期刊
FEBS LETTERS
卷 582, 期 23-24, 页码 3343-3347出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2008.08.025
关键词
Convertase; Protein processing; Prohormone
资金
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo, FAPESP [02/08661-1]
- CNPq
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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