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来自拟南芥的亲免素相互作用蛋白AtFIP37对植物发育至关重要,并参与毛状体核内再复制。

The immunophilin-interacting protein AtFIP37 from Arabidopsis is essential for plant development and is involved in trichome endoreduplication.

作者信息

Vespa Laurent, Vachon Gilles, Berger Frédéric, Perazza Daniel, Faure Jean-Denis, Herzog Michel

机构信息

Laboratoire Plastes et Différenciation Cellulaire, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 5575, Université Joseph Fourier, F-38041 Grenoble cedex 9, France.

出版信息

Plant Physiol. 2004 Apr;134(4):1283-92. doi: 10.1104/pp.103.028050. Epub 2004 Mar 26.

Abstract

The FKBP12 (FK506-binding protein 12 kD) immunophilin interacts with several protein partners in mammals and is a physiological regulator of the cell cycle. In Arabidopsis, only one specific partner of AtFKBP12, namely AtFIP37 (FKBP12 interacting protein 37 kD), has been identified but its function in plant development is not known. We present here the functional analysis of AtFIP37 in Arabidopsis. Knockout mutants of AtFIP37 show an embryo-lethal phenotype that is caused by a strong delay in endosperm development and embryo arrest. AtFIP37 promoter::beta-glucuronidase reporter gene constructs show that the gene is expressed during embryogenesis and throughout plant development, in undifferentiating cells such as meristem or embryonic cells as well as highly differentiating cells such as trichomes. A translational fusion with the enhanced yellow fluorescent protein indicates that AtFIP37 is a nuclear protein localized in multiple subnuclear foci that show a speckled distribution pattern. Overexpression of AtFIP37 in transgenic lines induces the formation of large trichome cells with up to six branches. These large trichomes have a DNA content up to 256C, implying that these cells have undergone extra rounds of endoreduplication. Altogether, these data show that AtFIP37 is critical for life in Arabidopsis and implies a role for AtFIP37 in the regulation of the cell cycle as shown for FKBP12 and TOR (target of rapamycin) in mammals.

摘要

FKBP12(FK506结合蛋白12千道尔顿)免疫亲和素在哺乳动物中与多个蛋白质伴侣相互作用,是细胞周期的生理调节因子。在拟南芥中,仅鉴定出AtFKBP12的一个特定伴侣,即AtFIP37(FKBP12相互作用蛋白37千道尔顿),但其在植物发育中的功能尚不清楚。我们在此展示了拟南芥中AtFIP37的功能分析。AtFIP37的敲除突变体表现出胚胎致死表型,这是由胚乳发育的强烈延迟和胚胎停滞引起的。AtFIP37启动子::β-葡萄糖醛酸酶报告基因构建体表明,该基因在胚胎发生期间以及整个植物发育过程中均有表达,在未分化细胞如分生组织或胚胎细胞以及高度分化细胞如毛状体中均有表达。与增强型黄色荧光蛋白的翻译融合表明,AtFIP37是一种核蛋白,定位于多个显示斑点状分布模式的亚核焦点。转基因系中AtFIP37的过表达诱导形成具有多达六个分支的大型毛状体细胞。这些大型毛状体的DNA含量高达256C,这意味着这些细胞经历了额外的内复制轮次。总之,这些数据表明AtFIP37对拟南芥的生命至关重要,并暗示AtFIP37在细胞周期调节中发挥作用,如同哺乳动物中的FKBP12和雷帕霉素靶蛋白(TOR)一样。

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