Rif1 and Rif2 shape telomere function and architecture through multivalent Rap1 interactions

Shi, Tianlai, Bunker, Richard D, Mattarocci, Stefano, Ribeyre, Cyril, Faty, Mahamadou, Gut, Heinz, Scrima, Andrea, Rass, Ulrich, Rubin, Seth M, Shore, David and Thomä, Nicolas H (2013) Rif1 and Rif2 shape telomere function and architecture through multivalent Rap1 interactions. Cell, 153 (6). pp. 1340-1353. ISSN 0092-8674

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Yeast telomeres comprise irregular TG₁₋₃ DNA repeats bound by the general transcription factor Rap1. Rif1 and Rif2, along with Rap1, form the telosome, a protective cap that inhibits telomerase, counteracts SIR-mediated transcriptional silencing, and prevents inadvertent recognition of telomeres as DNA double-strand breaks. We provide a molecular, biochemical, and functional dissection of the protein backbone at the core of the yeast telosome. The X-ray structures of Rif1 and Rif2 bound to the Rap1 C-terminal domain and that of the Rif1 C terminus are presented. Both Rif1 and Rif2 have separable and independent Rap1-binding epitopes, allowing Rap1 binding over large distances (42-110 Å). We identify tetramerization (Rif1) and polymerization (Rif2) modules that, in conjunction with the long-range binding, give rise to a higher-order architecture that interlinks Rap1 units. This molecular Velcro relies on Rif1 and Rif2 to recruit and stabilize Rap1 on telomeric arrays and is required for telomere homeostasis in vivo.

Item Type: Article
Keywords: Telomeres, Rif1, Rif2, Rap1, higher-order chromatin structure
Schools and Departments: School of Life Sciences > Sussex Centre for Genome Damage and Stability
Research Centres and Groups: Genome Damage and Stability Centre
Subjects: Q Science
Depositing User: Ulrich Rass
Date Deposited: 24 Sep 2018 13:43
Last Modified: 24 Sep 2018 13:43
URI: http://srodev.sussex.ac.uk/id/eprint/78930
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