Evidence map›Paper›PMID 42017784›Full record

ArticleeLife2026

SMC complex unidirectionally translocates DNA by coupling segment capture with an asymmetric kleisin path.

Masataka Yamauchi, Giovanni Bruno Brandani, Tsuyoshi Terakawa, Shoji Takada

Abstract read
In one paragraph

Article in eLife, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Motorized chain models of the ideal chromosome.Proceedings of the National Academy of Sciences of the United States of America · 2024
    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

4 authors.

Masataka YamauchiDepartment of Biophysics, Graduate School of Science, Kyoto University, Kitashirakawa Oiwakecho, Kyoto, Japan.ORCID https://orcid.org/0000-0002-5123-3993
Giovanni Bruno BrandaniDepartment of Biophysics, Graduate School of Science, Kyoto University, Kitashirakawa Oiwakecho, Kyoto, Japan.ORCID https://orcid.org/0000-0003-3379-0187
Tsuyoshi TerakawaDepartment of Biophysics, Graduate School of Science, Kyoto University, Kitashirakawa Oiwakecho, Kyoto, Japan.ORCID https://orcid.org/0000-0002-0151-1123
Shoji TakadaDepartment of Biophysics, Graduate School of Science, Kyoto University, Kitashirakawa Oiwakecho, Kyoto, Japan.ORCID https://orcid.org/0000-0001-5385-7217

Funding

JSPS KAKENHI 20H05934JSPS KAKENHI 21H02441MEXT grants "Program for Promoting Researches on the Supercomputer Fugaku" JPMXP1020230119
6 · The paper itself

Abstract

SMC (structural maintenance of chromosomes) protein complexes are ring-shaped molecular motors essential for genome folding. Despite recent progress, the detailed molecular mechanism of DNA translocation in concert with the ATP-driven conformational changes of the complex remains to be clarified. In this study, we elucidated the mechanisms of SMC action on DNA using all-atom and coarse-grained molecular dynamics simulations. We first created a near-atomic full-length model of a prokaryotic SMC-kleisin complex based on experimental structures and implemented ATP-dependent conformational changes using a structure-based coarse-grained model. We further incorporated key protein-DNA hydrogen-bond interactions derived from fully atomistic simulations. Extensive simulations of the SMC complex with 800 base pairs of duplex DNA over the ATP cycle observed unidirectional DNA translocation by the SMC complex. The process exhibited a step size of ~200 base pairs, wherein the SMC complex captured a DNA segment of about the same size within the SMC ring in the engaged state, followed by its pumping into the kleisin ring as ATP was hydrolyzed. Analysis of trajectories identified the asymmetric path of the kleisin as a critical factor for the observed unidirectionality.

Indexed as

Bacterial ProteinsCell Cycle ProteinsDNA, BacterialAdenosine TriphosphateMolecular Dynamics SimulationProtein ConformationAdenosine TriphosphateBacterial ProteinsCell Cycle ProteinsDNA, BacterialSMC protein, Bacteriacoarse-grained simulationmolecular biophysicsmolecular dynamics simulationnoneSMC complexesstructural biology

Identifiers

PMID42017784
PMCPMC13102395

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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.