Fast, Long-Range, Reversible Conformational Fluctuations in Nucleosomes Revealed by Single-Pair Fluorescence Resonance Energy Transfer
The nucleosome core particle, the basic repeated structure in chromatin fibers, consists of an octamer of eight core histone molecules, organized as dimers (H2A/H2B) and tetramers [( H3/ H4)2] around which DNA wraps tightly in almost two left-handed turns. The nucleosome has to undergo certain confo...
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Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 102; no. 9; pp. 3278 - 3283 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
United States
National Academy of Sciences
01.03.2005
National Acad Sciences |
Subjects | |
Online Access | Get full text |
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Summary: | The nucleosome core particle, the basic repeated structure in chromatin fibers, consists of an octamer of eight core histone molecules, organized as dimers (H2A/H2B) and tetramers [( H3/ H4)2] around which DNA wraps tightly in almost two left-handed turns. The nucleosome has to undergo certain conformational changes to allow processes that need access to the DNA template to occur. By single-pair fluorescence resonance energy transfer, we demonstrate fast, long-range, reversible conformational fluctuations in nucleosomes between two states: fully folded (closed), with the DNA wrapped around the histone core, or open, with the DNA significantly unraveled from the histone octamer. The brief excursions into an extended open state may create windows of opportunity for protein factors involved in DNA transactions to bind to or translocate along the DNA. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 To whom correspondence may be addressed. E-mail: leuba@pitt.edu or jordanka@uwyo.edu. Contributed by Ken van Holde, January 18, 2005 |
ISSN: | 0027-8424 1091-6490 |
DOI: | 10.1073/pnas.0500189102 |