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TPR-Mediated self-association of plant SGT1

机译：TPR介导的植物SGT1的自缔合

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The tetratricopeptide repeat (TPR) domain mediates inter-protein associations in a number of systems. The domain is also thought to mediate oligomerization of some proteins, but this has remained controversial, with conflicting data appearing in the literature. By way of investigating such TPR-mediated self-associations we used a variety of biophysical techniques to characterize purified recombinant Sgtl, a TPR-containing protein found in all eukaryotes that is involved in a broad range of biological processes, including kinetochore assembly in humans and yeast and disease resistance in plants. We show that recombinant Sgtl from Arabidopsis, barley, and yeast self-associates in vitro while recombinant human Sgtl does not. Further experiments on barley Sgtl demonstrate unambiguously a TPR-mediated dimerization, which is concentration- and ionic-strength-dependent and results in a global increase in helical structure and stability of the protein. Dimerization is also redox sensitive, being completely abolished by the formation of an intramolecular disulfide bond where the contributing cysteines are conserved in plant Sgtls. The dimer interface was mapped through cross-linking and mass spectrometry to the C-terminal region of the TPR domain. Our study, which provides the first biophysical characterization of plant Sgtl, highlights how TPR domains can mediate self-association in solution and that sequence variation in the regions involved in oligomerization affects the propensity of TPR-containing proteins to dimerize.
机译：四肽重复（TPR）域在许多系统中介导蛋白质间的缔合。该结构域也被认为可以介导某些蛋白质的寡聚化，但这仍然存在争议，文献中出现了相互矛盾的数据。通过研究这种TPR介导的自我缔合，我们使用了多种生物物理技术来表征纯化的重组Sgtl，这是在所有真核生物中发现的，含有TPR的蛋白质，其参与广泛的生物学过程，包括人体内的线粒体组装和植物中的酵母和抗病性。我们显示，从拟南芥，大麦和酵母的重组Sgtl在体外自我关联，而重组人Sgtl没有。在大麦Sgtl上的进一步实验清楚地证明了TPR介导的二聚作用，它是浓度和离子强度依赖性的，并导致蛋白质螺旋结构和稳定性的整体增加。二聚化也对氧化还原敏感，通过形成分子内二硫键而完全消除，其中贡献的半胱氨酸在植物Sgt1中是保守的。通过交联和质谱将二聚体界面映射到TPR结构域的C末端区域。我们的研究提供了植物Sgtl的第一个生物物理特征，强调了TPR域如何介导溶液中的自缔合，并且寡聚化区域中的序列变异会影响含TPR的蛋白质二聚化的倾向。

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