RluA is the sole protein responsible for the in vivo formation of 23S RNA pseudouridine746 . The dual-specificity enzyme also catalyses the formation of uridine32 in tRNA . cf. EC 5.4.99.28 (tRNA pseudouridine32 synthase).
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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SYSTEMATIC NAME
IUBMB Comments
23S rRNA-uridine746 uracil mutase
RluA is the sole protein responsible for the in vivo formation of 23S RNA pseudouridine746 [2]. The dual-specificity enzyme also catalyses the formation of uridine32 in tRNA [3]. cf. EC 5.4.99.28 (tRNA pseudouridine32 synthase).
Substrates: the enzyme reacts specifically with uridine746 in 23S rRNA. The enzyme is also responsible for the formation of pseudouridine32 in tRNA Products: -
the rluA deletion mutant fails to form either 23S RNA pseudouridine746 or tRNA pseudouridine32. Replacement of rluA in trans on a rescue plasmid restores both pseudouridines. There is no difference in exponential growth rate between wild-type and MG1655(rluA-) either in rich or minimal medium at 24, 37, or 42°C, but when both strains are grown together, a strong selection against the deletion strain is observed
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method. 2.05 A resolution structure of RluA bound to a substrate RNA comprising the anticodon stem loop of tRNAPhe reveals that enzyme binding induces a dramatic reorganization of the RNA
Wrzesinski, J.; Nurse, K.; Bakin, A.; Lane, B.G.; Ofengand, J.
A dual-specificity pseudouridine synthase: an Escherichia coli synthase purified and cloned on the basis of its specificity for psi 746 in 23S RNA is also specific for psi 32 in tRNA(phe)