ArticleNucleic acids research2013
Physical and functional interaction between yeast Pif1 helicase and Rim1 single-stranded DNA binding protein.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 40 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
- 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
- Identification of the nuclear localization signal in the Saccharomyces cerevisiae Pif1 DNA helicase.PLoS genetics · 2023Article
- Role and Regulation of Pif1 Family Helicases at the Replication Fork.International journal of molecular sciences · 2022Review
- Pif1 Activity is Modulated by DNA Sequence and Structure.Biochemistry · 2022Article
- Mammalian Resilience Revealed by a Comparison of Human Diseases and Mouse Models Associated With DNA Helicase Deficiencies.Frontiers in molecular biosciences · 2022Review
- Mitochondrial Function Are Disturbed in the Presence of the Anticancer Drug, 3-Bromopyruvate.International journal of molecular sciences · 2021Article
- Characterization of the telomerase modulating activities of yeast DNA helicases.Methods in enzymology · 2021Article
- Mitochondrial genetic variation is enriched in G-quadruplex regions that stall DNA synthesis in vitro.Human molecular genetics · 2020Article
- Review
- Excessive excision of correct nucleotides during DNA synthesis explained by replication hurdles.The EMBO journal · 2020Article
- Review
- Structural basis for adPEO-causing mutations in the mitochondrial TWINKLE helicase.Human molecular genetics · 2019Article
- A stable tetramer is not the only oligomeric state that mitochondrial single-stranded DNA binding proteins can adopt.The Journal of biological chemistry · 2019Article
- The mitochondrial single-stranded DNA binding protein from S. cerevisiae, Rim1, does not form stable homo-tetramers and binds DNA as a dimer of dimers.Nucleic acids research · 2018Article
- Screening for amyloid proteins in the yeast proteome.Current genetics · 2018Article
- Structure and function of Pif1 helicase.Biochemical Society transactions · 2017Review
- A 3'-5' exonuclease activity embedded in the helicase core domain of Candida albicans Pif1 helicase.Scientific reports · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
Pif1 helicase plays various roles in the maintenance of nuclear and mitochondrial genome integrity in most eukaryotes. Here, we used a proteomics approach called isotopic differentiation of interactions as random or targeted to identify specific protein complexes of Saccharomyces cerevisiae Pif1. We identified a stable association between Pif1 and a mitochondrial SSB, Rim1. In vitro co-precipitation experiments using recombinant proteins indicated a direct interaction between Pif1 and Rim1. Fluorescently labeled Rim1 was titrated with Pif1 resulting in an increase in anisotropy and a K(d) value of 0.69 µM. Deletion mutagenesis revealed that the OB-fold domain and the C-terminal tail of Rim1 are both involved in interaction with Pif1. However, a Rim1 C-terminal truncation (Rim1ΔC18) exhibited a nearly 4-fold higher K(d) value. Rim1 stimulated Pif1 DNA helicase activity by 4- to 5-fold, whereas Rim1ΔC18 stimulated Pif1 by 2-fold. Hence, two regions of Rim1, the OB-fold domain and the C-terminal domain, interact with Pif1. One of these interactions occurs through the N-terminal domain of Pif1 because a deletion mutant of Pif1 (Pif1ΔN) retained interaction with Rim1 but did not exhibit stimulation of helicase activity. In light of our in vivo and in vitro data, and previous work, it is likely that the Rim1-Pif1 interaction plays a role in coordination of their functions in mtDNA metabolism.
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