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鉴定核心组蛋白结合所需的不同SET/TAF-Iβ结构域以及相互作用的定量表征。

Identification of distinct SET/TAF-Ibeta domains required for core histone binding and quantitative characterisation of the interaction.

作者信息

Karetsou Zoe, Emmanouilidou Anastasia, Sanidas Ioannis, Liokatis Stamatis, Nikolakaki Eleni, Politou Anastasia S, Papamarcaki Thomais

机构信息

Laboratory of Biological Chemistry, Medical School, University of Ioannina, 451 10 Ioannina, Greece.

出版信息

BMC Biochem. 2009 Apr 9;10:10. doi: 10.1186/1471-2091-10-10.

DOI:10.1186/1471-2091-10-10
PMID:19358706
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2676315/
Abstract

BACKGROUND

The assembly of nucleosomes to higher-order chromatin structures is finely tuned by the relative affinities of histones for chaperones and nucleosomal binding sites. The myeloid leukaemia protein SET/TAF-Ibeta belongs to the NAP1 family of histone chaperones and participates in several chromatin-based mechanisms, such as chromatin assembly, nucleosome reorganisation and transcriptional activation. To better understand the histone chaperone function of SET/TAF-Ibeta, we designed several SET/TAF-Ibeta truncations, examined their structural integrity by circular Dichroism and assessed qualitatively and quantitatively the histone binding properties of wild-type protein and mutant forms using GST-pull down experiments and fluorescence spectroscopy-based binding assays.

RESULTS

Wild type SET/TAF-Ibeta binds to histones H2B and H3 with Kd values of 2.87 and 0.15 microM, respectively. The preferential binding of SET/TAF-Ibeta to histone H3 is mediated by its central region and the globular part of H3. On the contrary, the acidic C-terminal tail and the amino-terminal dimerisation domain of SET/TAF-Ibeta, as well as the H3 amino-terminal tail, are dispensable for this interaction.

CONCLUSION

This type of analysis allowed us to assess the relative affinities of SET/TAF-Ibeta for different histones and identify the domains of the protein required for effective histone recognition. Our findings are consistent with recent structural studies of SET/TAF-Ibeta and can be valuable to understand the role of SET/TAF-Ibeta in chromatin function.

摘要

背景

核小体组装成高阶染色质结构是由组蛋白与伴侣蛋白及核小体结合位点的相对亲和力精细调控的。髓系白血病蛋白SET/TAF-Iβ属于组蛋白伴侣蛋白的NAP1家族，并参与多种基于染色质的机制，如染色质组装、核小体重组和转录激活。为了更好地理解SET/TAF-Iβ的组蛋白伴侣功能，我们设计了几种SET/TAF-Iβ截短体，通过圆二色性检测它们的结构完整性，并使用GST下拉实验和基于荧光光谱的结合测定法对野生型蛋白和突变形式的组蛋白结合特性进行定性和定量评估。

结果

野生型SET/TAF-Iβ与组蛋白H2B和H3结合，解离常数（Kd）值分别为2.87和0.15微摩尔。SET/TAF-Iβ对组蛋白H3的优先结合由其中心区域和H3的球状部分介导。相反，SET/TAF-Iβ的酸性C末端尾巴和氨基末端二聚化结构域以及H3的氨基末端尾巴对于这种相互作用是可有可无的。

结论

这种类型的分析使我们能够评估SET/TAF-Iβ对不同组蛋白的相对亲和力，并确定有效识别组蛋白所需的蛋白质结构域。我们的发现与最近关于SET/TAF-Iβ的结构研究一致，对于理解SET/TAF-Iβ在染色质功能中的作用可能具有重要价值。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5d7c/2676315/6eab7df62367/1471-2091-10-10-4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5d7c/2676315/c61219383fc9/1471-2091-10-10-1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5d7c/2676315/86e48f8b8b5a/1471-2091-10-10-2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5d7c/2676315/dd57717b2b27/1471-2091-10-10-3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5d7c/2676315/6eab7df62367/1471-2091-10-10-4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5d7c/2676315/c61219383fc9/1471-2091-10-10-1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5d7c/2676315/86e48f8b8b5a/1471-2091-10-10-2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5d7c/2676315/dd57717b2b27/1471-2091-10-10-3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5d7c/2676315/6eab7df62367/1471-2091-10-10-4.jpg

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