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Originally published In Press as doi:10.1074/jbc.M007642200 on October 6, 2000

J. Biol. Chem., Vol. 275, Issue 49, 38286-38295, December 8, 2000
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Binding of an RNA Trafficking Response Element to Heterogeneous Nuclear Ribonucleoproteins A1 and A2*

Jianguo Shan, Kim Moran-Jones, Trent P. Munro, Grahame J. Kidd, Donald J. Winzor, Keith S. Hoek, and Ross SmithDagger

From the Biochemistry Department, The University of Queensland, Queensland 4072, Australia

Heterogeneous nuclear ribonucleoprotein (hnRNP) A2 binds a 21-nucleotide myelin basic protein mRNA response element, the A2RE, and A2RE-like sequences in other localized mRNAs, and is a trans-acting factor in oligodendrocyte cytoplasmic RNA trafficking. Recombinant human hnRNPs A1 and A2 were used in a biosensor to explore interactions with A2RE and the cognate oligodeoxyribonucleotide. Both proteins have a single site that bound oligonucleotides with markedly different sequences but did not bind in the presence of heparin. Both also possess a second, specific site that bound only A2RE and was unaffected by heparin. hnRNP A2 bound A2RE in the latter site with a Kd near 50 nM, whereas the Kd for hnRNP A1 was above 10 µM. UV cross-linking assays led to a similar conclusion. Mutant A2RE sequences, that in earlier qualitative studies appeared not to bind hnRNP A2 or support RNA trafficking in oligodendrocytes, had dissociation constants above 5 µM for this protein. The two concatenated RNA recognition motifs (RRMs), but not the individual RRMs, mimicked the binding behavior of hnRNP A2. These data highlight the specificity of the interaction of A2RE with these hnRNPs and suggest that the sequence-specific A2RE-binding site on hnRNP A2 is formed by both RRMs acting in cis.


* This work was supported by grants from the Australian National Health and Medical Research Council (to R. S.) and from the Australian Research Council (to R. S. and D. J. W.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Biochemistry Dept., University of Queensland, Qld 4072, Australia. Tel.: 61-7-3365-4627; Fax: 61-7-3365-4699; E-mail ross@biosci.uq.edu.au.


Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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