一个臂重复蛋白与S位点受体激酶的激酶结构域的结合。
Binding of an arm repeat protein to the kinase domain of the S-locus receptor kinase.
作者信息
Gu T, Mazzurco M, Sulaman W, Matias D D, Goring D R
机构信息
Biology Department, York University, 4700 Keele Street, North York, Ontario M3J 1P3, Canada.
出版信息
Proc Natl Acad Sci U S A. 1998 Jan 6;95(1):382-7. doi: 10.1073/pnas.95.1.382.
Abstract
Screening of a yeast two-hybrid library for proteins that interact with the kinase domain of an S-locus receptor kinase (SRK) resulted in the isolation of a plant protein called ARC1 (Arm Repeat Containing). This interaction was mediated by the C-terminal region of ARC1 in which five arm repeat units were identified. Using the yeast two-hybrid system and in vitro binding assays, ARC1 was found to interact specifically with the kinase domains from SRK-910 and SRK-A14 but failed to interact with kinase domains from two different Arabidopsis receptor-like kinases. In addition, treatment with a protein phosphatase or the use of a kinase-inactive mutant reduced or abolished the binding of ARC1 to the SRK-910 kinase domain, indicating that the interaction was phosphorylation dependent. Lastly, RNA blot analysis revealed that the expression of ARC1 is restricted to the stigma, the site of the self-incompatibility response.
摘要
通过酵母双杂交文库筛选与S-位点受体激酶（SRK）激酶结构域相互作用的蛋白质，得到了一种名为ARC1（含臂重复序列）的植物蛋白。这种相互作用由ARC1的C端区域介导，该区域鉴定出了五个臂重复单元。利用酵母双杂交系统和体外结合试验，发现ARC1与SRK-910和SRK-A14的激酶结构域特异性相互作用，但与两种不同的拟南芥类受体激酶的激酶结构域不相互作用。此外，用蛋白磷酸酶处理或使用激酶失活突变体可减少或消除ARC1与SRK-910激酶结构域的结合，表明这种相互作用依赖于磷酸化。最后，RNA印迹分析显示ARC1的表达仅限于柱头，即自交不亲和反应发生的部位。
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