ArticleThe Journal of biological chemistry2014
Structural and biophysical characterization of murine rif1 C terminus reveals high specificity for DNA cruciform structures.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 35 citations in OpenAlex.
- DNA-damage dependent isoform switching modulates RIF1 DNA repair complex assembly and phase separation.The Journal of biological chemistry · 2025Article
- Rif1 restrains the rate of replication origin firing in Xenopus laevis.Communications biology · 2023Article
- Interaction of Proteins with Inverted Repeats and Cruciform Structures in Nucleic Acids.International journal of molecular sciences · 2022Review
- 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
- RIF1 Links Replication Timing with Fork Reactivation and DNA Double-Strand Break Repair.International journal of molecular sciences · 2021Review
- Polo-like kinase 1 (Plk1) regulates DNA replication origin firing and interacts with Rif1 in Xenopus.Nucleic acids research · 2021Article
- A fork in the road: Where homologous recombination and stalled replication fork protection part ways.Seminars in cell & developmental biology · 2021Review
- RIF1 promotes replication fork protection and efficient restart to maintain genome stability.Nature communications · 2019Article
- Rif1 promotes association of G-quadruplex (G4) by its specific G4 binding and oligomerization activities.Scientific reports · 2019Article
- Both a Unique Motif at the C Terminus and an N-Terminal HEAT Repeat Contribute to G-Quadruplex Binding and Origin Regulation by the Rif1 Protein.Molecular and cellular biology · 2019Article
- Auxin sensing is a property of an unstructured domain in the Auxin Response Factor ETTIN of Arabidopsis thaliana.Scientific reports · 2018Article
- Shepherding DNA ends: Rif1 protects telomeres and chromosome breaks.Microbial cell (Graz, Austria) · 2018Review
- Rif1 phosphorylation site analysis in telomere length regulation and the response to damaged telomeres.DNA repair · 2018Article
- Oligomer formation and G-quadruplex binding by purified murine Rif1 protein, a key organizer of higher-order chromatin architecture.The Journal of biological chemistry · 2018Article
- Mouse Rif1 is a regulatory subunit of protein phosphatase 1 (PP1).Scientific reports · 2017Article
- A structural organization for the Disrupted in Schizophrenia 1 protein, identified by high-throughput screening, reveals distinctly folded regions, which are bisected by mental illness-related mutations.The Journal of biological chemistry · 2017Article
- Quarterly intrinsic disorder digest (April-May-June, 2014).Intrinsically disordered proteins · 2017Article
- Non-RVD mutations that enhance the dynamics of the TAL repeat array along the superhelical axis improve TALEN genome editing efficacy.Scientific reports · 2016Article
- Nuclear Architecture Organized by Rif1 Underpins the Replication-Timing Program.Molecular cell · 2016Article
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Authors and funding
6 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mammalian Rif1 is a key regulator of DNA replication timing, double-stranded DNA break repair, and replication fork restart. Dissecting the molecular functions of Rif1 is essential to understand how it regulates such diverse processes. However, Rif1 is a large protein that lacks well defined functional domains and is predicted to be largely intrinsically disordered; these features have hampered recombinant expression of Rif1 and subsequent functional characterization. Here we applied ESPRIT (expression of soluble proteins by random incremental truncation), an in vitro evolution-like approach, to identify high yielding soluble fragments encompassing conserved regions I and II (CRI and CRII) at the C-terminal region of murine Rif1. NMR analysis showed CRI to be intrinsically disordered, whereas CRII is partially folded. CRII binds cruciform DNA with high selectivity and micromolar affinity and thus represents a functional DNA binding domain. Mutational analysis revealed an α-helical region of CRII to be important for cruciform DNA binding and identified critical residues. Thus, we present the first structural study of the mammalian Rif1, identifying a domain that directly links its function to DNA binding. The high specificity of Rif1 for cruciform structures is significant given the role of this key protein in regulating origin firing and DNA repair.
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