4.5 Article

A conserved dibasic site is essential for correct processing of the peptide hormone AtRALF1 in Arabidopsis thaliana

Journal

FEBS LETTERS
Volume 582, Issue 23-24, Pages 3343-3347

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2008.08.025

Keywords

Convertase; Protein processing; Prohormone

Funding

  1. Fundacao de Amparo a Pesquisa do Estado de Sao Paulo, FAPESP [02/08661-1]
  2. CNPq

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Prohormone proteins in animals and yeast are typically processed at dibasic sites by convertases. Propeptide hormones are also found in plants but little is known about processing. We show for the first time that a dibasic site upstream of a plant peptide hormone, AtRALF1, is essential for processing. Overexpression of preproAtRALF1 causes semidwarfism whereas overexpression of preproAtRALF1(R69A), the propeptide with a mutation in the dibasic site, shows a normal phenotype. RALF1(R69A) plants accumulate only the mutated proprotein and not the processed peptide. In vitro processing using microsomal fractions suggests that processing is carried out by a kexin-like convertase. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

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