DNA segment capture by Smc5/6 holocomplexes
Open accessPublished version of a preprint
Abstract
Three distinct structural maintenance of chromosomes (SMC) complexes facilitate chromosome folding and segregation in eukaryotes, presumably by DNA loop extrusion. How SMCs interact with DNA to extrude loops is not well understood. Among the SMC complexes, Smc5/6 has dedicated roles in DNA repair and preventing a buildup of aberrant DNA junctions. In the present study, we describe the reconstitution of ATP-dependent DNA loading by yeast Smc5/6 rings. Loading strictly requires the Nse5/6 subcomplex which opens the kleisin neck gate. We show that plasmid molecules are topologically entrapped in the kleisin and two SMC subcompartments, but not in the full SMC compartment. This is explained by the SMC compartment holding a looped DNA segment and by kleisin locking it in place when passing between the two flanks of the loop for neck-gate closure. Related segment capture events may provide the power stroke in subsequent DNA extrusion steps, possibly also in other SMC complexes, thus providing a unifying principle for DNA loading and extrusion.
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Cites
Highly accurate protein structure prediction with AlphaFold
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“(2) In the ‘juxtaposed state’, the heads are ATP-disengaged and the Smc5 and Smc6 arms co-align yielding a closed SMC compartment 21.”
BackgroundHuman cohesin compacts DNA by loop extrusion
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Condensin structures chromosomal DNA through topological links
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SMC motor proteins extrude DNA asymmetrically and can switch directions
Barth, R., Davidson, I. F., van der Torre, J., Taschner, M., Gruber, S., Peters, J.-M., & Dekker, C. (2025) · Cell · doi:10.1016/j.cell.2024.12.020 · Cited by 40 · see citing works
Self-citationStructural basis for plasmid restriction by SMC JET nuclease
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Self-citation
- Authors
- Taschner, M., & Gruber, S.
- Affiliations
- University of Lausanne (CH)
- Corresponding author
- Gruber, Stephan
- Venue
- Nature Structural & Molecular Biology
- Published
- 2023-04-03
- Volume
- 30
- Issue
- 5
- Pages
- 619-628
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- PMC
- PMC10191858
- OpenAlex
- W4362521393
- Cited by
- 39
- References
- 5
- Citations by year
- 2026: 10 · 2025: 12 · 2024: 9 · 2023: 8
- FWCI
- 3.46
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Nature Structural & Molecular Biology (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- SERVAL (Université de Lausanne) (submittedVersion, cc-by)
- IRIS (submittedVersion, cc-by)
- Funders
- National Science Foundation
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (170242)
- Université de Lausanne
- H2020 European Research Council (724482)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- Smc5/6 complex, structural maintenance of chromosomes, DNA loop extrusion, DNA loading, ATP-dependent DNA binding, plasmid DNA, DNA repair, chromosome segregation
- MeSH terms
- Chromosomal Proteins, Non-Histone, Chromosomes, DNA, DNA Repair, Saccharomyces cerevisiae, Cell Cycle Proteins, Saccharomyces cerevisiae Proteins, Multiprotein Complexes
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