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Vol. 273, Issue 3, 1316-1323, January 16, 1998
From the The enzymatic activity of yeast gene product Deg1
was identified using both disrupted yeast strain and cloned recombinant protein expressed in yeast and in Escherichia coli. The
results show that the DEG1-disrupted yeast strain lacks
synthase activity for the formation of pseudouridines
Characterization of Yeast Protein Deg1 as Pseudouridine Synthase
(Pus3) Catalyzing the Formation of
38 and
39 in tRNA Anticodon Loop
,, and
Laboratoire d'Enzymologie et Biochimie
Structurales, CNRS, Gif-sur-Yvette, France and the
§ Universität Heidelberg, Institut für Biochemie
I, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany
38
and 39 in tRNA whereas the other activities, specific
for formation at positions 13, 27, 28, 32, 34, 35, 36, and 55 in
tRNA, remain unaffected. Also, the His6-tagged recombinant
yeast Deg1p expressed in E. coli as well as a protein
fusion with protein A in yeast display the enzymatic activity only
toward 38 and 39 formation in different
tRNA substrates. Therefore, Deg1p is the third tRNA:pseudouridine
synthase (Pus3p) characterized so far in yeast. Disruption of the
DEG1 gene is not lethal but reduces considerably the yeast
growth rate, especially at an elevated temperature (37 °C). Deg1p
localizes both in the nucleus and in the cytoplasm, as shown by
immunofluorescence microscopy. Identification of the pseudouridine
residues present (or absent) in selected naturally occurring
cytoplasmic and mitochondrial tRNAs from DEG1-disrupted
strain points out a common origin of 38- and
39-synthesizing activity in both of these two cellular compartments. The sensitivity of Pus3p (Deg1p) activity to overall three-dimensional tRNA architecture and to a few individual mutations in tRNA was also studied. The results indicate the existence of subtle
differences in the tRNA recognition by yeast Pus3p and by its
homologous tRNA:pseudouridine synthase truA from E. coli (initially called hisT or PSU-I gene
product).
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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