightly packed 50S ribosomal subunit, allowing RrmJ to gain access to the substrate nucleotide U2552, and where U2552 undergoes base flipping, allowing the enzyme to methylate the 2'-O position of the ribose
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
A0A140N5X9
Substrates: identification of the methylated nucleotide as 2'-O-methyluridine 2552, by reverse phase high performance liquid chromatography analysis, boronate affinity chromatography, and hybridization-protection experiments. In vitro, FtsJ does not efficiently methylate ribosomes purified from a strain producing FtsJ, suggesting that these ribosomes are already methylated in vivo by FtsJ. FtsJ is active on ribosomes and on the 50 S ribosomal subunit, but is inactive on free rRNA, suggesting that its natural substrate is ribosomes or a pre-ribosomal ribonucleoprotein particle
Products: -
Products: -
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S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
A0A140N5X9
Substrates: the 2'-O-ribose methylation of the universally conserved base U2552 in the A-loop of the 23 S rRNA. The active site of RrmJ appears to be formed by a catalytic triad consisting of two lysine residues, Lys-38 and Lys-164, and the negatively charged residue Asp-124. Another highly conserved residue, Glu-199, that is present in the active site of RrmJ and VP39 appears to play only a minor role in the methyltransfer reaction in vivo. A reaction mechanism for the methyltransfer activity of RrmJ is proposed
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
A0A140N5X9
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
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Substrates: rrmJ gene encodes a methyltransferase that modifies the U2552 residue of 23S rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
A0A140N5X9
Substrates: U2552 is an ubiquitously methylated residue
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
A0A140N5X9
Substrates: the enzyme is responsible for the 2'-O methylation of the universally conserved U2552 in the A loop of 23S rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
A0A140N5X9
Substrates: the 2'-O-ribose methylation of the universally conserved base U2552 in the A-loop of the 23 S rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
A0A140N5X9
Substrates: in vivo methylation of 23S rRNA by FtsJ goes to near completion
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
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Substrates: rrmJ gene encodes a methyltransferase that modifies the U2552 residue of 23S rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma of Lung
FTSJ2, a Heat Shock-Inducible Mitochondrial Protein, Suppresses Cell Invasion and Migration.
Carcinogenesis
MiR-542-3p exerts tumor suppressive functions in non-small cell lung cancer cells by upregulating FTSJ2.
Carcinoma, Non-Small-Cell Lung
FTSJ2, a Heat Shock-Inducible Mitochondrial Protein, Suppresses Cell Invasion and Migration.
Carcinoma, Non-Small-Cell Lung
MiR-542-3p exerts tumor suppressive functions in non-small cell lung cancer cells by upregulating FTSJ2.
Lung Neoplasms
FTSJ2, a Heat Shock-Inducible Mitochondrial Protein, Suppresses Cell Invasion and Migration.
Lung Neoplasms
Integrative genomic and gene expression analysis of chromosome 7 identified novel oncogene loci in non-small cell lung cancer.
Lung Neoplasms
MiR-542-3p exerts tumor suppressive functions in non-small cell lung cancer cells by upregulating FTSJ2.
Neoplasms
FTSJ2, a Heat Shock-Inducible Mitochondrial Protein, Suppresses Cell Invasion and Migration.
Neoplasms
Identification and characterization of FTSJ2, a novel human nucleolar protein homologous to bacterial ribosomal RNA methyltransferase.
Neoplasms
MiR-542-3p exerts tumor suppressive functions in non-small cell lung cancer cells by upregulating FTSJ2.
