2.1.1.166: 23S rRNA (uridine2552-2'-O)-methyltransferase
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For detailed information about 23S rRNA (uridine2552-2'-O)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.166
Reaction
Synonyms
23 S ribosomal RNA methyltransferase, 23S rRNA methyltransferase, FTSJ, FtsJ/RrmJ heat shock protein, FtsJ2, heat shock protein RrmJ, Mj0697, RlmE, RrmJ, Um(2552) 23S ribosomal RNA methyltransferase, Um2552 methyltransferase
ECTree
2.1.1.166 23S rRNA (uridine2552-2'-O)-methyltransferaseAdvanced search results
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General Information on EC 2.1.1.166 - 23S rRNA (uridine2552-2'-O)-methyltransferase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
metabolism
absence of functional RrmJ causes the cellular accumulation of the individual ribosomal subunits at the expense of the functional 70S ribosomes
physiological function
malfunction
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
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
null mutations in ftsJ show a dramatically altered ribosome profile, a severe growth disadvantage, and a temperature-sensitive phenotype
malfunction
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
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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
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enzyme deletion results in slow growth and accumulation of the 45S particle
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physiological function
the 23S rRNA modification is critical for ribosome stability
physiological function
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
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the enzyme is an assembly factor that acts at a late step of 50S formation
physiological function
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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
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the enzyme is an assembly factor that acts at a late step of 50S formation
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physiological function
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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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