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TitleHuman Condensin I and II Drive Extensive ATP-Dependent Compaction of Nucleosome-Bound DNA.
Journal, issue, pagesMol Cell, Vol. 79, Issue 1, Page 99-114.e9, Year 2020
Publish dateJul 2, 2020
AuthorsMuwen Kong / Erin E Cutts / Dongqing Pan / Fabienne Beuron / Thangavelu Kaliyappan / Chaoyou Xue / Edward P Morris / Andrea Musacchio / Alessandro Vannini / Eric C Greene /
PubMed AbstractStructural 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 ...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.
External linksMol Cell / PubMed:32445620 / PubMed Central
MethodsEM (single particle)
Resolution20.5 - 31.8 Å
Structure data

EMDB-10827:
Negative stain reconstruction of grafix crosslink human condensin I in the presence of ATPyS
Method: EM (single particle) / Resolution: 31.8 Å

EMDB-10833:
Negative stain reconstruction of grafix crosslink human condensin II in the presence of ATPyS
Method: EM (single particle) / Resolution: 20.5 Å

Source
  • Homo sapiens (human)

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