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Expression and purification of the full murine NPM2 and study of its interaction with protamines and histones

机译:完整鼠源NPM2的表达和纯化及其与鱼精蛋白和组蛋白相互作用的研究

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摘要

Mouse nucleoplasmin M.NPM2 was recombinantly expressed and the protein consisting of the complete sequence was purified and characterized. Similar to its Xenopus laevis X.NPM2 counterpart, the protein forms stable pentameric complexes and exhibits an almost undistinguishable hydrodynamic ionic strength-dependent unfolding behavior. The interaction of N.PM2 with histones and mouse P1/P2 protamines revealed that these chromosomal proteins bind preferentially to the distal part of the nucleoplasmin pentamer. Moreover, the present work highlights the critical role played by histones H2B and H4 in the association of the histone H2A-H2B dimers and histone octamer with nucleoplasmin.
机译:重组表达小鼠核纤溶酶M.NPM2,并纯化和鉴定由完整序列组成的蛋白质。与其Xenopus laevis X.NPM2对应物相似,该蛋白质形成稳定的五聚体复合物,并表现出几乎不可区分的流体动力学离子强度依赖性展开行为。 N.PM2与组蛋白和小鼠P1 / P2鱼精蛋白的相互作用表明,这些染色体蛋白优先结合至核纤溶酶五聚体的远端。此外,本工作突出了组蛋白H2B和H4在组蛋白H2A-H2B二聚体和组蛋白八聚体与核纤溶酶的结合中所起的关键作用。

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