5YBX

Crystal structure of the N-terminal domain of Bqt4 in S.pombe

5YBX の概要

• エントリーDOI: 10.2210/pdb5ybx/pdb
• 分子名称: Bouquet formation protein 4 (1 entity in total)
• 機能のキーワード: telomere bouquet, nuclear envelope, chromosome organization, dna binding protein
• 由来する生物種: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16192.59

構造登録者

Hu, C.,Chen, Y. (登録日: 2017-09-05, 公開日: 2018-09-19, 最終更新日: 2024-11-13)

主引用文献

Hu, C.,Inoue, H.,Sun, W.,Takeshita, Y.,Huang, Y.,Xu, Y.,Kanoh, J.,Chen, Y.
The Inner Nuclear Membrane Protein Bqt4 in Fission Yeast Contains a DNA-Binding Domain Essential for Telomere Association with the Nuclear Envelope.
Structure, 27:335-, 2019

PubMed Abstract: Telomeres, the protective caps at the end of the chromosomes, are often associated with the nuclear envelope (NE). Telomere positioning to the NE is dynamically regulated during mitosis and meiosis. One inner nuclear membrane protein, Bqt4, in Schizosaccharomyces pombe plays essential roles in connecting telomeres to the NE. However, the structural basis of Bqt4 in mediating telomere-NE association is not clear. Here, we report the crystal structure of the N-terminal domain of Bqt4. The N-terminal domain of Bqt4 structurally resembles the APSES-family DNA-binding domain and has a moderate double-stranded DNA-binding activity. Disruption of Bqt4-DNA interaction results in telomere detachment from the NE. These data suggest that the DNA-binding activity of Bqt4 may function to prime the chromosome onto the NE and promote telomere-NE association.

PubMed: 30503780
DOI: 10.1016/j.str.2018.10.010

実験手法

X-RAY DIFFRACTION (2.501 Å)