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J. Biol. Chem., Vol. 265, Issue 15, 8525-8532, May, 1990
C Niehrs, M Kraft, RW Lee and WB Huttner
Tyrosylprotein sulfotransferase (TPST) catalyzes the sulfation of proteins
at tyrosine residues. We have analyzed the substrate specificity of TPST
from bovine adrenal medulla with a novel assay, using synthetic peptides as
substrates. The peptides were modeled after the known, or putative,
tyrosine sulfation sites of the cholecystokinin precursor, chromogranin B
(secretogranin I) and vitronectin, as well as the tyrosine phosphorylation
sites of alpha-tubulin and pp60src. Varying the sequence of these peptides,
we found that (i) the apparent Km of peptides with multiple tyrosine
sulfation sites decreased exponentially with the number of sites; (ii)
acidic amino acids were the major determinant for tyrosine sulfation,
acidic amino acids adjacent to the tyrosine being more important than
distant ones; (iii) a carboxyl terminally located tyrosine residue may be
sulfated. Moreover, TPST catalyzed the sulfation of a peptide corresponding
to the tyrosine autophosphorylation site of pp60v-src (Tyr-416) but not of
a peptide corresponding to the non-autophosphorylation site of pp60c- src
(Tyr-527). These results experimentally define structural determinants for
the substrate specificity of TPST and show that this enzyme and certain
autophosphorylating tyrosine kinases have overlapping substrate
specificities in vitro.
Analysis of the substrate specificity of tyrosylprotein sulfotransferase using synthetic peptides
Cell Biology Programme, European Molecular Biology Laboratory, Heidelberg, Federal Republic of Germany.
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