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Nucleic Acids Research, 2003, Vol. 31, No. 5 1470-1480
© 2003 Oxford University Press

The highly related DEAD box RNA helicases p68 and p72 exist as heterodimers in cells

V. C. Ogilvie, B. J. Wilson, S. M. Nicol, N. A. Morrice1, L. R. Saunders2, G. N. Barber2 and F. V. Fuller-Pace*

Department of Molecular and Cellular Pathology, University of Dundee, Ninewells Hospital and Medical School, Dundee DD1 9SY, UK, 1 MRC Protein Phosphorylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK and 2 Department of Microbiology and Immunology, Sylvester Comprehensive Cancer Center, University of Miami School of Medicine, Miami, FL 33136, USA

*To whom correspondence should be addressed. Tel: +44 1382 496370; Fax: +44 1382 633952; Email: f.v.fullerpace{at}dundee.ac.uk
Present address:
V. C. Ogilvie, Molecular Medicine Centre, University of Edinburgh, Western General Hospital, Edinburgh EH4 2XU, UK
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors

The RNA helicases p68 and p72 are highly related members of the DEAD box family of proteins, sharing 90% identity across the conserved core, and have been shown to be involved in both transcription and mRNA processing. We previously showed that these proteins co-localise in the nucleus of interphase cells. In this study we show that p68 and p72 can interact with each other and self-associate in the yeast two-hybrid system. Co-immunoprecipitation experiments confirmed that p68 and p72 can interact in the cell and indicated that these proteins preferentially exist as hetero-dimers. In addition, we show that p68 can interact with NFAR-2, a protein that is also thought to function in mRNA processing. Moreover, gel filtration analysis suggests that p68 and p72 can exist in a variety of complexes in the cell (ranging from ~150 to ~400 kDa in size), with a subset of p68 molecules being in very large complexes (>2 MDa). The potential to exist in different complexes that may contain p68 and/or p72, together with a range of other factors, would provide the potential for these proteins to interact with different RNA substrates and would be consistent with recent reports implying a wide range of functions for p68/p72.


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