ArticleNucleic acids research2016
Crystal structures of the BsPif1 helicase reveal that a major movement of the 2B SH3 domain is required for DNA unwinding.
Article in Nucleic acids research, 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, 32 citations in OpenAlex.
- Article
- Rare SNP in theNAR molecular medicine · 2025Article
- Structure-based discovery of first inhibitors targeting the helicase activity of human PIF1.Nucleic acids research · 2024Article
- 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
- Single-molecule visualization of Pif1 helicase translocation on single-stranded DNA.The Journal of biological chemistry · 2023Article
- Structural Studies of Pif1 Helicases from Thermophilic Bacteria.Microorganisms · 2023Article
- Tideglusib Inhibits Pif1 Helicase ofACS omega · 2022Article
- Role and Regulation of Pif1 Family Helicases at the Replication Fork.International journal of molecular sciences · 2022Review
- The large bat Helitron DNA transposase forms a compact monomeric assembly that buries and protects its covalently bound 5'-transposon end.Molecular cell · 2021Article
- An atomistic model of the coronavirus replication-transcription complex as a hexamer assembled around nsp15.The Journal of biological chemistry · 2021Article
- Srs2 and Pif1 as Model Systems for Understanding Sf1a and Sf1b Helicase Structure and Function.Genes · 2021Review
- 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
- 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 and functional analysis of the nucleotide and DNA binding activities of the human PIF1 helicase.Nucleic acids research · 2019Article
- 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
- The Pif1 signature motif of Pfh1 is necessary for both protein displacement and helicase unwinding activities, but is dispensable for strand-annealing activity.Nucleic acids research · 2018Article
- Insights into the structural and mechanistic basis of multifunctional S. cerevisiae Pif1p helicase.Nucleic acids research · 2018Article
- Structure and function of Pif1 helicase.Biochemical Society transactions · 2017Review
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pif1 helicases are ubiquitous members of the SF1B family and are essential for maintaining genome stability. It was speculated that Pif1-specific motifs may fold in specific structures, conferring distinct activities upon it. Here, we report the crystal structures of the Pif1 helicase from Bacteroides spp with and without adenosine triphosphate (ATP) analog/ssDNA. BsPif1 shares structural similarities with RecD2 and Dda helicases but has specific features in the 1B and 2B domains. The highly conserved Pif1 family specific sequence motif interacts with and constraints a putative pin-loop in domain 1B in a precise conformation. More importantly, we found that the 2B domain which contains a specific extended hairpin undergoes a significant rotation and/or movement upon ATP and DNA binding, which is absolutely required for DNA unwinding. We therefore propose a mechanism for DNA unwinding in which the 2B domain plays a predominant role. The fact that the conformational change regulates Pif1 activity may provide insight into the puzzling observation that Pif1 becomes highly processive during break-induced replication in association with Polδ, while the isolated Pif1 has low processivity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.