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Human Condensin I and II Drive Extensive ATP-Dependent Compaction of Nucleosome-Bound DNA.
Kong, Muwen; Cutts, Erin E; Pan, Dongqing; Beuron, Fabienne; Kaliyappan, Thangavelu; Xue, Chaoyou; Morris, Edward P; Musacchio, Andrea; Vannini, Alessandro; Greene, Eric C.
Afiliación
  • Kong M; Department of Biochemistry and Molecular Biophysics, Columbia University Irving Medical Center, New York, NY 10032, USA.
  • Cutts EE; Division of Structural Biology, The Institute of Cancer Research, London SW7 3RP, UK.
  • Pan D; Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.
  • Beuron F; Division of Structural Biology, The Institute of Cancer Research, London SW7 3RP, UK.
  • Kaliyappan T; Division of Structural Biology, The Institute of Cancer Research, London SW7 3RP, UK.
  • Xue C; Department of Biochemistry and Molecular Biophysics, Columbia University Irving Medical Center, New York, NY 10032, USA.
  • Morris EP; Division of Structural Biology, The Institute of Cancer Research, London SW7 3RP, UK.
  • Musacchio A; Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.
  • Vannini A; Division of Structural Biology, The Institute of Cancer Research, London SW7 3RP, UK; Fondazione Human Technopole, Structural Biology Research Centre, 20157 Milan, Italy. Electronic address: alessandro.vannini@icr.ac.uk.
  • Greene EC; Department of Biochemistry and Molecular Biophysics, Columbia University Irving Medical Center, New York, NY 10032, USA. Electronic address: ecg2108@cumc.columbia.edu.
Mol Cell ; 79(1): 99-114.e9, 2020 07 02.
Article en En | MEDLINE | ID: mdl-32445620
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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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: ADN / Nucleosomas / Adenosina Trifosfato / Adenosina Trifosfatasas / Complejos Multiproteicos / Proteínas de Unión al ADN Límite: Humans Idioma: En Revista: Mol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2020 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: ADN / Nucleosomas / Adenosina Trifosfato / Adenosina Trifosfatasas / Complejos Multiproteicos / Proteínas de Unión al ADN Límite: Humans Idioma: En Revista: Mol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2020 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos