ArticleNucleic acids research2010
Structure and DNA binding activity of the mouse condensin hinge domain highlight common and diverse features of SMC proteins.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 96 citations in OpenAlex.
- Condensin complexes: from chromatin organization to disease.Nucleus (Austin, Tex.) · 2026Review
- The Phenotype ofGenes · 2025Article
- Condensin II interacts with BLM helicase in S phase to maintain genome stability.Communications biology · 2025Article
- Adding a twist to the loops: the role of DNA superhelicity in the organization of chromosomes by SMC protein complexes.Biochemical Society transactions · 2024Review
- Condensin pinches a short negatively supercoiled DNA loop during each round of ATP usage.The EMBO journal · 2023Article
- DNA tension-modulated translocation and loop extrusion by SMC complexes revealed by molecular dynamics simulations.Nucleic acids research · 2022Article
- Theory and simulations of condensin mediated loop extrusion in DNA.Nature communications · 2021Article
- Modeling of DNA binding to the condensin hinge domain using molecular dynamics simulations guided by atomic force microscopy.PLoS computational biology · 2021Article
- Nse5/6 is a negative regulator of the ATPase activity of the Smc5/6 complex.Nucleic acids research · 2021Article
- Prospective pathway signaling and prognostic values of MicroRNA-9 in ovarian cancer based on gene expression omnibus (GEO): a bioinformatics analysis.Journal of ovarian research · 2021Article
- The condensin holocomplex cycles dynamically between open and collapsed states.Nature structural & molecular biology · 2020Article
- Structural insights into DNA loop extrusion by SMC protein complexes.Current opinion in structural biology · 2020Review
- Condensin complexes: understanding loop extrusion one conformational change at a time.Biochemical Society transactions · 2020Review
- Relating SMCHD1 structure to its function in epigenetic silencing.Biochemical Society transactions · 2020Review
- Human Condensin I and II Drive Extensive ATP-Dependent Compaction of Nucleosome-Bound DNA.Molecular cell · 2020Article
- Modes of action of the archaeal Mre11/Rad50 DNA-repair complex revealed by fast-scan atomic force microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Transient DNA Occupancy of the SMC Interarm Space in Prokaryotic Condensin.Molecular cell · 2019Article
- Isolation of Fission Yeast Condensin Temperature-Sensitive Mutants with Single Amino Acid Substitutions Targeted to Hinge Domain.G3 (Bethesda, Md.) · 2019Article
- Structural basis of HEAT-kleisin interactions in the human condensin I subcomplex.EMBO reports · 2019Article
- A folded conformation of MukBEF and cohesin.Nature structural & molecular biology · 2019Article
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Structural Maintenance of Chromosomes (SMC) proteins are vital for a wide range of processes including chromosome structure and dynamics, gene regulation and DNA repair. Eukaryotes have three SMC complexes, consisting of heterodimeric pairs of six different SMC proteins along with several specific regulatory subunits. In addition to their other functions, all three SMC complexes play distinct roles in DNA repair. Cohesin (SMC1-SMC3) is involved in DNA double-strand break repair, condensin (SMC2-SMC4) participates in single-strand break (SSB) repair, and the SMC5-SMC6 complex functions in various DNA repair pathways. SMC proteins consist of N- and C-terminal domains that fold back onto each other to create an ATPase 'head' domain, connected to a central 'hinge' domain via long coiled-coils. The hinge domain mediates dimerization of SMC proteins and binds DNA, but it is not clear to what purpose this activity serves. We studied the structure and function of the condensin hinge domain from mouse. While the SMC hinge domain structure is largely conserved from prokaryotes to eukaryotes, its function seems to have diversified throughout the course of evolution. The condensin hinge domain preferentially binds single-stranded DNA. We propose that this activity plays a role in the SSB repair function of the condensin complex.
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