Plant Molecular Biology Center and Department of Biological Sciences, Northern Illinois University, DeKalb, IL 60115, USA.
Biochem Soc Trans. 2010 Apr;38(2):622-6. doi: 10.1042/BST0380622.
The recent identification of several proteins playing key roles in S-RNase-based gametophytic self-incompatibility has led both to a greater understanding of the molecular biology of this response, as well as to questions regarding the precise mechanism by which compatible pollen tubes are recognized and accepted. A proposed variant SCF(SLF) (where SCF is SSK1/cullin/F-box and SLF is S-locus F-box) ubiquitin ligase complex is thought to play a central role in recognizing and inhibiting non-self S-RNases, but the exact role of ubiquitination remains unclear. How the possible sequestration of non-self S-RNases in a pollen vacuolar compartment can be reconciled with the need for protein interaction between S-RNase and the SCF(SLF) complex needs to be determined. Current work to answer these questions focuses on more precisely defining quantitative protein interactions and subcellular localization of proteins involved in S-RNase-based gametophytic self-incompatibility.
最近鉴定出几种在 S-RNase 基础的配子体自交不亲和中起关键作用的蛋白质，这不仅使我们对这种反应的分子生物学有了更深入的了解，也提出了关于识别和接受亲和花粉管的确切机制的问题。一个提出的变体 SCF(SLF)（其中 SCF 是 SSK1/cullin/F-box，SLF 是 S 座位 F-box）泛素连接酶复合物被认为在识别和抑制非自身 S-RNases 中起核心作用，但泛素化的确切作用仍不清楚。如何将非自身 S-RNases 隔离在花粉液泡隔室中，同时又需要 S-RNase 与 SCF(SLF) 复合物之间的蛋白相互作用，这需要确定。目前为回答这些问题所做的工作侧重于更精确地定义参与 S-RNase 基础的配子体自交不亲和的蛋白质的定量蛋白相互作用和亚细胞定位。
