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 inProceedings of the National Academy of Sciences - PNAS Vol. 102; no. 9; pp. 3278 - 3283
Main Authors Tomschik, Miroslav, Zheng, Haocheng, van Holde, Ken, Zlatanova, Jordanka, Leuba, Sanford H.
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 01.03.2005
National Acad Sciences
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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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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