二元酸
前蛋白转化酶类
蛋白质前体
可欣
前蛋白转化酶
肽
拟南芥
生物化学
毛皮
化学
生物
突变体
基因
酶
脂蛋白
低密度脂蛋白受体
胆固醇
高分子化学
作者
Juliana L. Matos,Celso S. Fiori,Márcio C. Silva-Filho,Daniel S. Moura
出处
期刊:FEBS Letters
[Wiley]
日期:2008-09-05
卷期号:582 (23-24): 3343-3347
被引量:95
标识
DOI:10.1016/j.febslet.2008.08.025
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 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.
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