Publikation: RNA helicase activity associated with the human p68 protein
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It has been proposed that p68, a nuclear protein of relative molecular mass 68,000, functions in the regulation of cell growth and division. A complementary DNA analysis of the protein 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. The protein products of the new gene family have several motifs in common which are thought to be involved in nucleic acid unwinding. As yet, however, only elF-4A, through its effect on RNA, has been shown to possess unwinding activity. 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 antigen, the transforming protein of a small DNA tumour virus. Surprisingly, T antigen also has an RNA-unwinding activity: the homology between the two polypeptides, although confined to only a small region resembling the epitope of the cross-reacting antibody (PAb204), 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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HIRLING, Harald, Martin SCHEFFNER, Tobias RESTLE, Hans STAHL, 1989. RNA helicase activity associated with the human p68 protein. In: Nature. 1989, 339, pp. 562-564. ISSN 0028-0836. eISSN 1476-4687. Available under: doi: 10.1038/339562a0BibTex
@article{Hirling1989helic-42775, year={1989}, doi={10.1038/339562a0}, title={RNA helicase activity associated with the human p68 protein}, volume={339}, issn={0028-0836}, journal={Nature}, pages={562--564}, author={Hirling, Harald and Scheffner, Martin and Restle, Tobias and Stahl, Hans} }
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