dc.contributor.author | Kong, M | |
dc.contributor.author | Cutts, EE | |
dc.contributor.author | Pan, D | |
dc.contributor.author | Beuron, F | |
dc.contributor.author | Kaliyappan, T | |
dc.contributor.author | Xue, C | |
dc.contributor.author | Morris, EP | |
dc.contributor.author | Musacchio, A | |
dc.contributor.author | Vannini, A | |
dc.contributor.author | Greene, EC | |
dc.date.accessioned | 2020-06-02T09:34:26Z | |
dc.date.issued | 2020-07-02 | |
dc.identifier.citation | Molecular cell, 2020, 79 (1), pp. 99 - 114.e9 | |
dc.identifier.issn | 1097-2765 | |
dc.identifier.uri | https://repository.icr.ac.uk/handle/internal/3668 | |
dc.identifier.eissn | 1097-4164 | |
dc.identifier.doi | 10.1016/j.molcel.2020.04.026 | |
dc.description.abstract | Structural maintenance of chromosomes (SMC) complexes are essential for genome organization from bacteria to humans, but their mechanisms of action remain poorly understood. Here, we characterize human SMC complexes condensin I and II and unveil the architecture of the human condensin II complex, revealing two putative DNA-entrapment sites. Using single-molecule imaging, we demonstrate that both condensin I and II exhibit ATP-dependent motor activity and promote extensive and reversible compaction of double-stranded DNA. Nucleosomes are incorporated into DNA loops during compaction without being displaced from the DNA, indicating that condensin complexes can readily act upon nucleosome-bound DNA molecules. These observations shed light on critical processes involved in genome organization in human cells. | |
dc.format | Print-Electronic | |
dc.format.extent | 99 - 114.e9 | |
dc.language | eng | |
dc.language.iso | eng | |
dc.publisher | CELL PRESS | |
dc.rights.uri | https://www.rioxx.net/licenses/all-rights-reserved | |
dc.subject | Nucleosomes | |
dc.subject | Humans | |
dc.subject | Multiprotein Complexes | |
dc.subject | DNA-Binding Proteins | |
dc.subject | DNA | |
dc.subject | Adenosine Triphosphate | |
dc.subject | Protein Conformation | |
dc.subject | Protein Binding | |
dc.subject | Models, Molecular | |
dc.subject | Adenosine Triphosphatases | |
dc.subject | Single Molecule Imaging | |
dc.title | Human Condensin I and II Drive Extensive ATP-Dependent Compaction of Nucleosome-Bound DNA. | |
dc.type | Journal Article | |
dcterms.dateAccepted | 2020-04-22 | |
rioxxterms.versionofrecord | 10.1016/j.molcel.2020.04.026 | |
rioxxterms.licenseref.uri | https://creativecommons.org/licenses/by/4.0 | |
rioxxterms.licenseref.startdate | 2020-07 | |
rioxxterms.type | Journal Article/Review | |
dc.relation.isPartOf | Molecular cell | |
pubs.issue | 1 | |
pubs.notes | No embargo | |
pubs.organisational-group | /ICR | |
pubs.organisational-group | /ICR/Primary Group | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Structural Biology | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Structural Biology/Structural Electron Microscopy | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Structural Biology/Vannini Group | |
pubs.organisational-group | /ICR | |
pubs.organisational-group | /ICR/Primary Group | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Structural Biology | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Structural Biology/Structural Electron Microscopy | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Structural Biology/Vannini Group | |
pubs.publication-status | Published | |
pubs.volume | 79 | |
pubs.embargo.terms | No embargo | |
icr.researchteam | Structural Electron Microscopy | |
icr.researchteam | Vannini Group | |
dc.contributor.icrauthor | Beuron, Fabienne | |
dc.contributor.icrauthor | Morris, Edward | |
dc.contributor.icrauthor | Vannini, Alessandro | |