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  • Human Condensin I and II Drive Extensive ATP-Dependent Compaction of Nucleosome-Bound DNA

Human Condensin I and II Drive Extensive ATP-Dependent Compaction of Nucleosome-Bound DNA

Autori:

  • Kong M.,
  • Cutts E. E.,
  • Pan D.,
  • Beuron F.,
  • Kaliyappan T.,
  • Xue C.,
  • Morris E. P.,
  • Musacchio A.,
  • Vannini A.,
  • Greene E. C.

Sommario:

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.

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