Current Genetics

, Volume 37, Issue 6, pp 356–363

Phosphorylation is required for high-affinity binding of DBP, a yeast mitochondrial site-specific RNA binding protein

Authors

  • Huilin Li
    • Department of Molecular Biology and Pharmacology, Washington University School of Medicine, St. Louis, MO 63110
  • H. Peter Zassenhaus
    • Department of Molecular Microbiology and Immunology, St. Louis University Health Sciences Center, St. Louis, MO 63104 e-mail: zassenp@slu.edu Tel.: (314) 577-8443; Fax: (314) 773-3403
ORIGINAL PAPER

DOI: 10.1007/s002940000117

Cite this article as:
Li, H. & Zassenhaus, H. Curr Genet (2000) 37: 356. doi:10.1007/s002940000117

Abstract

All yeast mitochondrial mRNAs terminate at their 3′ ends with a conserved dodecamer sequence, a site for high-affinity binding by DBP (dodecamer binding protein). Using purified DBP, we show that binding requires an intact dodecamer site and is enhanced by the presence in an oligonucleotide of the immediate 4–5 upstream nucleotides. Binding affinity varied from 0.25 to 0.85 nM towards a set of RNA oligonucleotides containing messenger specific upstream sequences in addition to the dodecamer site. Furthermore, we show that phosphatase treatment of DBP abolishes its specific binding, indicating the involvement of reversible phosphorylation in the regulation of its binding activities. This finding will further our understanding of the mechanism of DBP in the regulation of RNA metabolism in yeast mitochondria.

Key words Dodecamer sequenceRNA binding proteinPhosphorylation

Copyright information

© Springer-Verlag Berlin Heidelberg 2000