A cathepsin F-like peptidase involved in barley grain protein mobilization, HvPap-1, is modulated by its own propeptide and by cystatins.

A cathepsin F-like peptidase involved in barley grain protein mobilization, HvPap-1, is modulated by its own propeptide and by cystatins.
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DOI:
10.1093/jxb/ers137
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发表时间:
2012-07
影响因子:
6.9
通讯作者:
Diaz I
Diaz I
中科院分区:
生物学1区
文献类型:
--
作者:
Cambra I;Martinez M;Dáder B;González-Melendi P;Gandullo J;Santamaría ME;Diaz I

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在C1 A半胱氨酸蛋白酶中,植物组织蛋白酶F样组的研究很少。本文描述了大麦HvPap-1组织蛋白酶F样蛋白的分子和功能特性。该肽酶是N-糖基化的,并且必须通过其自身的前肽(作为肽酶活性的重要调节剂)进行加工以变得有活性。其mRNA和蛋白质的表达模式表明,它在大麦植物中参与不同的蛋白水解过程。HvPap-1肽酶已在大肠杆菌中纯化,并且重组蛋白能够降解不同的底物,包括储存在大麦胚乳中的大麦籽粒蛋白(大麦醇溶蛋白、白蛋白和球蛋白)。它定位于胚的蛋白体和小泡中,并通过赤霉素处理在糊粉层中诱导。这三个特征支持了HvPap-1在谷物萌发过程中的贮藏蛋白动员中的作用。此外,还描述了大麦半胱氨酸蛋白酶抑制剂及其自身前肽的复杂调节作用
Among the C1A cysteine proteases, the plant cathepsin F-like group has been poorly studied. This paper describes the molecular and functional characterization of the HvPap-1 cathepsin F-like protein from barley. This peptidase is N-glycosylated and has to be processed to become active by its own propeptide being an important modulator of the peptidase activity. The expression pattern of its mRNA and protein suggest that it is involved in different proteolytic processes in the barley plant. HvPap-1 peptidase has been purified in Escherichia coli and the recombinant protein is able to degrade different substrates, including barley grain proteins (hordeins, albumins, and globulins) stored in the barley endosperm. It has been localized in protein bodies and vesicles of the embryo and it is induced in aleurones by gibberellin treatment. These three features support the implication of HvPap-1 in storage protein mobilization during grain germination. In addition, a complex regulation exerted by the barley cystatins, which are cysteine protease inhibitors, and by its own propeptide, is also described
DOI: 10.1186/1471-2148-8-198
发表时间: 2008-07-10
影响因子: 3.4
作者:
Martinez M;Diaz I
通讯作者: Diaz I
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影响因子: 11.1
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发表时间: 1987-11-01
影响因子: 11.1
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