Rhabdomyosarcoma
FTSJ2, a Heat Shock-Inducible Mitochondrial Protein, Suppresses Cell Invasion and Migration.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
A0A140N5X9
changes in apparent Km-values for 50S subunit binding in RrmJ mutant proteins
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additional information
additional information
A0A140N5X9
apparent Km values for 50S ribosomal subunits. The apparent Km value for 23S rRNA within 50S ribosomal subunits is 0.0008 mM at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
A0A140N5X9
changes in apparent kcat-values for 50S subunit binding in RrmJ mutant proteins
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additional information
additional information
A0A140N5X9
the apparent kcat value for 23 S rRNA within 50S ribosomal subunits is 0.001/sec mM at 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 60
A0A140N5X9
50°C: about 75% of maximal activity, 60°C: about 95% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
A0A140N5X9
absence of functional RrmJ causes the cellular accumulation of the individual ribosomal subunits at the expense of the functional 70S ribosomes
physiological function
malfunction
A0A140N5X9
rrmJ-deficient strain exhibit growth and translational defects compared to the wild-type strain. Growth rates of the rrmJ mutant are decreased at both low and high temperatures. Protein synthesis activity is reduced up to 65% when S30 rrmJ mutant extracts are tested in a coupled in vitro transcription/translation assay. In vitro methylation of these extracts by RrmJ partially restores protein synthesis activity
malfunction
A0A140N5X9
lack of U2552 methylation, obtained in rrmJ-deficient mutants, results in a decrease in programmed +1 and -1 translational frameshifing and a decrease in readthrough of UAA and UGA stop codons. The increased translational accuracy of rrmJ-deficient strains suggests that the interaction between aminoacyl-tRNA and U2552 is important for selection of the correct tRNA at the ribosomal A site, and supports the idea that translational accuracy in vivo is optimal rather than maximal, thus pointing to the participation of recoding events in the normal cell physiology
malfunction
A0A140N5X9
absence of this methylation, which occurs late in the maturation process of the ribosome, appears to cause the destabilization and premature dissociation of the 50 S ribosomal subunit
malfunction
A0A140N5X9
null mutations in ftsJ show a dramatically altered ribosome profile, a severe growth disadvantage, and a temperature-sensitive phenotype
malfunction
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rrmJ gene deletion causes a severe growth defect and accumulation of aberrant 50S ribosomal subunits in DELTArrmJ. Overexpression of GTPase Der suppresses growth impairment, effects of several Der mutants, overview. In a rrmJ deletion strain, two GTPase domains of Der regulate its association with 50S subunit via the KH-like domain. Phenotypes, overview
malfunction
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enzyme deletion results in slow growth and accumulation of the 45S particle
malfunction
an absence of just two rRNA modification enzymes is conditionally lethal (at 20°C): RlmE and RluC (c.f. EC 5.4.99.24). At a permissive temperature (37°C), this double knockout is shown to abolish four modifications and be defective in ribosome assembly, though not more so than the RlmE single knockout. However, the double knockout exhibits an even lower rate of tripeptide synthesis than does the single knockout, suggesting an even more defective ribosomal translocation. A combination knockout of the five critical-region-modifying enzymes RluC, RlmKL, RlmN, RlmM, and RluE, which synthesize five of the seven critical-region modifications and 14 rRNA and tRNA modifications altogether, is viable. This five-knockout combination has minimal effects on ribosome assembly and frameshifting at 37°C, but greater effects on ribosome assembly and in vitro peptidyl transferase activity at cooler temperatures
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
malfunction
-
enzyme deletion results in slow growth and accumulation of the 45S particle
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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
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malfunction
-
an absence of just two rRNA modification enzymes is conditionally lethal (at 20°C): RlmE and RluC (c.f. EC 5.4.99.24). At a permissive temperature (37°C), this double knockout is shown to abolish four modifications and be defective in ribosome assembly, though not more so than the RlmE single knockout. However, the double knockout exhibits an even lower rate of tripeptide synthesis than does the single knockout, suggesting an even more defective ribosomal translocation. A combination knockout of the five critical-region-modifying enzymes RluC, RlmKL, RlmN, RlmM, and RluE, which synthesize five of the seven critical-region modifications and 14 rRNA and tRNA modifications altogether, is viable. This five-knockout combination has minimal effects on ribosome assembly and frameshifting at 37°C, but greater effects on ribosome assembly and in vitro peptidyl transferase activity at cooler temperatures
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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
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physiological function
A0A140N5X9
the RrmJ-catalyzed methylation of Um2552 in 23S RNA strengthens ribosomal subunit interactions, increases protein synthesis activity, and improves cell growth rates even at non-heat shock temperatures
physiological function
A0A140N5X9
the 23S rRNA modification is critical for ribosome stability
physiological function
-
the enzyme is an assembly factor that acts at a late step of 50S formation
physiological function
-
in an Escherichia coli strain lacking SAH nucleosidase Mtn, in which cellular SAM is down-regulated, hypomodification of several methylation sites is observed, including 2'-O-methylation at position 2552 (Um2552) of 23S rRNA. There is a severe growth defect of the strain with significant accumulation of 45S ribosomal precursor harboring 23S rRNA with hypomodified Um2552. The growth defect is partially restored by overexpression of SAM-dependent methyltransferase RlmE
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
physiological function
-
the enzyme is an assembly factor that acts at a late step of 50S formation
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physiological function
-
