RNA helicase activity associated with the human p68 protein (original) (raw)

Nature volume 339, pages 562–564 (1989)Cite this article

Abstract

IT has been proposed that p68, a nuclear protein of relative molecular mass 68,000, functions in the regulation of cell growth and division1. A complementary DNA analysis of the protein2 has revealed extensive amino-acid sequence homology to the products of a set of genes recently identified in organisms as diverse as Escherichia coli and man, which include the eukaryotic translation initiation factor elF-4A (refs3–9). The protein products of the new gene family have several motifs in common which are thought to be involved in nucleic acid unwinding10–12. As yet, however, only elF-4A, through its effect on RNA, has been shown to possess unwinding activity13,14. Here we report that purified p68 also exhibits RNA-dependent ATPase activity and functions as an RNA helicase in vitro. The protein was first identified by its specific immunological cross reaction with the simian virus 40 large T antigen1, the transforming protein of a small DNA tumour virus15. Surprisingly, T antigen also has an RNA-unwinding activity16: the homology between the two polypeptides, although confined to only a small region resembling the epitope of the cross-reacting antibody (PAb204) (ref. 2), should therefore be of functional significance. Furthermore, the RNA-unwinding activity may be involved in the growth-regulating functions of both proteins.

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Authors and Affiliations

  1. Fakultät für Biologie, Universität Konstanz, D-7750, Konstanz, FRG
    H. Hirling, M. Scheffner, T. Restle & H. Stahl

Authors

  1. H. Hirling
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  2. M. Scheffner
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  3. T. Restle
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  4. H. Stahl
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Hirling, H., Scheffner, M., Restle, T. et al. RNA helicase activity associated with the human p68 protein.Nature 339, 562–564 (1989). https://doi.org/10.1038/339562a0

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