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J. Biol. Chem., Vol. 279, Issue 47, 48950-48958, November 19, 2004

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Conservation of Bmp2 Post-transcriptional Regulatory Mechanisms^*

David T. Fritz, Donglin Liu, Junwang Xu, Shan Jiang, and Melissa B. Rogers

From the Department of Biochemistry and Molecular Biology, University of Medicine and Dentistry of New Jersey (UMDNJ)-NJ Medical School, Newark, New Jersey 07101

Bone morphogenetic protein (BMP) orthologs from diverse species like flies and humans are functionally interchangeable and play key roles in fundamental processes such as dorso-ventral axis formation in metazoans. Because both transcriptional and post-transcriptional mechanisms play central roles in modulating developmental protein levels, we have analyzed the 3'-untranslated region (3'UTR) of the Bmp 2 gene. This 3'UTR is unusually long and is alternatively polyadenylated. Mouse, human, and dog mRNAs are 83–87% identical within this region. A 265-nucleotide sequence, conserved between mammals, birds, frogs, and fish, is present in Bmp2 but not Bmp4. The ability of AmphiBMP2/4, a chordate ortholog to Bmp2 and Bmp4, to align with this sequence suggests that its function may have been lost in Bmp4. Activation of reporter genes by the conserved region acts by a post-transcriptional mechanism. Mouse, human, chick, and zebrafish Bmp2 synthetic RNAs decay rapidly in extracts from cells not expressing Bmp2. In contrast, these RNAs are relatively stable in extracts from Bmp2-expressing cells. Thus, Bmp2 RNA half-lives in vitro correlate with natural Bmp2 mRNA levels. The fact that non-murine RNAs interact appropriately with the mouse decay machinery suggests that the function of these cis-regulatory regions has been conserved for 450 million years since the fish and tetrapod lineages diverged. Overall, our results suggest that the Bmp2 3'UTR contains essential regulatory elements that act post-transcriptionally.

Received for publication, August 20, 2004 , and in revised form, September 9, 2004.

^* This work was supported in part by the Molecular Resource Facility at the University of Medicine and Dentistry of New Jersey Medical School, by NICHD Grant HD31117 from the National Institutes of Health, and by a grant from the Foundation of University of Medicine and Dentistry of New Jersey. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains Fig. S1.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY714781, AY722408, and AY722409.

To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology (MSB E627), University of Medicine and Dentistry of New Jersey Medical School, 185 South Orange Ave., P. O. Box 1709, Newark, NJ 07101-1709. Tel.: 973-972-2984; Fax: 973-972-5594; E-mail: rogersmb{at}umdnj.edu.

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