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Nucleic Acids Research Advance Access originally published online on March 13, 2007
Nucleic Acids Research 2007 35(7):2167-2176; doi:10.1093/nar/gkm084
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Nucleic Acids Research, 2007, Vol. 35, No. 7 2167-2176
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

RNA

ElrA binding to the 3'UTR of cyclin E1 mRNA requires polyadenylation elements

Michael K. Slevin1, Francoise Gourronc2 and Rebecca S. Hartley3,*

1Molecular and Cellular Biology Program, University of Iowa, Iowa City, IA 52242, USA 2Department of Anatomy and Cell Biology, University of Iowa, Iowa City, IA 52242, USA and 3Department of Cell Biology and Physiology, University of New Mexico, Albuquerque, NM 87131, USA

*To whom correspondence should be addressed. Tel: +505-272-4009; Fax: +505-272-9105; Email: rhartley{at}salud.unm.edu

Received November 16, 2006. Revised January 29, 2007. Accepted January 30, 2007.

The early cell divisions of Xenopus laevis and other metazoan embryos occur in the presence of constitutively high levels of the cell cycle regulator cyclin E1. Upon completion of the 12th cell division, a time at which many maternal proteins are downregulated by deadenylation and destabilization of their encoding mRNAs, maternal cyclin E1 protein is downregulated while its mRNA is polyadenylated and stable. We report here that stable polyadenylation of cyclin E1 mRNA requires three cis-acting elements in the 3' untranslated region; the nuclear polyadenylation sequence, a contiguous cytoplasmic polyadenylation element and an upstream AU-rich element. ElrA, the Xenopus homolog of HuR and a member of the ELAV gene family binds the cyclin E1 3'UTR with high affinity. Deletion of these elements dramatically reduces the affinity of ElrA for the cyclin E1 3'UTR, abolishes polyadenylation and destabilizes the mRNA. Together, these findings provide compelling evidence that ElrA functions in polyadenylation and stabilization of cyclin E1 mRNA via binding these elements.

Present address: Michael K. Slevin, Department of Cell Biology and Physiology, University of New Mexico, Albuquerque, NM 87131, USA


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