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Nucleic Acids Research Advance Access originally published online on October 2, 2007
Nucleic Acids Research 2007 35(19):6648-6662; doi:10.1093/nar/gkm739
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Nucleic Acids Research, 2007, Vol. 35, No. 19 6648-6662
© 2007 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.

Molecular Biology

The ePHD protein SPBP interacts with TopBP1 and together they co-operate to stimulate Ets1-mediated transcription

Eva Sjøttem2, Cecilie Rekdal1, Gunbjørg Svineng1, Sylvia Sagen Johnsen2, Helle Klenow2, Rebecca Dale Uglehus1 and Terje Johansen1,*

1Biochemistry Department and 2Department of Molecular Biotechnology, Institute of Medical Biology, University of Tromsø, 9037 Tromsø, Norway

*To whom correspondence should be addressed. Tel: +47 776 44720; Fax: +47 776 45350; Email: terjej{at}fagmed.uit.no

Received April 23, 2007. Revised September 6, 2007. Accepted September 6, 2007.

SPBP (Stromelysin-1 PDGF responsive element binding protein) is a ubiquitously expressed 220 kDa nuclear protein shown to enhance or repress the transcriptional activity of various transcription factors. A yeast two-hybrid screen, with the extended plant homeodomain (ePHD) of SPBP as bait, identified TopBP1 (topoisomerase II ß-binding protein 1) as a candidate interaction partner of SPBP. TopBP1 has eight BRCA1 carboxy-terminal (BRCT) domains and is involved in DNA replication, DNA damage responses and in the regulation of gene expression. The interaction between SPBP and TopBP1 was confirmed in vitro and in vivo, and was found to be mediated by the ePHD domain of SPBP and the BRCT6 domain of TopBP1. Both SPBP and TopBP1 enhanced the transcriptional activity of Ets1 on the c-myc P1P2- and matrix metalloproteinase-3 (MMP3) promoters. Together they displayed a more than additive effect. Both proteins were associated with these promoters. The involvement of TopBP1 was dependent on the serine 1159 phosphorylation site, known to be important for transcriptional activation. Depletion of endogenous SPBP by siRNA treatment reduced MMP3 secretion by 50% in phorbol ester-stimulated human fibroblasts. Taken together, our results show that TopBP1 and SPBP interact physically and functionally to co-operate as co-activators of Ets1.


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