Journal
FEBS LETTERS
Volume 582, Issue 23-24, Pages 3343-3347Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2008.08.025
Keywords
Convertase; Protein processing; Prohormone
Funding
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo, FAPESP [02/08661-1]
- 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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