A novel zinc finger protein is associated with U7 snRNP and interacts with the stem–loop binding protein in the histone pre-mRNP to stimulate 3′-end processing

  1. Zbigniew Dominski,
  2. Judith A. Erkmann,
  3. Xiaocui Yang,
  4. Ricardo Sànchez, and
  5. William F. Marzluff1
  1. Department of Biochemistry and Biophysics, Program in Molecular Biology and Biotechnology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA

Abstract

The stem–loop binding protein (SLBP) is the posttranscriptional regulator of histone mRNA in metazoan cells. SLBP binds histone pre-mRNAs and facilitates 3′-end processing by promoting stable association of U7 snRNP with the pre-mRNA. To identify other factors involved in histone pre-mRNA processing, we used a modified yeast two-hybrid assay in which SLBP and its RNA target were coexpressed as bait. A novel zinc finger protein, hZFP100, which interacts with the SLBP/RNA complex but not with free SLBP, was cloned. The interaction requires regions of SLBP that are important for histone pre-mRNA processing. Antibodies to hZFP100 precipitate U7 snRNA, and expression of hZFP100 in Xenopus oocytes stimulates processing of histone pre-mRNA, showing that hZFP100 is a component of the processing machinery.

Keywords

Footnotes

  • 1 Corresponding author.

  • E-MAIL marzluff{at}med.unc.edu; FAX (919) 966-6821.

  • Article and publication are at http://www.genesdev.org/cgi/doi/10.1101/gad.932302.

    • Received July 30, 2001.
    • Accepted November 7, 2001.
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