ArticleThe Journal of biological chemistry2013
Yeast Pif1 helicase exhibits a one-base-pair stepping mechanism for unwinding duplex DNA.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed.
- Bacterial RecD2 is a processive single-stranded DNA translocase with strand-switching capacity at DNA forks.Nucleic acids research · 2025Article
- The Role of SF1 and SF2 Helicases in Biotechnological Applications.Applied biochemistry and biotechnology · 2024Review
- Two residues in the DNA binding site of Pif1 helicase are essential for nuclear functions but dispensable for mitochondrial respiratory growth.Nucleic acids research · 2024Article
- Pif1 Helicase Mediates Remodeling of Protein-Nucleic Acid Complexes by Promoting Dissociation of Sub1 from G-Quadruplex DNA and Cdc13 from G-Rich Single-Stranded DNA.Biochemistry · 2023Article
- How much (ATP) does it cost to build a trypanosome? A theoretical study on the quantity of ATP needed to maintain and duplicate a bloodstream-form Trypanosoma brucei cell.PLoS pathogens · 2023Article
- Insight into the biochemical mechanism of DNA helicases provided by bulk-phase and single-molecule assays.Methods (San Diego, Calif.) · 2022Review
- A structural feature of Dda helicase which enhances displacement of streptavidin and trp repressor from DNA.Protein science : a publication of the Protein Society · 2022Article
- Pif1 Helicases and the Evidence for a Prokaryotic Origin of Helitrons.Molecular biology and evolution · 2022Article
- Pif1 Activity is Modulated by DNA Sequence and Structure.Biochemistry · 2022Article
- Alignment of helicases on single-stranded DNA increases activity.Methods in enzymology · 2022Article
- Monitoring helicase-catalyzed unwinding of multiple duplexes simultaneously.Methods in enzymology · 2022Article
- The large bat Helitron DNA transposase forms a compact monomeric assembly that buries and protects its covalently bound 5'-transposon end.Molecular cell · 2021Article
- Budding yeast Rap1, but not telomeric DNA, is inhibitory for multiple stages of DNA replication in vitro.Nucleic acids research · 2021Article
- Structural and functional studies of SF1B Pif1 from Thermus oshimai reveal dimerization-induced helicase inhibition.Nucleic acids research · 2021Article
- Dynamic regulation of Pif1 acetylation is crucial to the maintenance of genome stability.Current genetics · 2021Review
- RNA helicases required for viral propagation in humans.The Enzymes · 2021Review
- 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
- Direct quantification of the translocation activities of Saccharomyces cerevisiae Pif1 helicase.Nucleic acids research · 2019Article
- DNA-unwinding activity ofThe Journal of biological chemistry · 2018Article
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7 authors.
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Abstract
Kinetic analysis of the DNA unwinding and translocation activities of helicases is necessary for characterization of the biochemical mechanism(s) for this class of enzymes. Saccharomyces cerevisiae Pif1 helicase was characterized using presteady state kinetics to determine rates of DNA unwinding, displacement of streptavidin from biotinylated DNA, translocation on single-stranded DNA (ssDNA), and ATP hydrolysis activities. Unwinding of substrates containing varying duplex lengths was fit globally to a model for stepwise unwinding and resulted in an unwinding rate of ∼75 bp/s and a kinetic step size of 1 base pair. Pif1 is capable of displacing streptavidin from biotinylated oligonucleotides with a linear increase in the rates as the length of the oligonucleotides increased. The rate of translocation on ssDNA was determined by measuring dissociation from varying lengths of ssDNA and is essentially the same as the rate of unwinding of dsDNA, making Pif1 an active helicase. The ATPase activity of Pif1 on ssDNA was determined using fluorescently labeled phosphate-binding protein to measure the rate of phosphate release. The quantity of phosphate released corresponds to a chemical efficiency of 0.84 ATP/nucleotides translocated. Hence, when all of the kinetic data are considered, Pif1 appears to move along DNA in single nucleotide or base pair steps, powered by hydrolysis of 1 molecule of ATP.
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