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Mechanical unfolding of nanoscale DNA-histone complex, using an atomic force microscope, shows a stepwise disassembly of histones from the nucleosome. A quantitative analysis of the rupture jump statistics and the length released per jump reveals insights into the possible histone contacts within the octamer complex. The measured ruptures correlate with the breakage of multiple contacts that stabilize the histone octamer. These results provide a mechanistic basis by which stepwise disassembly of histone proteins may result from an external force exerted by the adenosinetriphosphate (ATP) dependent chromatin remodeling machines to access regulatory sites on DNA.
Published in:
Applied Physics Letters
(Volume:90
,
Issue:
16
)
Date of Publication: Apr 2007
- Page(s):
- 163904 - 163904-3
- ISSN :
- 0003-6951
- Digital Object Identifier :
- 10.1063/1.2728031
- Product Type:
- Journals & Magazines
- Date of Current Version :
- 18 June 2009
- Issue Date :
- Apr 2007
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