ArticleJournal of molecular biology2016
A Monomer of Pif1 Unwinds Double-Stranded DNA and It Is Regulated by the Nature of the Non-Translocating Strand at the 3'-End.
Article in Journal of molecular biology, 2016. 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, 22 citations in OpenAlex.
- Regulation of Pfh1 helicase activity by nucleic acid interactions and mitochondrial SSB.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Eukaryotic Pif1 helicase unwinds G-quadruplex and dsDNA using a conserved wedge.Nature communications · 2024Article
- Rrm3 and Pif1 division of labor during replication through leading and lagging strand G-quadruplex.Nucleic acids research · 2024Article
- Identification of the nuclear localization signal in the Saccharomyces cerevisiae Pif1 DNA helicase.PLoS genetics · 2023Article
- "Helicase" Activity promoted through dynamic interactions between a ssDNA translocase and a diffusing SSB protein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structural Studies of Pif1 Helicases from Thermophilic Bacteria.Microorganisms · 2023Article
- Pif1 Activity is Modulated by DNA Sequence and Structure.Biochemistry · 2022Article
- Quantitative and kinetic single-molecule analysis of DNA unwinding byBiophysics and physicobiology · 2022Article
- Structural and functional studies of SF1B Pif1 from Thermus oshimai reveal dimerization-induced helicase inhibition.Nucleic acids research · 2021Article
- Pif1, RPA, and FEN1 modulate the ability of DNA polymerase δ to overcome protein barriers during DNA synthesis.The Journal of biological chemistry · 2020Article
- Branched unwinding mechanism of the Pif1 family of DNA helicases.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structural basis for DNA unwinding at forked dsDNA by two coordinating Pif1 helicases.Nature communications · 2019Article
- Complementary roles of Pif1 helicase and single stranded DNA binding proteins in stimulating DNA replication through G-quadruplexes.Nucleic acids research · 2019Article
- Direct quantification of the translocation activities of Saccharomyces cerevisiae Pif1 helicase.Nucleic acids research · 2019Article
- Pif1 is essential for efficient replisome progression through lagging strand G-quadruplex DNA secondary structures.Nucleic acids research · 2018Article
- Pif1 helicase unfolding of G-quadruplex DNA is highly dependent on sequence and reaction conditions.The Journal of biological chemistry · 2018Article
- The signature motif of the Saccharomyces cerevisiae Pif1 DNA helicase is essential in vivo for mitochondrial and nuclear functions and in vitro for ATPase activity.Nucleic acids research · 2018Article
- Role of the Pif1-PCNA Complex in Pol δ-Dependent Strand Displacement DNA Synthesis and Break-Induced Replication.Cell reports · 2017Article
- Structure and function of Pif1 helicase.Biochemical Society transactions · 2017Review
- Chemo-mechanical pushing of proteins along single-stranded DNA.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Using a DNA polymerase coupled assay and FRET (Förster resonance energy transfer)-based helicase assays, in this work, we show that a monomer of Saccharomyces cerevisiae Pif1 can unwind dsDNA (double-stranded DNA). The helicase activity of a Pif1 monomer is modulated by the nature of the 3'-ssDNA (single-stranded DNA) tail of the substrate and its effect on a Pif1-dependent re-winding activity that is coupled to the opening of dsDNA. We propose that, in addition to the ssDNA site on the protein that interacts with the translocating strand, Pif1 has a second site that binds the 3'-ssDNA of the substrate. Interaction of DNA with this site modulates the degree to which re-winding counteracts unwinding. Depending on the nature of the 3'-tail and the length of the duplex DNA to be unwound, this activity is sufficiently strong to mask the helicase activity of a monomer. In excess Pif1 over the DNA, the Pif1-dependent re-winding of the opened DNA strongly limits unwinding, independent of the 3'-tail. We propose that, in this case, binding of DNA to the second site is precluded and modulation of the Pif1-dependent re-winding activity is largely lost.
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