5.4.99.23: 23S rRNA pseudouridine1911/1915/1917 synthase
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For detailed information about 23S rRNA pseudouridine1911/1915/1917 synthase, go to the full flat file.
Reaction
Synonyms
pseudouridine synthase RluD, pseudouridine synthases RluD, ribosomal large subunit pseudouridine synthase D, RluD, RluD pseudouridine synthase, sfhB, YfiI, YfiL
ECTree
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Engineering
Engineering on EC 5.4.99.23 - 23S rRNA pseudouridine1911/1915/1917 synthase
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D139N
D139T
mutation completely blocks pseudouridine formation in vivo and in vitro. The mutant rluD gene produces a protein capable of complete reversal of the growth defect (of Escherichia coli mutant with a truncation in the rluD gene) without concomitant pseudouridine formation
additional information
construction of a chimeric pseudouridine synthase (RluCD) containing the N-terminal S4 domain of enzyme RluC (EC 5.4.99.24) and the C-terminal catalytic domain of enzyme RluD (EC 5.4.99.23). The chimeric mutant is able to introduce excessive pseudouridines into rRNA at non-native positions. The chimeric enzyme RluCD is used as a tool to study an effect of over-modification of rRNA on the ribosome biogenesis. Excessive pseudouridylation of 23S rRNA reduces progression of ribosome assembly during early or middle stages. A modification interference approach identifies the sites in 23S rRNA whose modification prevents ribosome assembly. It is plausible that pseudouridines can cause RNA misfolding when present at non-native positions. RluCD isomerizes many uridines of rRNA in a non-specific manner. Induction of the RluCD at the exponential growth phase leads to severe inhibition of translation while transcription is only slightly affected
mutation completely blocks pseudouridine formation in vivo and in vitro. The mutant rluD gene produces a protein capable of complete reversal of the growth defect (of Escherichia coli mutant with a truncation in the rluD gene) without concomitant pseudouridine formation
D139N
site-directed mutagenesis of the chimeric enzyme mutant RluCD, the mutant is catalytically inactive