5NVR

Crystal structure of the Rif1 N-terminal domain (RIF1-NTD) from Saccharomyces cerevisiae

5NVR の概要

• エントリーDOI: 10.2210/pdb5nvr/pdb
• 分子名称: Telomere length regulator protein RIF1 (1 entity in total)
• 機能のキーワード: telomere maintenance, dna double-strand break repair, irregular helical repeat, all-alpha fold, structural protein
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 129054.05

構造登録者

Bunker, R.D.,Shi, T.,Thoma, N.H. (登録日: 2017-05-04, 公開日: 2017-06-14, 最終更新日: 2024-10-09)

主引用文献

Mattarocci, S.,Reinert, J.K.,Bunker, R.D.,Fontana, G.A.,Shi, T.,Klein, D.,Cavadini, S.,Faty, M.,Shyian, M.,Hafner, L.,Shore, D.,Thoma, N.H.,Rass, U.
Rif1 maintains telomeres and mediates DNA repair by encasing DNA ends.
Nat. Struct. Mol. Biol., 24:588-595, 2017

PubMed Abstract: In yeast, Rif1 is part of the telosome, where it inhibits telomerase and checkpoint signaling at chromosome ends. In mammalian cells, Rif1 is not telomeric, but it suppresses DNA end resection at chromosomal breaks, promoting repair by nonhomologous end joining (NHEJ). Here, we describe crystal structures for the uncharacterized and conserved ∼125-kDa N-terminal domain of Rif1 from Saccharomyces cerevisiae (Rif1-NTD), revealing an α-helical fold shaped like a shepherd's crook. We identify a high-affinity DNA-binding site in the Rif1-NTD that fully encases DNA as a head-to-tail dimer. Engagement of the Rif1-NTD with telomeres proved essential for checkpoint control and telomere length regulation. Unexpectedly, Rif1-NTD also promoted NHEJ at DNA breaks in yeast, revealing a conserved role of Rif1 in DNA repair. We propose that tight associations between the Rif1-NTD and DNA gate access of processing factors to DNA ends, enabling Rif1 to mediate diverse telomere maintenance and DNA repair functions.

PubMed: 28604726
DOI: 10.1038/nsmb.3420

実験手法

X-RAY DIFFRACTION (3.95 Å)