Evidence map›Paper›PMID 40138714›Full record

ArticleNucleic acids research2025

Spatiotemporal dynamics of protamine-DNA condensation revealed by high-speed atomic force microscopy.

Goro Nishide, Keesiang Lim, Akiko Kobayashi, Yujia Qiu, Masaharu Hazawa, Toshio Ando, Yuki Okada, Richard W Wong

Abstract read
In one paragraph

Article in Nucleic acids research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Measuring bridging forces in protein-DNA condensates.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  9. Review
  10. Review
  11. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Goro NishideDivision of Nano Life Science in the Graduate School of Frontier Science Initiative, WISE Program for Nano-Precision Medicine, Science and Technology, Kanazawa University, Kanazawa, Ishikawa 920-1192, Japan.
Keesiang LimWPI-Nano Life Science Institute, Kanazawa University, Kakuma-machi, Kanazawa, Ishikawa 920-1192, Japan.
Akiko KobayashiWPI-Nano Life Science Institute, Kanazawa University, Kakuma-machi, Kanazawa, Ishikawa 920-1192, Japan.
Yujia QiuDivision of Nano Life Science in the Graduate School of Frontier Science Initiative, Kanazawa University, Kanazawa Ishikawa 920-1192, Japan.
Masaharu HazawaWPI-Nano Life Science Institute, Kanazawa University, Kakuma-machi, Kanazawa, Ishikawa 920-1192, Japan.ORCID 0000-0003-0342-9016
Toshio AndoWPI-Nano Life Science Institute, Kanazawa University, Kakuma-machi, Kanazawa, Ishikawa 920-1192, Japan.ORCID 0000-0001-8819-154X
Yuki OkadaInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo113-0032, Japan.
Richard W WongDivision of Nano Life Science in the Graduate School of Frontier Science Initiative, WISE Program for Nano-Precision Medicine, Science and Technology, Kanazawa University, Kanazawa, Ishikawa 920-1192, Japan.ORCID 0000-0002-2131-6595

Funding

CREST JPMJCR22E3Hokuriku Bank grantKAKENHI 24K18449MEXTShimadzu Science Foundation, JapanTakeda Science FoundationWISE Program for Nano-Precision Medicine, Science, and Technology of Kanazawa UniversityWorld Premier International Research Center Initiative
6 · The paper itself

Abstract

Protamines (PRMs) play a crucial role in sperm chromatin condensation, replacing histones to form nucleo-PRM structures, specifically PRM-DNA complexes. Despite their importance in reproduction, the detailed mechanisms underlying PRM-mediated DNA condensation have remained elusive. In this study, we employed high-speed atomic force microscopy (HS-AFM) to directly visualize the real-time binding dynamics of PRM to DNA under physiological conditions. Our HS-AFM observations reveal that PRM insertion initiating the formation of DNA coils. Further, we observed a heterogeneous spatial distribution of PRM-induced DNA looping. With continuous PRM addition, DNA progresses through a series of folding transitions, forming coiled-like structures that evolve into clockwise spirals, rod-shaped intermediates, and ultimately toroid-like nanostructures. Based on these real-time observations, we propose the CARD (Coil-Assembly-Rod-Doughnut) model to describe the stepwise process of toroid formation during DNA condensation. Our findings underscore the versatility of HS-AFM in capturing the spatiotemporal dynamics of PRM-DNA interactions and provide critical insights into the molecular mechanisms driving PRM-induced chromatin compaction. This study advances our understanding of sperm chromatin architecture and offers a framework for future research into chromatin organization, reproductive biology, and nucleic acid therapeutics.

Indexed as

DNAProtaminesAnimalsChromatinMaleMicroscopy, Atomic ForceNucleic Acid ConformationSpermatozoaChromatinDNAProtamines

Identifiers

PMID40138714
PMCPMC11930356

What OpenQuestion holds

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Registered trials

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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.