8YNU

Crystal structure of the myb domain of S.pombe Tbf1 in the P222 space group

Summary for 8YNU

• Entry DOI: 10.2210/pdb8ynu/pdb
• Descriptor: Telomeric DNA-binding factor trf1, GLYCEROL (3 entities in total)
• Functional Keywords: telomere binding protein, dna binding protein
• Biological source: Schizosaccharomyces pombe 972h-
• Total number of polymer chains: 2
• Total formula weight: 18214.99

Authors

Zhou, Y.Z.,Wu, Z.F. (deposition date: 2024-03-12, release date: 2025-04-09)

Primary citation

Wu, Z.,Gu, X.,Zha, L.,Yang, Q.,Zhou, Y.,Zeng, Z.
Structural and functional insights into yeast Tbf1 as an atypical telomeric repeat-binding factor.
Structure, 32:889-898.e3, 2024

PubMed Abstract: Telomeric repeat-binding factor 1 (Tbf1) has a similar architecture as the TRF family of telomeric proteins and plays important roles in both telomere homeostasis and ribosome regulation. However, the molecular basis of why Tbf1 has such different functions compared to other TRFs remains unclear. Here, we present the crystal structures of the TRF homology (TRFH) and Myb-L domains from Schizosaccharomyces pombe Tbf1 (spTbf1). TRFH-mediated homodimerization is essential for spTbf1 stability. Importantly, spTbf1 lacks the conserved docking motif for interactions with telomeric proteins, explaining why spTbf1 does not participate in the assembly of the shelterin complex. Finally, structural and biochemical analyses demonstrate that TRFH and Myb-L domains as well as the loop region of spTbf1 coordinate to recognize S. pombe telomeric double-stranded DNA. Overall, our findings provide structural and functional insights into how fungi Tbf1 acts as an atypical telomeric repeat-binding factor, which helps to understand the evolution of TRFH-containing telomeric proteins.

PubMed: 38677290
DOI: 10.1016/j.str.2024.04.002

Experimental method

X-RAY DIFFRACTION (1.76 Å)