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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results (Engineering
Engineering on EC 2.1.1.166 - 23S rRNA (uridine2552-2'-O)-methyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D124A
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
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
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
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
mutant strain shows ribosome profiles that are indistinguishable from wild-type ribosome profile
K164A
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
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
mutant strain shows ribosome profiles that are indistinguishable from wild-type ribosome profile
R32A/R34A
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
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
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
extensive site-directed mutagenesis of the residues conserved in RrmJ and characterization of the mutant proteins both in vivo and in vitro
additional information
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
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
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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
