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Oligomerisation of the developmental regulator proline rich homeodomain (PRH/Hex) is mediated by a novel proline-rich dimerisation domain
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UNSPECIFIED (2006) Oligomerisation of the developmental regulator proline rich homeodomain (PRH/Hex) is mediated by a novel proline-rich dimerisation domain. Journal of Molecular Biology, 358 (4). pp. 943-962. doi:10.1016/j.jmb.2006.02.020 ISSN 0022-2836.
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Official URL: http://dx.doi.org/10.1016/j.jmb.2006.02.020
Abstract
Homeodomain proteins regulate multiple developmental pathways by altering gene expression temporally and in a tissue-specific fashion. The Proline Rich Homeodomain protein (PRH/Hex) is a transcription factor and an essential regulator of embryonic development and haematopoiesis. Recent discoveries have implicated self-association as an important feature of transcription factor function. Here, we show using a variety of techniques including gel-filtration, analytical ultracentrifugation, electron microscopy and in vitro cross-linking, that purified recombinant PRH is oligomeric and we use in vivo cross-linking to confirm that this protein exists as oligomers in cells. This is the first demonstration that a homeodomain protein can oligomerise in vivo. Consistent with these findings we show that a fraction of endogenous and exogenous PRH appears as discrete foci within the nucleus and at the nuclear periphery. The N-terminal domain of PRH is involved in the regulation of cell proliferation and transcriptional repression and can make multiple protein-protein interactions. We show that this region of PRH contains a novel proline-rich dimerisation domain that mediates oligomerisation. We propose a model that explains how PRH forms oligomers and we discuss how these oligomers might control transcription. (c) 2006 Elsevier Ltd. All rights reserved.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QD Chemistry | ||||
Journal or Publication Title: | Journal of Molecular Biology | ||||
Publisher: | ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD | ||||
ISSN: | 0022-2836 | ||||
Official Date: | 12 May 2006 | ||||
Dates: |
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Volume: | 358 | ||||
Number: | 4 | ||||
Number of Pages: | 20 | ||||
Page Range: | pp. 943-962 | ||||
DOI: | 10.1016/j.jmb.2006.02.020 | ||||
Publication Status: | Published |
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