Journal
BIOCHEMICAL JOURNAL
Volume 417, Issue -, Pages 121-132Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20080872
Keywords
co-repressor; Groucho; haematopoiesis; haematopoietically expressed homeobox (Hex); nuclear retention; proline-rich homeodomain (PRH); transcriptional repression; transdominant negative; transducin-like enhancer (TLE)
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Funding
- Wellcome Trust [WT0765271]
- Biotechnology and Biological Sciences Research Council [BB/D005094/1]
- BBSRC [BB/D005094/1] Funding Source: UKRI
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The PRH (proline-rich homeodomain) [also known as Hex (haematopoietically expressed homeobox)] protein is a transcription factor that functions as an important regulator of vertebrate development and many other processes in the adult including haematopoiesis. The Groucho/TLE (transducin-like enhancer) family of co-repressor proteins also regulate development and modulate the activity of many DNA-binding transcription factors during a range of diverse cellular processes including haematopoiesis. We have shown previously that PRH is it repressor of transcription in haematopoietic cells and that an Eh-1 (Engrailed homology) motif present within the N-terminal transcription repression domain of PRH mediates binding to Groucho/TLE proteins and enables co-repression. In the Present Study we demonstrate that PRH regulates the nuclear retention of TLE proteins during cellular fractionation. We show that transcriptional repression and the nuclear retention of TLE proteins requires PRH to bind to both TLE and DNA. In addition, we characterize a trans-dominant-negative PRH protein that inhibits wild-type PRH activity by sequestering TLE proteins to specific subnuclear C, domains. These results demonstrate that transcriptional repression by PRH is dependent oil TLE availability and suggest that subnuclear localization of TLE plays an important role in transcriptional repression by PRH.
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