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

Abdenour Soufi, Anyaporn Sawasdichai, Anshuman Shukla, Peter Noy, Timothy R Dafforn, Corinne J I Smith, Padma-Sheela Jayaraman, Kevin Gaston

Research output: Contribution to journalArticle (Academic Journal)peer-review

4 Citations (Scopus)
249 Downloads (Pure)

Abstract

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.
Translated title of the contributionThe DNA compaction by the higher-order assembly of PRH/Hex homeodomain protein oligomers
Original languageEnglish
Pages (from-to)7513-7525
Number of pages13
JournalNucleic Acids Research
Volume38
Issue number21
Early online date31 Jul 2010
DOIs
Publication statusPublished - 21 Nov 2010

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