Unknown

Dataset Information

0

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


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.

SUBMITTER: Karetsou Z 

PROVIDER: S-EPMC2676315 | biostudies-literature | 2009

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Karetsou Zoe Z   Emmanouilidou Anastasia A   Sanidas Ioannis I   Liokatis Stamatis S   Nikolakaki Eleni E   Politou Anastasia S AS   Papamarcaki Thomais T  

BMC biochemistry 20090409


<h4>Background</h4>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 designe  ...[more]

Similar Datasets

| S-EPMC1810507 | biostudies-literature
| S-EPMC2564889 | biostudies-literature
| S-EPMC5128866 | biostudies-other
| S-EPMC5714232 | biostudies-literature
| S-EPMC4538685 | biostudies-literature
| S-EPMC8443253 | biostudies-literature
| S-EPMC2350211 | biostudies-literature
| S-EPMC10582448 | biostudies-literature
| S-EPMC4052288 | biostudies-literature
| S-EPMC5622319 | biostudies-literature