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首页> 外文期刊>Protoplasma: An International Journal of Cell Biology >Tandem affinity purification of AtTERT reveals putative interaction partners of plant telomerase in vivo
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Tandem affinity purification of AtTERT reveals putative interaction partners of plant telomerase in vivo

机译：Attert的串联亲和纯化揭示了体内植物端粒酶的推定互动伴侣

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The life cycle of telomerase involves dynamic and complex interactions between proteins within multiple macromolecular networks. Elucidation of these associations is a key to understanding the regulation of telomerase under diverse physiological and pathological conditions from telomerase biogenesis, through telomere recruitment and elongation, to its non-canonical activities outside of telomeres. We used tandem affinity purification coupled to mass spectrometry to build an interactome of the telomerase catalytic subunit AtTERT, using Arabidopsis thaliana suspension cultures. We then examined interactions occurring at the AtTERT N-terminus, which is thought to fold into a discrete domain connected to the rest of the molecule via a flexible linker. Bioinformatic analyses revealed that interaction partners of AtTERT have a range of molecular functions, a subset of which is specific to the network around its N-terminus. A significant number of proteins co-purifying with the N-terminal constructs have been implicated in cell cycle and developmental processes, as would be expected of bona fide regulatory interactions and we have confirmed experimentally the direct nature of selected interactions. To examine AtTERT protein-protein interactions from another perspective, we also analysed AtTERT interdomain contacts to test potential dimerization of AtTERT. In total, our results provide an insight into the composition and architecture of the plant telomerase complex and this will aid in delineating molecular mechanisms of telomerase functions.
机译：端粒酶的生命周期涉及多个大分子网络内蛋白质之间的动态和复杂的相互作用。这些关联的阐明是了解通过端粒酶生物发生的不同生理和病理条件下对端粒酶调节的关键，通过端粒招生和伸长率，在端粒外的非规范活动中。我们使用串联亲和净化偶联至质谱法，以使用拟南芥悬浮培养物构建端粒酶催化亚单位子单元的偶联。然后，我们检查了在attert n-terminus处发生的相互作用，这被认为通过柔性接头折叠成与分子的其余部分连接的离散结构域。生物信息分析显示，Attert的相互作用伴侣具有一定程度的分子函数，其子集是特定于其N-末端的网络。与N-末端构建体共同纯化的大量蛋白质已经涉及细胞周期和发育过程，正如对邦·诉讼调节相互作用的那样，我们已经通过实验证实了所选相互作用的直接性质。为了从另一种观点来检查Attert蛋白质 - 蛋白质 - 蛋白质相互作用，我们还分析了Attert Interdomain的触点，以测试出物电位二聚化。总共，我们的结果介绍了植物端粒酶复合物的组成和结构的洞察力，这将有助于描绘端粒酶功能的分子机制。

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