5NVR
Crystal structure of the Rif1 N-terminal domain (RIF1-NTD) from Saccharomyces cerevisiae
Summary for 5NVR
| Entry DOI | 10.2210/pdb5nvr/pdb |
| Descriptor | Telomere length regulator protein RIF1 (1 entity in total) |
| Functional Keywords | telomere maintenance, dna double-strand break repair, irregular helical repeat, all-alpha fold, structural protein |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 129054.05 |
| Authors | Bunker, R.D.,Shi, T.,Thoma, N.H. (deposition date: 2017-05-04, release date: 2017-06-14, Last modification date: 2024-10-09) |
| Primary citation | 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 Cited by 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: 28604726DOI: 10.1038/nsmb.3420 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.95 Å) |
Structure validation
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