in an Escherichia coli strain lacking SAH nucleosidase Mtn, in which cellular SAM is down-regulated, hypomodification of several methylation sites is observed, including 2'-O-methylation at position 2552 (Um2552) of 23S rRNA. There is a severe growth defect of the strain with significant accumulation of 45S ribosomal precursor harboring 23S rRNA with hypomodified Um2552. The growth defect is partially restored by overexpression of SAM-dependent methyltransferase RlmE
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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
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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
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Show AA Sequence and Transmembrane Helices (8103 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the FtsJ protein at 1.5 A resolution in complex with its cofactor S-adenosyl-L-methionine
A0A140N5X9
identification of a conserved tetrad K-D-K-H in the family of small nucleolar RNA-guided ribose 2'-O-methyltransferases related to fibrillarin. The corresponding functional groups of putative catalytic tetrads of Escherichia coli RrmJ and Methanococcus jannaschii Mj0697 may be superimposed in space. The invariant residues K164 in RrmJ and K179 in Mj0697 are observed in two distinct locations in the primary sequence, suggesting an interesting case of migration of the conserved side chain within the framework of the active site
identification of a conserved tetrad K-D-K-H in the family of small nucleolar RNA-guided ribose 2'-O-methyltransferases related to fibrillarin. The corresponding functional groups of putative catalytic tetrads of Escherichia coli RrmJ and Methanococcus jannaschii Mj0697 may be superimposed in space. The invariant residues K164 in RrmJ and K179 in Mj0697 are observed in two distinct locations in the primary sequence, suggesting an interesting case of migration of the conserved side chain within the framework of the active site
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identification of a conserved tetrad K-D-K-H in the family of small nucleolar RNA-guided ribose 2'-O-methyltransferases related to fibrillarin. The corresponding functional groups of putative catalytic tetrads of Escherichia coli RrmJ and Methanococcus jannaschii Mj0697 may be superimposed in space. The invariant residues K164 in RrmJ and K179 in Mj0697 are observed in two distinct locations in the primary sequence, suggesting an interesting case of migration of the conserved side chain within the framework of the active site
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D124A
A0A140N5X9
the mutant D124A is unable to rescue the growth defect of the rrmJ deletion strain, indicating that this mutation causes the inactivation of RrmJ in vivo
D136N
D83A
A0A140N5X9
the mutant D83A is unable to rescue the growth defect of the rrmJ deletion strain, indicating that this mutation causes the inactivation of RrmJ in vivo
E199A
A0A140N5X9
the RrmJ deletion strains expressing the E199A variant protein shows only slight growth defects, indicating that the residue is not as important in the catalytic mechanism
F166A
A0A140N5X9
decrease in S-adenosyl-L-methionine binding affinity and/or the presence of a certain amount of an inactive yet stably folded RrmJ mutant species
F37A/L39A
A0A140N5X9
mutant strain shows ribosome profiles that are indistinguishable from wild-type ribosome profile
K164A
A0A140N5X9
the mutant D83A is unable to rescue the growth defect of the rrmJ deletion strain, indicating that this mutation causes the inactivation of RrmJ in vivo
K38A
A0A140N5X9
the mutant D83A is unable to rescue the growth defect of the rrmJ deletion strain, indicating that this mutation causes the inactivation of RrmJ in vivo
Q67A/Y68A
A0A140N5X9
mutant strain shows ribosome profiles that are indistinguishable from wild-type ribosome profile
R32A/R34A
A0A140N5X9
R32A/R34A mutant strain accumulates larger amounts of 30S and 50S ribosomal subunits than wild-type strains under nonstringent salt conditions, and has a significant amount of 40S ribosomal particles under stringent salt conditions
Y201A
A0A140N5X9
the RrmJ deletion strains expressing the Y201A variant protein shows only slight growth defects, indicating that the residue is not as important in the catalytic mechanism
additional information
D136N
A0A140N5X9
D136N mutant strain accumulates larger amounts of 30S and 50S ribosomal subunits than wild-type strains under nonstringent salt conditions, and has a significant amount of 40S ribosomal particles under stringent salt conditions
additional information
A0A140N5X9
rrmJ-deficient strain exhibit growth and translational defects compared to the wild-type strain. Growth rates of the rrmJ mutant are decreased at both low and high temperatures. Protein synthesis activity is reduced up to 65% when S30 rrmJ mutant extracts are tested in a coupled in vitro transcription/translation assay. In vitro methylation of these extracts by RrmJ partially restores protein synthesis activity
additional information
-
rrmJ-deficient strain exhibit growth and translational defects compared to the wild-type strain. Growth rates of the rrmJ mutant are decreased at both low and high temperatures. Protein synthesis activity is reduced up to 65% when S30 rrmJ mutant extracts are tested in a coupled in vitro transcription/translation assay. In vitro methylation of these extracts by RrmJ partially restores protein synthesis activity
additional information
A0A140N5X9
lack of U2552 methylation, obtained in rrmJ-deficient mutants, results in a decrease in programmed +1 and -1 translational frameshifing and a decrease in readthrough of UAA and UGA stop codons. The increased translational accuracy of rrmJ-deficient strains suggests that the interaction between aminoacyl-tRNA and U2552 is important for selection of the correct tRNA at the ribosomal A site, and supports the idea that translational accuracy in vivo is optimal rather than maximal, thus pointing to the participation of recoding events in the normal cell physiology
additional information
A0A140N5X9
extensive site-directed mutagenesis of the residues conserved in RrmJ and characterization of the mutant proteins both in vivo and in vitro
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
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
-
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a chimera protein of RrmJ fused to a chitin-binding domain was purified by affinity chromatography on a chitin affinity column
A0A140N5X9
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Caldas, T.; Binet, E.; Bouloc, P.; Richarme, G.
