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

被引：71

作者：

Matos, Juliana L. ^{[2
]}

Fiori, Celso S. ^{[2
]}

Silva-Filho, Marcio C. ^{[2
]}

Moura, Daniel S. ^{[1
,2
]}

机构：

[1] Univ Fed Sao Paulo, Escola Paulista Ciencias Biol, Dept Ciencias Biol, BR-09972270 Diadema, SP, Brazil

[2] Univ Sao Paulo, Escola Super Agr Luiz de Queiroz, Dept Genet, BR-13400970 Piracicaba, SP, Brazil

来源：

FEBS LETTERS | 2008年 / 582卷 / 23-24期

基金：

巴西圣保罗研究基金会;

关键词：

Convertase; Protein processing; Prohormone;

D O I：

10.1016/j.febslet.2008.08.025

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：3343 / 3347

页数：5

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