Premium
A conserved dibasic site is essential for correct processing of the peptide hormone AtRALF1 in Arabidopsis thaliana
Author(s) -
Matos Juliana L.,
Fiori Celso S.,
Silva-Filho Marcio C.,
Moura Daniel S.
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.08.025
Subject(s) - dibasic acid , proprotein convertases , protein precursor , kexin , proprotein convertase , peptide , arabidopsis thaliana , biochemistry , furin , chemistry , biology , mutant , gene , enzyme , lipoprotein , ldl receptor , cholesterol , polymer chemistry
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.