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    Biochem Biophys Res Commun. 1997 May 19;234(2):335-40.

    Cloning and characterization of Gu/RH-II binding protein.

    Valdez BC, Henning D, Perlaky L, Busch RK, Busch H.

    Source

    Department of Pharmacology, Baylor College of Medicine, Houston, Texas 77030, USA. bvaldez@bcm.tmc.edu

    Abstract

    Gu/RNA helicase II (Gu/RH-II) is the first reported mammalian nucleolar RNA helicase that is a member of the D-E-A-D (Asp-Glu-Ala-Asp) box family of proteins. It has an ATP-dependent RNA unwinding (helicase) activity and a separate RNA folding activity (introduction of intramolecular secondary structure into single-stranded RNA). To determine which proteins may bind to Gu/RH-II, a yeast two-hybrid system was used. A cDNA which encoded a protein, called Gu/RH-II binding protein or GBP, was isolated and sequenced. The GBP protein is localized to the nucleus in speckled or diffuse nucleoplasmic patterns. The GBP mRNA level is highest in testis, 9- to 49-fold greater than other tissues. When GBP interacts with Gu/RH-II, proteolytic cleavage of Gu/RH-II occurs; the amino-terminal portion of Gu/RH-II is critical for this proteolysis.

    PMID:
    9177271
    [PubMed - indexed for MEDLINE]

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