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PMID: 15728351 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Fast, long-range, reversible conformational fluctuations in nucleosomes revealed by single-pair fluorescence resonance energy transfer.

Tomschik M, Zheng H, van Holde K, Zlatanova J, Leuba SH

Abstract

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.

MeSH Terms
Base Sequence DNA/chemistry Fluorescence Resonance Energy Transfer Microscopy, Fluorescence Molecular Sequence Data Nucleosomes/chemistry Protein Conformation
Chemicals
Nucleosomes DNA
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Tomschik Miroslav
Department of Cell Biology and Physiology, Hillman Cancer Center, University of Pittsburgh Cancer Institute, University of Pittsburgh School of Medicine, Pittsburgh, PA 15213, USA.
Zheng Haocheng
van Holde Ken
Zlatanova Jordanka
Leuba Sanford H
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
2005-03-01
Epub
2005-00-22
Pages
3278-83
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC549292
Subset
IM
Corrections
ErratumIn
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