ArticleThe Journal of biological chemistry2015
Structural Basis for Dimer Formation of Human Condensin Structural Maintenance of Chromosome Proteins and Its Implications for Single-stranded DNA Recognition.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- 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
- SMCHD1's ubiquitin-like domain is required for N-terminal dimerization and chromatin localization.The Biochemical journal · 2021Article
- Modeling of DNA binding to the condensin hinge domain using molecular dynamics simulations guided by atomic force microscopy.PLoS computational biology · 2021Article
- 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
- The Fab portion of immunoglobulin G contributes to its binding to Fcγ receptor III.Scientific reports · 2019Article
- Transient DNA Occupancy of the SMC Interarm Space in Prokaryotic Condensin.Molecular cell · 2019Article
- Subunits of human condensins are potential therapeutic targets for cancers.Cell division · 2018Article
- Of Rings and Rods: Regulating Cohesin Entrapment of DNA to Generate Intra- and Intermolecular Tethers.PLoS genetics · 2016Review
Corrections and comments
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Authors and funding
14 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic structural maintenance of chromosome proteins (SMC) are major components of cohesin and condensins that regulate chromosome structure and dynamics during cell cycle. We here determine the crystal structure of human condensin SMC hinge heterodimer with ~30 residues of coiled coils. The structure, in conjunction with the hydrogen exchange mass spectrometry analyses, revealed the structural basis for the specific heterodimer formation of eukaryotic SMC and that the coiled coils from two different hinges protrude in the same direction, providing a unique binding surface conducive for binding to single-stranded DNA. The characteristic hydrogen exchange profiles of peptides constituted regions especially across the hinge-hinge dimerization interface, further suggesting the structural alterations upon single-stranded DNA binding and the presence of a half-opened state of hinge heterodimer. This structural change potentially relates to the DNA loading mechanism of SMC, in which the hinge domain functions as an entrance gate as previously proposed for cohesin. Our results, however, indicated that this is not the case for condensins based on the fact that the coiled coils are still interacting with each other, even when DNA binding induces structural changes in the hinge region, suggesting the functional differences of SMC hinge domain between condensins and cohesin in DNA recognition.
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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.