Furuyama T, Dzelzkalns V A
Department of Biology, Case Western Reserve University, Cleveland, OH 44106-7080, USA.
Plant Mol Biol. 1999 Mar;39(4):729-37. doi: 10.1023/a:1006169808171.
We describe the cloning and characterization of PCP, a novel calcium-binding protein that is expressed predominantly in the pistils and anthers of Brassica flowers late in flower development. A PCP cDNA - isolated from a subtracted cDNA library enriched in transcripts present in the pistil late in flower development - potentially encodes a 175 amino acid protein with a calculated molecular weight of 19.1 kDa. Other than limited homology to a repetitive C-terminal polyacidic region of PCP, none of the sequences in the GenBank database shares identity to PCP. This unique protein was purified from an Escherichia coli expression system and shown to bind calcium in a specific manner, both in a protein blot assay and by equilibrium dialysis. PCP binds 29 mol of calcium per mol of PCP protein with an apparent affinity constant of 3.2 x 10(2)/M, values consistent with the presence of a high capacity/low-affinity calcium-binding domain. PCP-specific mRNAs are detected predominantly in the stigma and style of pistils excised from open flowers; much lower levels of expression are seen in anthers of open flowers and in root and leaf tissue. Expression in the pistil steadily increases during flower development and peaks at flower opening. A PCP-specific antibody first detects the protein in pistils at one day prior to flowering, with higher levels of the protein seen in the pistils of open flowers. A low level of the protein is present in anthers of open flowers; however, PCP is not detected in either root or leaf extracts. The pattern of PCP expression is consistent with a possible role for PCP in pollen-pistil interactions or in pistil development. The results are also discussed in light of the central role calcium maintains in pollen tube growth and fertilization.
我们描述了PCP的克隆和特性,PCP是一种新型钙结合蛋白,在油菜花发育后期主要在雌蕊和花药中表达。从一个在花发育后期雌蕊中富集转录本的消减cDNA文库中分离出的PCP cDNA,可能编码一种175个氨基酸的蛋白质,计算分子量为19.1 kDa。除了与PCP的重复C末端多酸性区域有有限的同源性外,GenBank数据库中的序列均与PCP无同一性。这种独特的蛋白质从大肠杆菌表达系统中纯化出来,并在蛋白质印迹分析和平衡透析中显示以特定方式结合钙。PCP每摩尔PCP蛋白结合29摩尔钙,表观亲和常数为3.2×10²/M,这些值与存在高容量/低亲和力钙结合结构域一致。PCP特异性mRNA主要在从开放花中切除的雌蕊的柱头和花柱中检测到;在开放花的花药以及根和叶组织中表达水平要低得多。在花发育过程中,雌蕊中的表达稳步增加,并在开花时达到峰值。一种PCP特异性抗体在开花前一天首次在雌蕊中检测到该蛋白,在开放花的雌蕊中可见较高水平的该蛋白。开放花的花药中存在低水平的该蛋白;然而,在根或叶提取物中未检测到PCP。PCP的表达模式与PCP在花粉 - 雌蕊相互作用或雌蕊发育中可能发挥的作用一致。还根据钙在花粉管生长和受精中所起的核心作用对结果进行了讨论。