Processing of a plant peptide hormone precursor facilitated by posttranslational tyrosine sulfation

Stefanie Royek (1) , Martin Bayer (2) , Jens Pfannstiel (3) , Jürgen Pleiss (4) , Gwyneth Ingram (5) , Annick Stintzi (4) , Andreas Schaller (4)

1 University of Hohenheim
2 Max-Planck-Institut fur Biologie = Max Planck Institute for Biology [Tübingen]
3 University of Tübingen
4 Universität Hohenheim
5 RDP - Reproduction et développement des plantes

Most peptide hormones and growth factors are matured from larger inactive precursor proteins by proteolytic processing and further post-translational modification. Whether or how posttranslational modifications contribute to peptide bioactivity is still largely unknown. We address this question here for TWS1 (Twisted Seed 1), a peptide regulator of embryonic cuticle formation in Arabidopsis thaliana. Using synthetic peptides encompassing the N-and C-terminal processing sites and the recombinant TWS1 precursor as substrates, we show that the precursor is cleaved by the subtilase SBT1.8 at both the N-and the C-terminus of TWS1. Recognition and correct processing at the N-terminal site depended on sulfation of an adjacent tyrosine residue. Arginine 302 of SBT1.8 was found to be required for sulfo-tyrosine binding and for accurate processing of the TWS1 precursor. The data reveal a critical role for post-translational modification, here tyrosine sulfation of a plant peptide hormone precursor, in mediating processing specificity and peptide maturation.

Mots clés: Biological Sciences; Plant Biology peptide hormone; post-translational modification; proteolytic processing; tyrosine sulfation

Domaines: Biologie végétale

Stefanie Royek, Martin Bayer, Jens Pfannstiel, Jürgen Pleiss, Gwyneth Ingram, et al.. Processing of a plant peptide hormone precursor facilitated by posttranslational tyrosine sulfation. Proceedings of the National Academy of Sciences of the United States of America, 2022, 119 (16), pp.e2201195119. ⟨10.1073/pnas.2201195119⟩. ⟨hal-03841269⟩