Nucleic Acids Research, Vol 25, Issue 4 735-742, Copyright © 1997 by Oxford University Press
E Chernokalskaya, R Dompenciel and DR Schoenberg
Previous work from this laboratory [Dompenciel,R.E., Garnepudi,V.R. and
Schoenberg,D.R. (1995)J. Biol. Chem.270, 6108-6118] described the
purification and properties of an estrogen-regulated endonuclease isolated
from Xenopus liver polysomes that is involved in the destabilization of
albumin mRNA. The present study mapped cleavages made by this enzyme onto
the secondary structure of the portion of albumin mRNA bearing the major
cleavage sites. The predominant cleavages occur in the overlapping APyrUGA
sequence AUUGACUGA present in a single-stranded loop region, and in AUUGA
located within a bulged AU-rich stem. A structural mutation which converted
the major loop cleavage site to a hairpin bearing one APyrUGA element
eliminated cleavage at the intact site. This confirms that the polysomal
RNase is specific for single-stranded RNA. Additional point mutations in
the major loop characterized the nucleoside sequence requirements for
cleavage. Finally, snake venom exonuclease was used to demonstrate the
polysomal RNase generates products with a 3' hydroxyl. Binding of an
estrogen-induced protein to a portion of the 3'UTR of vitellogenin mRNA may
be involved in its stabilization by estrogen [Dodson,R.E. and Shapiro,D.J.
(1994)Mol. Cell. Biol.14, 3130-3138]. The core binding site for this
protein bears the sequence APyrUGA, suggesting that stabilization may be
accomplished by occlusion of a cleavage site for the polysomal RNase.
ARTICLES
Cleavage properties of an estrogen-regulated polysomal ribonuclease involved in the destabilization of albumin mRNA
Department of Pharmacology, Ohio State University College of Medicine, Columbus, OH 43210-1239, USA.
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