ArticleNucleic acids research2015
Mapping the interactions of the single-stranded DNA binding protein of bacteriophage T4 (gp32) with DNA lattices at single nucleotide resolution: gp32 monomer binding.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 32 citations in OpenAlex.
- Functional Integration of the Bacteriophage T4 DNA Replication Complex: The Multiple Roles of the ssDNA Binding Protein (gp32).Biochemistry · 2026Article
- Bacteriophage T4 gene 32 protein: Insights into its interaction with ssDNA, binding cooperativity, and conformational change.PloS one · 2026Article
- Functional integration of the bacteriophage T4 DNA replication complex: The multiple roles of the ssDNA binding protein (gp32).bioRxiv : the preprint server for biology · 2025Article
- Recombinase-Controlled Multiphase Condensates Accelerate Nucleic Acid Amplification and CRISPR-Based Diagnostics.Journal of the American Chemical Society · 2025Article
- Diverse single-stranded nucleic acid binding proteins enable both stable protection and rapid exchange required for biological function.QRB discovery · 2025Article
- Structural and functional insights into the interaction between the bacteriophage T4 DNA processing proteins gp32 and Dda.Nucleic acids research · 2024Article
- Article
- Single molecule technique unveils the role of electrostatic interactions in ssDNA-gp32 molecular complex stability.RSC advances · 2024Article
- Dynamic structure of T4 gene 32 protein filaments facilitates rapid noncooperative protein dissociation.Nucleic acids research · 2023Article
- Unravelling How Single-Stranded DNA Binding Protein Coordinates DNA Metabolism Using Single-Molecule Approaches.International journal of molecular sciences · 2023Review
- Characterization of the T4 gp32-ssDNA complex by native, cross-linking, and ultraviolet photodissociation mass spectrometry.Chemical science · 2021Article
- A comparative study of protein-ssDNA interactions.NAR genomics and bioinformatics · 2021Article
- Mapping DNA conformations and interactions within the binding cleft of bacteriophage T4 single-stranded DNA binding protein (gp32) at single nucleotide resolution.Nucleic acids research · 2021Article
- Unlimited Cooperativity ofFrontiers in microbiology · 2021Article
- Local DNA Base Conformations and Ligand Intercalation in DNA Constructs Containing Optical Probes.Biophysical journal · 2019Article
- Structural alteration of DNA induced by viral protein R of HIV-1 triggers the DNA damage response.Retrovirology · 2018Article
- Article
- Structural Basis for DNA Recognition of a Single-stranded DNA-binding Protein from Enterobacter Phage Enc34.Scientific reports · 2017Article
- Isothermal Amplification of Long, Discrete DNA Fragments Facilitated by Single-Stranded Binding Protein.Scientific reports · 2017Article
- Using microsecond single-molecule FRET to determine the assembly pathways of T4 ssDNA binding protein onto model DNA replication forks.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Combining biophysical measurements on T4 bacteriophage replication complexes with detailed structural information can illuminate the molecular mechanisms of these 'macromolecular machines'. Here we use the low energy circular dichroism (CD) and fluorescent properties of site-specifically introduced base analogues to map and quantify the equilibrium binding interactions of short (8 nts) ssDNA oligomers with gp32 monomers at single nucleotide resolution. We show that single gp32 molecules interact most directly and specifically near the 3'-end of these ssDNA oligomers, thus defining the polarity of gp32 binding with respect to the ssDNA lattice, and that only 2-3 nts are directly involved in this tight binding interaction. The loss of exciton coupling in the CD spectra of dimer 2-AP (2-aminopurine) probes at various positions in the ssDNA constructs, together with increases in fluorescence intensity, suggest that gp32 binding directly extends the sugar-phosphate backbone of this ssDNA oligomer, particularly at the 3'-end and facilitates base unstacking along the entire 8-mer lattice. These results provide a model (and 'DNA map') for the isolated gp32 binding to ssDNA targets, which serves as the nucleation step for the cooperative binding that occurs at transiently exposed ssDNA sequences within the functioning T4 DNA replication complex.
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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.