1: Nucleic Acids Res. 1996 Jun 15;24(12):2411-5.

Pseudouridine synthases: four families of enzymes containing a putative
uridine-binding motif also conserved in dUTPases and dCTP deaminases.

Koonin EV.

National Center for Biotechnology Information, National Library of Medicine,
National Institutes of Health, Bethesda, MD 20894, USA.

Using a combination of several methods for protein sequence comparison and motif 
analysis, it is shown that the four recently described pseudouridine syntheses
with different specificities belong to four distinct families. Three of these
families share two conserved motifs that are likely to be directly involved in
catalysis. One of these motifs is detected also in two other families of enzymes 
that specifically bind uridine, namely deoxycitidine triphosphate deaminases and 
deoxyuridine triphosphatases. It is proposed that this motif is an essential part
of the uridine-binding site. Two of the pseudouridine syntheses, one of which
modifies the anticodon arm of tRNAs and the other is predicted to modify a
portion of the large ribosomal subunit RNA belonging to the peptidyltransferase
center, are encoded in all extensively sequenced genomes, including the 'minimal'
genome of Mycoplasma genitalium. These particular RNA modifications and the
respective enzymes are likely to be essential for the functioning of any cell.

PMCID: PMC145960
PMID: 8710514 [PubMed - indexed for MEDLINE]

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