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Nucleic Acids Research Advance Access originally published online on March 5, 2009
Nucleic Acids Research 2009 37(8):2504-2513; doi:10.1093/nar/gkp114
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Nucleic Acids Research, 2009, Vol. 37, No. 8 2504-2513
© 2009 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Gene Regulation, Chromatin and Epigenetics

Mutations to the histone H3 {alpha}N region selectively alter the outcome of ATP-dependent nucleosome-remodelling reactions

Joanna Somers and Tom Owen-Hughes*

Wellcome Trust Centre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK

*To whom correspondence should be addressed. Tel: 01382 385796; Fax: 01382 388072; Email: t.a.owenhughes{at}dundee.ac.uk

Received November 4, 2008. Revised January 13, 2009. Accepted February 9, 2009.

Mutational analysis of the histone H3 N-terminal region has shown it to play an important role both in chromatin function in vivo and nucleosome dynamics in vitro. Here we use a library of mutations in the H3 N-terminal region to investigate the contribution of this region to the action of the ATP-dependent remodelling enzymes Chd1, RSC and SWI/SNF. All of the enzymes were affected differently by the mutations with Chd1 being affected the least and RSC being most sensitive. In addition to affecting the rate of remodelling by RSC, some mutations prevented RSC from moving nucleosomes to locations in which DNA was unravelled. These observations illustrate that the mechanisms by which different ATP-dependent remodelling enzymes act are sensitive to different features of nucleosome structure. They also show how alterations to histones can affect the products generated as a result of ATP-dependent remodelling reactions.


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