Translational defects of Escherichia coli mutants deficient in the Um(2552) 23S ribosomal RNA methyltransferase RrmJ/FTSJ
Biochem. Biophys. Res. Commun.
271
714-718
2000
Escherichia coli (A0A140N5X9), Escherichia coli
brenda
Feder, M.; Pas, J.; Wyrwicz, L.S.; Bujnicki, J.M.
Molecular phylogenetics of the RrmJ/fibrillarin superfamily of ribose 2'-O-methyltransferases
Gene
302
129-138
2003
Escherichia coli, Methanocaldococcus jannaschii
brenda
Widerak, M.; Kern, R.; Malki, A.; Richarme, G.
U2552 methylation at the ribosomal A-site is a negative modulator of translational accuracy
Gene
347
109-114
2005
Escherichia coli (A0A140N5X9)
brenda
Ching, Y.P.; Zhou, H.J.; Yuan, J.G.; Qiang, B.Q.; Kung Hf, H.F.; Jin, D.Y.
Identification and characterization of FTSJ2, a novel human nucleolar protein homologous to bacterial ribosomal RNA methyltransferase
Genomics
79
2-6
2002
Homo sapiens (Q9UI43), Homo sapiens
brenda
Hager, J.; Staker, B.L.; Jakob, U.
Substrate binding analysis of the 23S rRNA methyltransferase RrmJ
J. Bacteriol.
186
6634-6642
2004
Escherichia coli (A0A140N5X9)
brenda
Caldas, T.; Binet, E.; Bouloc, P.; Costa, A.; Desgres, J.; Tanaka, Y.; Tokuyama, S.; Ochi, K.; Richarme, G.
The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23 S ribosomal RNA methyltransferase
J. Biol. Chem.
275
16414-16419
2000
Escherichia coli (A0A140N5X9), Escherichia coli
brenda
Hager, J.; Staker, B.L.; Bugl, H.; Jakob, U.
Active site in RrmJ, a heat shock-induced methyltransferase
J. Biol. Chem.
277
41978-41986
2002
Escherichia coli (A0A140N5X9)
brenda
Bgl, H.; Fauman, E.B.; Staker, B.L.; Zheng, F.; Kushner, S.R.; Saper, M.A.; Bardwell, J.C.; Jakob, U.
RNA methylation under heat shock control
Mol. Cell
6
349-360
2000
Escherichia coli (A0A140N5X9)
brenda
Hwang, J.; Inouye, M.
Interaction of an essential Escherichia coli GTPase, Der, with the 50S ribosome via the KH-like domain
J. Bacteriol.
192
2277-2283
2010
Escherichia coli
brenda
Arai, T.; Ishiguro, K.; Kimura, S.; Sakaguchi, Y.; Suzuki, T.; Suzuki, T.
Single methylation of 23S rRNA triggers late steps of 50S ribosomal subunit assembly
Proc. Natl. Acad. Sci. USA
112
E4707-E4716
2015
Escherichia coli, Escherichia coli BW25113
brenda
Ishiguro, K.; Arai, T.; Suzuki, T.
Depletion of S-adenosylmethionine impacts on ribosome biogenesis through hypomodification of a single rRNA methylation
Nucleic Acids Res.
47
4226-4239
2019
Escherichia coli, Escherichia coli BW25113
brenda
Koculi, E.; Cho, S.
RNA post-transcriptional modifications in two large subunit intermediates populated in E. coli cells expressing helicase inactive R331A DbpA
Biochemistry
61
833-842
2022
Escherichia coli (P0C0R7), Escherichia coli K12 (P0C0R7)
brenda
Wang, W.; Li, W.; Ge, X.; Yan, K.; Mandava, C.S.; Sanyal, S.; Gao, N.
Loss of a single methylation in 23S rRNA delays 50S assembly at multiple late stages and impairs translation initiation and elongation
Proc. Natl. Acad. Sci. USA
117
15609-15619
2020
Escherichia coli (P0C0R7), Escherichia coli BW25113 (P0C0R7), Escherichia coli K12 (P0C0R7)
brenda
EXTERNAL LINKS (specific for EC-Number 2.1.1.166)
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