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

Abstract : 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.
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Submitted on : Monday, November 7, 2022 - 8:51:39 AM
Last modification on : Thursday, November 17, 2022 - 3:38:36 AM


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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⟩



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