G-quadruplex–stalled eukaryotic replisome structure reveals helical inchworm DNA translocation

DNA G-quadruplexes (G4s) are non-B-form DNA secondary structures that threaten genome stability by impeding DNA replication. To elucidate how G4s induce replication fork arrest, we characterized fork collisions with preformed G4s in the parental DNA using reconstituted yeast and human replisomes. We demonstrate that a single G4 in the leading strand template is sufficient to stall replisomes by arresting the CMG helicase. Cryo-electron microscopy structures of stalled yeast and human CMG complexes reveal that the folded G4 is lodged inside the central CMG channel, arresting translocation. The G4 stabilizes the CMG at distinct translocation intermediates, suggesting an unprecedented helical inchworm mechanism for DNA translocation. These findings illuminate the eukaryotic replication fork mechanism under normal and perturbed conditions.

Authors

Institutions

Publication Details

Journal
Science
Published
2025-03-06
DOI
https://doi.org/10.1126/science.adt1978
Citations
20
Primary Topic
Advanced biosensing and bioanalysis techniques
Type
article
Field-Weighted Citation Impact
16.12
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

G-quadruplex–stalled eukaryotic replisome structure reveals helical inchworm DNA translocation

Dirk Remus, Chong M. Lee, Jan-Gert Brüning, Richard K. Hite et al.
20 citations
Science
Advanced biosensing and bioanalysis techniques
16.12
article

G-quadruplex–stalled eukaryotic replisome structure reveals helical inchworm DNA translocation

Dirk Remus, Chong M. Lee, Jan-Gert Brüning, Richard K. Hite, Charanya Kumar, Sujan Devbhandari, Benjamin Allwein, Sahil Batra, Kenneth J. Marians, Soon Bahng
article en
20 citations

Abstract

DNA G-quadruplexes (G4s) are non-B-form DNA secondary structures that threaten genome stability by impeding DNA replication. To elucidate how G4s induce replication fork arrest, we characterized fork collisions with preformed G4s in the parental DNA using reconstituted yeast and human replisomes. We demonstrate that a single G4 in the leading strand template is sufficient to stall replisomes by arresting the CMG helicase. Cryo-electron microscopy structures of stalled yeast and human CMG complexes reveal that the folded G4 is lodged inside the central CMG channel, arresting translocation. The G4 stabilizes the CMG at distinct translocation intermediates, suggesting an unprecedented helical inchworm mechanism for DNA translocation. These findings illuminate the eukaryotic replication fork mechanism under normal and perturbed conditions.

ScienceVol. 387(6738)
Memorial Sloan Kettering Cancer Center (US), Cornell University (US)
Life below water
Openalex Percentile: Top 1%
Advanced biosensing and bioanalysis techniques
16.12
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.