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首页> 外文期刊>Molecular and Cellular Biology >The Balance of Nuclear Import and Export Determines the Intracellular Distribution and Function of Tomato Heat Stress Transcription Factor HsfA2
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The Balance of Nuclear Import and Export Determines the Intracellular Distribution and Function of Tomato Heat Stress Transcription Factor HsfA2

机译：核进出口的平衡决定了番茄热应激转录因子HsfA2的细胞内分布和功能。

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Tomato heat stress transcription factor HsfA2 is a shuttling protein with dominant cytoplasmic localization as a result of a nuclear import combined with an efficient export. Besides the nuclear localization signal (NLS) adjacent to the oligomerization domain, a C-terminal leucine-rich motif functions as a nuclear export signal (NES). Mutant forms of HsfA2 with a defective or an absent NES are nuclear proteins. The same is true for the wild-type HsfA2 if coexpressed with HsfA1 or in the presence of export inhibitor leptomycin B (LMB). Fusion of the NES domain of HsfA2 to HsfB1, which is a nuclear protein, caused export of the HsfB1-A2NES hybrid protein, and this effect was reversed by the addition of LMB. Due to the lack of background problems, Chinese hamster ovary (CHO) cells represent an excellent system for expression and functional analysis of tomato Hsfs. The results faithfully reflect the situation found in plant cells (tobacco protoplasts). The intriguing role of NLS and NES accessibility for the intracellular distribution of HsfA2 is underlined by the results of heat stress treatments of CHO cells (41°C). Despite the fact that nuclear import and export are not markedly affected, HsfA2 remains completely cytoplasmic at 41°C even in the presence of LMB. The temperature-dependent conformational transition of HsfA2 with shielding of the NLS evidently needs intramolecular interaction between the internal HR-A/B and the C-terminal HR-C regions. It is not observed with the HR oligomerization domain (HR-A/B region) deletion form of HsfA2 or in HsfA2-HsfA1 hetero-oligomers.
机译：番茄热胁迫转录因子HsfA2是一种穿梭蛋白，由于核输入与有效输出的结合，具有占主导地位的胞质定位。除了与寡聚化结构域相邻的核定位信号（NLS）外，富含C末端亮氨酸的基序还用作核输出信号（NES）。 NES缺陷或缺失的HsfA2突变形式是核蛋白。如果与HsfA1共表达或存在出口抑制剂瘦霉素B（LMB），则野生型HsfA2也是一样。 HsfA2的NES结构域与HsfB1（一种核蛋白）的融合导致HsfB1-A2NES杂合蛋白的输出，并且通过添加LMB可以逆转这种作用。由于缺乏背景问题，中国仓鼠卵巢（CHO）细胞代表了番茄Hsfs表达和功能分析的出色系统。结果忠实地反映了植物细胞（烟草原生质体）中发现的情况。 CHO细胞的热应激处理结果（41°C）突显了NLS和NES可及性对HsfA2的细胞内分布的有趣作用。尽管没有明显影响核进出口的事实，但即使在存在LMB的情况下，HsfA2在41°C仍保持完全的细胞质。 HsfA2的温度依赖性构象转变与NLS的屏蔽显然需要内部HR-A / B和C端HR-C区之间的分子内相互作用。没有观察到HsfA2的HR寡聚域（HR-A / B区）缺失形式或在HsfA2-HsfA1杂合寡聚体中观察到。

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