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首页> 外文期刊>Parasitology >Characterization of monomeric DNA-binding protein Histone H1 in Leishmania braziliensis.
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Characterization of monomeric DNA-binding protein Histone H1 in Leishmania braziliensis.

机译：巴西利什曼原虫的单体DNA结合蛋白组蛋白H1的表征。

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SUMMARYHistone H1 in Leishmania presents relevant differences compared to higher eukaryote counterparts, such as the lack of a DNA-binding central globular domain. Despite that, it is apparently fully functional since its differential expression levels have been related to changes in chromatin condensation and infectivity, among other features. The localization and the aggregation state of L. braziliensis H1 has been determined by immunolocalization, mass spectrometry, cross-linking and electrophoretic mobility shift assays. Analysis of H1 sequences from the Leishmania Genome Database revealed that our protein is included in a very divergent group of histones H1 that is present only in L. braziliensis. An antibody raised against recombinant L. braziliensis H1 recognized specifically that protein by immunoblot in L. braziliensis extracts, but not in other Leishmania species, a consequence of the sequence divergences observed among Leishmania species. Mass spectrometry analysis and in vitro DNA-binding experiments have also proven that L. braziliensis H1 is monomeric in solution, but oligomerizes upon binding to DNA. Finally, despite the lack of a globular domain, L. braziliensis H1 is able to form complexes with DNA in vitro, with higher affinity for supercoiled compared to linear DNA.
机译：总结利什曼原虫中的组蛋白H1与较高等的真核生物相比存在相关差异，例如缺乏DNA结合的中心球状结构域。尽管如此，由于它的差异表达水平与染色质浓缩和感染力的变化有关，因此它显然是功能齐全的。通过免疫定位，质谱，交联和电泳迁移率迁移测定法确定了巴西乳杆菌H1的定位和聚集状态。对利什曼原虫基因组数据库中H1序列的分析表明，我们的蛋白质包含在非常不同的组蛋白H1中，而组蛋白H1仅存在于巴西乳杆菌中。针对重组巴西乳杆菌H1的抗体通过免疫印迹法特异性识别了巴西乳杆菌提取物中的蛋白质，但在其他利什曼原虫物种中却没有，这是由于在利什曼原虫中观察到的序列差异所致。质谱分析和体外DNA结合实验还证明，巴西乳杆菌H1在溶液中为单体，但在与DNA结合后发生寡聚。最后，尽管缺少球形结构域，但巴西乳杆菌H1仍能在体外与DNA形成复合物，与线性DNA相比，其对超螺旋的亲和力更高。

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