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New consensus features for tyrosine O-sulfation determined by mutational analysis

J R Bundgaard1, J Vuust, J F Rehfeld

  • 1Department of Clinical Biochemistry, Rigshospitalet, University of Copenhagen, DK-2100 Copenhagen, Denmark. jensbund@rh.dk

The Journal of Biological Chemistry
|August 29, 1997
PubMed
Summary

Tyrosine sulfation, a key protein modification, is influenced by neighboring residues more broadly than previously thought. This finding expands the range of potential substrates for tyrosylprotein sulfotransferase.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Post-translational Modifications

Background:

  • Tyrosine sulfation is a common protein modification in the secretory pathway, crucial for protein interactions and bioactivity.
  • Previous predictions for tyrosine sulfation relied on acidic residues near the target tyrosine, based on sequence analysis and in vitro studies.

Purpose of the Study:

  • To investigate the in vivo role of residues neighboring the sulfation site in human progastrin.
  • To determine the influence of neighboring amino acid charges on tyrosine sulfation within an intact protein.

Main Methods:

  • Site-directed mutagenesis was employed to alter residues surrounding the tyrosine sulfation site in human progastrin.
  • In vivo analysis was conducted to assess the impact of these mutations on protein sulfation.

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Main Results:

  • The charge of the amino-terminal residue (-1 position) is critical; neutral or acidic residues support sulfation, while basic residues abolish it.
  • Residues at positions -2 and -3 significantly influence the degree of sulfation, with a basic residue at -2 surprisingly enhancing the process.
  • These findings indicate a broader substrate specificity for tyrosylprotein sulfotransferase than previously assumed.

Conclusions:

  • The rules governing tyrosine sulfation are more flexible than the established consensus, particularly regarding the amino-terminal positions.
  • Tyrosylprotein sulfotransferase exhibits cell-specific expression, suggesting tissue-specific regulation of protein sulfation.
  • This study broadens the understanding of tyrosine sulfation and its potential substrates, impacting the study of secreted protein function.