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(Received for publication, May 13, 1997)
From the Department of Clinical Biochemistry, Rigshospitalet,
University of Copenhagen, DK-2100 Copenhagen, Denmark and the
§ Laboratory of Molecular Biology, Statens Seruminstitut,
DK-2300 Copenhagen, Denmark
Tyrosine sulfation is an ubiquitous modification
of proteins synthesized along the secretory pathway. It enhances
protein-protein interactions and may be necessary for the bioactivity
of secreted proteins and peptides. To predict tyrosine sulfation, a
consensus has been proposed based on sequence comparisons of known
substrates and on in vitro studies using synthetic
peptides. This consensus predicts the presence of acidic residues on
the amino-terminal side of the target tyrosine as the key feature.
Using site-directed mutagenesis, we have examined the role of residues
neighboring the sulfation site of an intact protein, human progastrin,
in vivo. The results show that the charge of the residue in
the amino-terminal position (
Volume 272, Number 35,
Issue of August 29, 1997
pp. 21700-21705
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
1) of the tyrosine is critical and can
be neutral or acidic, whereas a basic residue abolishes sulfation. In
addition, the degree of sulfation is influenced by the residues in
positions 2 and 3. Hence, surprisingly a basic residue in position
2 enhances sulfation. Our data suggest a considerably broader range of substrates for the tyrosylprotein sulfotransferase than hitherto assumed and that the tyrosylprotein sulfotransferase is
cell-specifically expressed.
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