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


Autoria(s): MATOS, Juliana L.; FIORI, Celso S.; SILVA-FILHO, Marcio C.; MOURA, Daniel S.
Contribuinte(s)

UNIVERSIDADE DE SÃO PAULO

Data(s)

18/10/2012

18/10/2012

2008

Resumo

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.

Fundacao de Amparo a Pesquisa do Estado de Sao Paulo, FAPESP[02/08661-1]

CNPq

Identificador

FEBS LETTERS, v.582, n.23-24, p.3343-3347, 2008

0014-5793

http://producao.usp.br/handle/BDPI/19402

10.1016/j.febslet.2008.08.025

http://dx.doi.org/10.1016/j.febslet.2008.08.025

Idioma(s)

eng

Publicador

ELSEVIER SCIENCE BV

Relação

Febs Letters

Direitos

restrictedAccess

Copyright ELSEVIER SCIENCE BV

Palavras-Chave #Convertase #Protein processing #Prohormone #MEMBRANE-PROTEINS #ROOT-GROWTH #PLANTS #GENES #POLYPEPTIDE #EXPRESSION #SUBTILASE #PROTEASES #CULTURES #FAMILY #Biochemistry & Molecular Biology #Biophysics #Cell Biology
Tipo

article

original article

publishedVersion