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Nucleic Acids Research Advance Access published online on November 13, 2009
Nucleic Acids Research, doi:10.1093/nar/gkp1003
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© The Author(s) 2009. Published by Oxford University Press.
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Structural Biology

Probing the (H3-H4)2 histone tetramer structure using pulsed EPR spectroscopy combined with site-directed spin labelling

Andrew Bowman1, Richard Ward2, Hassane El-Mkami3, Tom Owen-Hughes1 and David G. Norman2,*

1Wellcome Trust Centre for Gene Regulation and Expression, 2Nucleic Acid Structure Research Group, College of Life Sciences, University of Dundee, Dundee DD1 5EH and 3School of Physics and Astronomy, University of St Andrews, St Andrews FE2 4KM, UK

*To whom correspondence should be addressed. Tel: +44 1382 384798; Fax: +44(0)1382 386373; Email: d.g.norman{at}dundee.ac.uk

Received August 25, 2009. Revised October 6, 2009. Accepted October 12, 2009.

The (H3-H4)2 histone tetramer forms the central core of nucleosomes and, as such, plays a prominent role in assembly, disassembly and positioning of nucleosomes. Despite its fundamental role in chromatin, the tetramer has received little structural investigation. Here, through the use of pulsed electron-electron double resonance spectroscopy coupled with site-directed spin labelling, we survey the structure of the tetramer in solution. We find that tetramer is structurally more heterogeneous on its own than when sequestered in the octamer or nucleosome. In particular, while the central region including the H3-H3' interface retains a structure similar to that observed in nucleosomes, other regions such as the H3 {alpha}N helix display increased structural heterogeneity. Flexibility of the H3 {alpha}N helix in the free tetramer also illustrates the potential for post-translational modifications to alter the structure of this region and mediate interactions with histone chaperones. The approach described here promises to prove a powerful system for investigating the structure of additional assemblies of histones with other important factors in chromatin assembly/fluidity.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.


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