Disruption of the novel plant protein NEF1 affects lipid accumulation in the plastids of the tapetum and exine formation of pollen, resulting in male sterility in Arabidopsis thaliana
Disruption of the novel plant protein NEF1 affects lipid accumulation in the plastids of the tapetum and exine formation of pollen, resulting in male sterility in Arabidopsis thaliana
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DOI：
10.1111/j.1365-313x.2004.02118.x
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发表时间：
2004-07-01
期刊：
影响因子：
7.2
通讯作者：
Toriyama, K
中科院分区：
文献类型：
--
作者：
Ariizumi, T;Hatakeyama, K;Toriyama, K
利用T-DNA标签技术分离到一个新的拟南芥雄性不育突变体。小孢子释放后，突变体花粉败育明显，开花期花粉粒完全缺失。透射电子显微镜分析表明，primexine是粗糙的发展，虽然产生孢粉素，它不是沉积在小孢子质膜上。未能沉积的孢粉素在室内和室壁上聚集积累。最后观察到as（n）在baro下（e）在bar xine下（f）在bar xine下，将该突变体命名为nef 1。绒毡层质体内的质体细胞减少，脂质积累明显减少。该突变体叶片叶绿体超微结构发生明显改变，表现出多种生长缺陷。脂质分析显示，Nef 1的总脂质含量低于野生型，表明Nef 1参与了脂质代谢。克隆的全长Nef 1基因编码一个新的植物蛋白的1123个氨基酸的有限的序列相似性的膜蛋白或转运蛋白样蛋白，和NEF 1被预测为质体整合膜蛋白。基序分析表明，NEF 1含有原核细胞膜脂蛋白脂质附着位点，参与维持细胞包膜的完整性。据预测，Nef 1编码的膜蛋白，保持在质体的包膜完整性。
A novel male-sterile mutant of Arabidopsis thaliana was isolated by means of T-DNA tagging. Pollen abortion of the mutant was evident after microspore release, and pollen grains were completely absent at anthesis. Transmission electron microscope analysis revealed that primexine was coarsely developed, and that although sporopollenin was produced, it was not deposited onto the microspore plasma membrane. The sporopollenin that failed to be deposited aggregated and accumulated within the locule and on the locule wall. Finally, as (n) under baro (e) under bar xine (f) under bar ormation was observed, the mutant was named nef1. The plastoglobuli within the plastids of the tapetum were reduced, and lipid accumulation was considerably decreased. The mutant had a significantly altered leaf chloroplast ultrastructure and showed various growth defects. Lipid analysis revealed that the total lipid content in nef1 was lower than that in the wild type, which indicated that Nef1 was involved in lipid metabolism. Cloning of the full-length Nef1 indicated that the gene encodes a novel plant protein of 1123 amino acids with limited sequence similarities to membrane proteins or transporter-like proteins, and the NEF1 is predicted to be a plastid integral membrane protein. Motif analysis revealed that NEF1 contains prokaryotic membrane lipoprotein lipid attachment sites that are involved in maintaining cell envelope integrity. It is predicted that the Nef1 encodes a membrane protein that maintains the envelope integrity in the plastids.