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DNA compaction by the higher-order assembly of PRH/Hex homeodomain protein oligomers

Soufi, A. and Sawasdichai, A. and Shukla, A. and Noy, P. and Dafforn, T. and Smith, C. and Jayaraman, P.-S. and Gaston, K. (2010) DNA compaction by the higher-order assembly of PRH/Hex homeodomain protein oligomers. Nucleic Acids Research, 38 (21). p. 7513. ISSN 0305-1048

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URL of Published Version: http://dx.doi.org/10.1093/nar/gkq659

Identification Number/DOI: doi:10.1093/nar/gkq659

Protein self-organization is essential for the establishment and maintenance of nuclear architecture and for the regulation of gene expression. We have shown previously that the Proline-Rich Homeodomain protein (PRH/Hex) self-assembles to form oligomeric complexes that bind to arrays of PRH binding sites with high affinity and specificity. We have also shown that many PRH target genes contain suitably spaced arrays of PRH sites that allow this protein to bind and regulate transcription. Here, we use analytical ultracentrifugation and electron microscopy to further characterize PRH oligomers. We use the same techniques to show that PRH oligomers bound to long DNA fragments self-associate to form highly ordered assemblies. Electron microscopy and linear dichroism reveal that PRH oligomers can form protein–DNA fibres and that PRH is able to compact DNA in the absence of other proteins. Finally, we show that DNA compaction is not sufficient for the repression of PRH target genes in cells. We conclude that DNA compaction is a consequence of the binding of large PRH oligomers to arrays of binding sites and that PRH is functionally and structurally related to the Lrp/AsnC family of proteins from bacteria and archaea, a group of proteins formerly thought to be without eukaryotic equivalents.

Type of Work:Article
Date:2010 (Publication)
School/Faculty:Colleges (2008 onwards) > College of Life & Environmental Sciences
Department:Institute of Biomedical Research
Subjects:R Medicine (General)
Institution:University of Birmingham
Copyright Holders:Oxford University Press
ID Code:587
Refereed:YES
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