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. Morrice, L. R. Saunders, G. N. Barber, F. V. Fuller-Pace

    Research output: Contribution to journalArticlepeer-review

    67 Citations (Scopus)

    Abstract

    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.
    Original languageEnglish
    Pages (from-to)1470-1480
    Number of pages11
    JournalNucleic Acids Research
    Volume31
    Issue number5
    DOIs
    Publication statusPublished - Mar 2003

    Keywords

    • Adenosine triphosphatases metabolism
    • Phosphoproteins
    • Protein kinases metabolism
    • RNA helicases metabolism
    • DEAD box protein
    • p68
    • p72

    Fingerprint Dive into the research topics of 'The highly related DEAD box RNA helicases p68 and p72 exist as heterodimers in cells'. Together they form a unique fingerprint.

    Cite this