Compatible and self-incompatible pollination in Pyrus communis displays different polyamine levels and transglutaminase activity

Compatible and self-incompatible pollination in Pyrus communis displays different polyamine levels and transglutaminase activity
复制标题

DOI:
10.1007/s00726-009-0426-5
复制
发表时间:
2010-02-01
期刊:
影响因子:
3.5
通讯作者:
Serafini-Fracassini, D.
Serafini-Fracassini, D.
中科院分区:
生物学3区
文献类型:
--
作者:
Del Duca, S.;Cai, G.;Serafini-Fracassini, D.

文献摘要

被引文献

相似文献

研究了梨与亲和和自交不亲和(SI)花粉授粉中的多胺(PA)含量和转谷氨酰胺酶(TGase)活性,以加深它们在植物繁殖的繁殖阶段的可能参与。根据授粉过程中可能的作用,讨论了 PA 在未发芽 (UGP)、发芽花粉 (GP)、花柱和具有亲和花粉和 SI 花粉的授粉花柱中作为游离、高氯酸 (PCA) 可溶和 PCA 不溶部分的分布。一般来说,PCA 可溶性和 PCA 不溶性部分中的缀合 PA 均高于游离形式。在共轭 PA 中,除未授粉花柱外,PCA 不溶性最高。由于 TGase 通过将 PA 与蛋白质共价结合来介导 PA 的一些作用,因此检查了这种酶的活性,以前从未在花柱和授粉花柱中检查过。在 SI 花柱中,与亲和花粉授粉的花柱相比,TGase 活性更高,并且形成了高分子量交联产物,表明 TGase 参与了 SI 反应。这是证明这种酶活性在未授粉和授粉风格中存在的第一个证据。
The polyamine (PA) content and the transglutaminase (TGase) activity have been investigated in Pyrus communis pollination with compatible and self-incompatible (SI) pollen in order to deepen their possible involvement in the progamic phase of plant reproduction. The PA distribution as free, perchloric acid (PCA)-soluble and PCA-insoluble fractions in ungerminated (UGP), germinating pollen (GP), styles and pollinated styles with compatible and SI pollens is discussed in the light of a possible role during pollination. Generally, the conjugated PAs both in PCA-soluble and PCA-insoluble fractions were higher than the free form. Within the conjugated PAs, the PCA-insoluble ones were the highest with the exception of the not pollinated styles. As TGase mediates some of the effects of PAs by covalently binding them to proteins, the activity of this enzyme, never checked before in styles and pollinated styles, was examined. In the SI styles, the TGase activity is higher in comparison to style-pollinated with compatible pollen, and high molecular mass cross-linked products were formed, suggesting an involvement of TGase in SI response. This is the first evidence on the presence of this enzyme activity in not pollinated and pollinated styles.