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J Biol Chem, Vol. 274, Issue 30, 21450-21456, July 23, 1999
From the Molecular Biology Department, National Institute of
Bioscience and Human Technology, 1-1 Higashi, Tsukuba,
Ibaraki 305-8566, Japan
The gene for the open reading frame YER005w that
is homologous to yeast Golgi GDPase encoded by the GDA1
gene was cloned and named YND1. It encodes a 630-amino acid
protein that contains a single transmembrane region near the carboxyl
terminus. The overexpression of the YND1 gene in the
gda1 null mutant caused a significant increase in
microsomal membrane-bound nucleoside phosphatase activity with a
luminal orientation. The activity was equally high toward ADP/ATP,
GDP/GTP, and UDP/UTP and ~50% less toward CDP/CTP and thiamine
pyrophosphate, but there was no activity toward GMP, indicating that
the Ynd1 protein belongs to the apyrase family. This substrate
specificity is different from that of yeast GDPase, but similar to that
of human Golgi UDPase. The 
ynd1 mutant cells were
defective in O- and N-linked glycosylation in
the Golgi compartments. The overexpression of the YND1 gene
complemented some glycosylation defects in gda1 disruptants, suggesting a partially redundant function of yeast apyrase
and GDPase. From these results and the phenotype of the ynd1gda1 double deletion showing a
synthetic effect, we conclude that yeast apyrase is required for Golgi
glycosylation and cell wall integrity, providing the first direct
evidence for the in vivo function of intracellular apyrase
in eukaryotic cells.
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