ArticleNucleic acids research2016
DNA compaction by the bacteriophage protein Cox studied on the single DNA molecule level using nanofluidic channels.
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 10 papers.
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Who cites it
10 citing papers in PubMed, 25 citations in OpenAlex.
- Structural basis for control of integrative and conjugative element excision and transfer by the oligomeric winged helix-turn-helix protein RdfS.Nucleic acids research · 2025Article
- High-throughput single-molecule nanofluidic studies onQRB discovery · 2025Article
- Assembly path dependence of telomeric DNA compaction by TRF1, TIN2, and SA1.Biophysical journal · 2023Article
- A quantitative binding model for the Apl protein, the dual purpose recombination-directionality factor and lysis-lysogeny regulator of bacteriophage 186.Nucleic acids research · 2020Article
- DNA looping by two 5-methylcytosine-binding proteins quantified using nanofluidic devices.Epigenetics & chromatin · 2020Article
- Nanoplumbing with 2D Metamaterials.Small (Weinheim an der Bergstrasse, Germany) · 2019Article
- Alpha-Synuclein Modulates the Physical Properties of DNA.Chemistry (Weinheim an der Bergstrasse, Germany) · 2018Article
- PrgB promotes aggregation, biofilm formation, and conjugation through DNA binding and compaction.Molecular microbiology · 2018Article
- Motor-like DNA motion due to an ATP-hydrolyzing protein under nanoconfinement.Scientific reports · 2018Article
- Studying protein-DNA interactions using atomic force microscopy.Seminars in cell & developmental biology · 2018Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Cox protein from bacteriophage P2 forms oligomeric filaments and it has been proposed that DNA can be wound up around these filaments, similar to how histones condense DNA. We here use fluorescence microscopy to study single DNA-Cox complexes in nanofluidic channels and compare how the Cox homologs from phages P2 and WΦ affect DNA. By measuring the extension of nanoconfined DNA in absence and presence of Cox we show that the protein compacts DNA and that the binding is highly cooperative, in agreement with the model of a Cox filament around which DNA is wrapped. Furthermore, comparing microscopy images for the wild-type P2 Cox protein and two mutants allows us to discriminate between compaction due to filament formation and compaction by monomeric Cox. P2 and WΦ Cox have similar effects on the physical properties of DNA and the subtle, but significant, differences in DNA binding are due to differences in binding affinity rather than binding mode. The presented work highlights the use of single DNA molecule studies to confirm structural predictions from X-ray crystallography. It also shows how a small protein by oligomerization can have great impact on the organization of DNA and thereby fulfill multiple regulatory functions.
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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.