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Characterization of elements determining the dimerization properties of RelB and p50.

机译:决定RelB和p50二聚特性的元素的表征。

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Members of the Rel/NF-kappa B family of transcription factors share a region of approximately 300 amino acids which mediates dimerization and sequence-specific binding to DNA. Here we report a detailed characterization of the dimerization domain of RelB. The structural core sufficient to form stable Rel/NF-kappa B dimeric complexes consists of about 110 residues. The dimerization and DNA binding properties of more than 50 RelB mutants were analyzed by using p50 and p52 as partners. We present evidence that amino acids of a conserved element in the dimerization domain play a role in the recognition of a kappa B DNA target sequence. The analysis of hybrid molecules with dimerization domains containing different parts of p50 and RelB allowed us to identify some important structural elements determining homo- and heterodimerization properties. Furthermore, we were able to rescue the dimerization-defective mutant RelB-N287D by the introduction of a counteracting mutation intramolecularly (cis), and also intermolecularly (trans) by a mutation in the NF-kappa B dimerization partner p50. Correspondingly, a dimerization defective p50 mutant was effectively rescued by RelB-N287D.
机译:Rel /NF-κB转录因子家族成员共享大约300个氨基酸的区域,介导二聚化和与DNA的序列特异性结合。在这里,我们报告RelB的二聚化域的详细表征。足以形成稳定的Rel /NF-κB二聚体复合物的结构核心由约110个残基组成。使用p50和p52作为伴侣,分析了50多个RelB突变体的二聚化和DNA结合特性。我们提供的证据表明,二聚化域中一个保守元素的氨基酸在识别kappa B DNA靶序列中起作用。对具有包含p50和RelB不同部分的二聚化结构域的杂合分子的分析,使我们能够确定一些重要的结构要素,这些要素决定了均二聚和异二聚化性质。此外,我们能够通过在分子内(顺式)引入反作用突变来挽救二聚化缺陷型突变体RelB-N287D,并且通过在NF-κB二聚体伴侣p50中引入突变在分子间(反式)突变。相应地,RelB-N287D有效地拯救了二聚化缺陷的p50突变体。

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