5YBX

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

Summary for 5YBX

• Entry DOI: 10.2210/pdb5ybx/pdb
• Descriptor: Bouquet formation protein 4 (1 entity in total)
• Functional Keywords: telomere bouquet, nuclear envelope, chromosome organization, dna binding protein
• Biological source: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
• Total number of polymer chains: 1
• Total formula weight: 16192.59

Authors

Hu, C.,Chen, Y. (deposition date: 2017-09-05, release date: 2018-09-19, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.501 Å)