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(Received for publication, June 5, 1997, and in revised form, July 9, 1997)
From the We previously isolated a mutant cell that is the
only mammalian cell reported to have a persistently low level of
UDP-glucose. In this work we obtained a spontaneous revertant whose
UDP-glucose level lies between those found in the wild type and the
mutant cell. The activity of UDP-glucose pyrophosphorylase (UDPG:PP), the enzyme that catalyzes the formation of UDP-glucose, was in the
mutant 4% and in the revertant 56% of the activity found in the wild
type cell. Sequence analysis of UDPG: PP cDNAs from the mutant
cell showed one missense mutation, which changes amino acid residue 115 from glycine to aspartic acid. The substituted glycine is located
within the largest stretch of strictly conserved residues among
eukaryotic UDPG:PPs. The analysis of the cDNAs from the revertant
cell indicated the presence of an equimolar mixture of the wild
type and the mutated mRNAs, suggesting that the mutation has
reverted in only one of the alleles. In summary, we demonstrate that
the G115D substitution in the Chinese hamster UDPG:PP
dramatically impairs its enzymatic activity, thereby causing cellular
UDP-glucose deficiency.
Volume 272, Number 38,
Issue of September 19, 1997
pp. 23784-23791
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,§¶
,
,
and
Microbiology and Tumorbiology Center and the
** Department of Medical Biochemistry and Biophysics, Karolinska
Institutet, S-171 77 Stockholm, Sweden, the § Instituto
Clodomiro Picado, Orion-Pharma, R & D, Drug Design Unit,
NMR Laboratory, P.O. Box 65, FIN-02101, Espoo, Finland, and the
§§ Institut für Medizinische Mikrobiologie
und Hygiene, Verfügungsgebaude für Forschung und
Entwicklung, Johannes Gutenberg-Universität Mainz,
55101 Mainz, Germany
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