4BJ5

Crystal structure of Rif2 in complex with the C-terminal domain of Rap1 (Rap1-RCT)

4BJ5 の概要

• エントリーDOI: 10.2210/pdb4bj5/pdb
• 関連するPDBエントリー: 4BJ1 4BJ6
• 分子名称: PROTEIN RIF2, DNA-BINDING PROTEIN RAP1, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: transcription, genome stability, telomere associated proteins, aaa+ fold
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 142138.59

構造登録者

Shi, T.,Bunker, R.D.,Gut, H.,Scrima, A.,Thoma, N.H. (登録日: 2013-04-16, 公開日: 2013-06-19, 最終更新日: 2023-12-20)

主引用文献

Shi, T.,Bunker, R.D.,Mattarocci, S.,Ribeyre, C.,Faty, M.,Gut, H.,Scrima, A.,Rass, U.,Rubin, S.M.,Shore, D.,Thoma, N.H.
Rif1 and Rif2 Shape Telomere Funcation and Architecture Through Multivalent RAP1 Interactions
Cell(Cambridge,Mass.), 153:1340-, 2013

PubMed Abstract: 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.

PubMed: 23746845
DOI: 10.1016/J.CELL.2013.05.007

実験手法

X-RAY DIFFRACTION (3.29 Å)