| Literature DB >> 18775699 |
Juliana L Matos1, Celso S Fiori, Marcio C Silva-Filho, Daniel S Moura.
Abstract
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 semi-dwarfism 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.Entities:
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Year: 2008 PMID： 18775699 DOI： 10.1016/j.febslet.2008.08.025
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124