ArticleThe Journal of biological chemistry2018
Oligomer formation and G-quadruplex binding by purified murine Rif1 protein, a key organizer of higher-order chromatin architecture.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 44 citations in OpenAlex.
- Fuzzy protein-DNA interactions and beyond: A common theme in transcription?Current opinion in structural biology · 2024Review
- Bioactive nutraceuticals as G4 stabilizers: potential cancer prevention and therapy-a critical review.Naunyn-Schmiedeberg's archives of pharmacology · 2024Review
- Shedding Light on the Interaction Between Rif1 and Telomeres in Ovarian Cancer.Aging and disease · 2024Review
- Where and when to start: Regulating DNA replication origin activity in eukaryotic genomes.Nucleus (Austin, Tex.) · 2023Review
- An AlphaFold2 map of the 53BP1 pathway identifies a direct SHLD3-RIF1 interaction critical for shieldin activity.EMBO reports · 2023Article
- Rif1 restrains the rate of replication origin firing in Xenopus laevis.Communications biology · 2023Article
- Aberrant association of chromatin with nuclear periphery induced by Rif1 leads to mitotic defect.Life science alliance · 2023Article
- The organizer of chromatin topology RIF1 ensures cellular resilience to DNA replication stress.Life science alliance · 2023Article
- Rif1 interacts with non-canonical polycomb repressive complex PRC1.6 to regulate mouse embryonic stem cells fate potential.Cell regeneration (London, England) · 2022Article
- Temporal control of late replication and coordination of origin firing by self-stabilizing Rif1-PP1 hubs inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Exploring the Parallel G-Quadruplex Nucleic Acid World: A Spectroscopic and Computational Investigation on the Binding of the c-myc Oncogene NHE III1 Region by the Phytochemical Polydatin.Molecules (Basel, Switzerland) · 2022Article
- Telomere length regulation by Rif1 protein fromeLife · 2022Article
- SPR Analysis of SUMO-Murine Rap1-Interacting Factor 1 C-Terminal Domain Interaction with G4.Biosensors · 2022Article
- Loss of full-length DNA replication regulator Rif1 in two-cell embryos is associated with zygotic transcriptional activation.The Journal of biological chemistry · 2021Article
- Nuclear organisation and replication timing are coupled through RIF1-PP1 interaction.Nature communications · 2021Article
- A predictable conserved DNA base composition signature defines human core DNA replication origins.Nature communications · 2020Article
- Heterochromatin replication goes hand in hand with telomere protection.Nature structural & molecular biology · 2020Review
- Integrative characterization of G-Quadruplexes in the three-dimensional chromatin structure.Epigenetics · 2019Article
- Dormant origin signaling during unperturbed replication.DNA repair · 2019Review
- Rif1 promotes association of G-quadruplex (G4) by its specific G4 binding and oligomerization activities.Scientific reports · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rap1-interacting protein 1 (Rif1) regulates telomere length in budding yeast. We previously reported that, in metazoans and fission yeast, Rif1 also plays pivotal roles in controlling genome-wide DNA replication timing. We proposed that Rif1 may assemble chromatin compartments that contain specific replication-timing domains by promoting chromatin loop formation. Rif1 also is involved in DNA lesion repair, restart after replication fork collapse, anti-apoptosis activities, replicative senescence, and transcriptional regulation. Although multiple physiological functions of Rif1 have been characterized, biochemical and structural information on mammalian Rif1 is limited, mainly because of difficulties in purifying the full-length protein. Here, we expressed and purified the 2418-amino-acid-long, full-length murine Rif1 as well as its partially truncated variants in human 293T cells. Hydrodynamic analyses indicated that Rif1 forms elongated or extended homo-oligomers in solution, consistent with the presence of a HEAT-type helical repeat segment known to adopt an elongated shape. We also observed that the purified murine Rif1 bound G-quadruplex (G4) DNA with high specificity and affinity, as was previously shown for Rif1 from fission yeast. Both the N-terminal (HEAT-repeat) and C-terminal segments were involved in oligomer formation and specifically bound G4 DNA, and the central intrinsically disordered polypeptide segment increased the affinity for G4. Of note, pulldown assays revealed that Rif1 simultaneously binds multiple G4 molecules. Our findings support a model in which Rif1 modulates chromatin loop structures through binding to multiple G4 assemblies and by holding chromatin fibers together.
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