5YC2

Crystal structure of inner membrane protein Bqt4 in complex with telomeric protein Rap1

Summary for 5YC2

• Entry DOI: 10.2210/pdb5yc2/pdb
• Descriptor: Ubiquitin-like protein SMT3,Bouquet formation protein 4, DNA-binding protein rap1 (3 entities in total)
• Functional Keywords: choromosome organization, teleomere bouquet, nuclear envelope, spore formation, membrane protein
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 4
• Total formula weight: 51147.84

Authors

Chen, Y.,Hu, C. (deposition date: 2017-09-06, release date: 2018-11-14, Last modification date: 2023-11-22)

Primary citation

Hu, C.,Inoue, H.,Sun, W.,Takeshita, Y.,Huang, Y.,Xu, Y.,Kanoh, J.,Chen, Y.
Structural insights into chromosome attachment to the nuclear envelope by an inner nuclear membrane protein Bqt4 in fission yeast.
Nucleic Acids Res., 47:1573-1584, 2019

PubMed Abstract: The dynamic association of chromosomes with the nuclear envelope (NE) is essential for chromosome maintenance. Schizosaccharomyces pombe inner nuclear membrane protein Bqt4 plays a critical role in connecting telomeres to the NE, mainly through a direct interaction with the telomeric protein Rap1. Bqt4 also interacts with Lem2 for pericentric heterochromatin maintenance. How Bqt4 coordinates the interactions with different proteins to exert their functions is unclear. Here, we report the crystal structures of the N-terminal domain of Bqt4 in complexes with Bqt4-binding motifs from Rap1, Lem2, and Sad1. The structural, biochemical and cellular analyses reveal that the N-terminal domain of Bqt4 is a protein-interaction module that recognizes a consensus motif and plays essential roles in telomere-NE association and meiosis progression. Phosphorylation of Bqt4-interacting proteins may act as a switch to regulate these interactions during cell cycles. Our studies provide structural insights into the identification and regulation of Bqt4-mediated interactions.

PubMed: 30462301
DOI: 10.1093/nar/gky1186

Experimental method

X-RAY DIFFRACTION (2.704 Å)