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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
Matos, Juliana L. [1] ; Fiori, Celso S. [1] ; Silva-Filho, Marcio C. [1] ; Moura, Daniel S. [1, 2]
Total Authors: 4
Affiliation:
[1] Univ Sao Paulo, Escola Super Agr Luiz de Queiroz, Dept Genet, BR-13400970 Piracicaba, SP - Brazil
[2] Univ Fed Sao Paulo, Escola Paulista Ciencias Biol, Dept Ciencias Biol, BR-09972270 Diadema, SP - Brazil
Total Affiliations: 2
Document type: Journal article
Source: FEBS Letters; v. 582, n. 23-24, p. 3343-3347, OCT 15 2008.
Web of Science Citations: 41
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 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. (AU)